General Information of Drug Transporter (DT)
DT ID DTD0526 Transporter Info
Gene Name SCN1A
Transporter Name Voltage-gated sodium channel alpha Nav1.1
Gene ID
6323
UniProt ID
P35498
Post-Translational Modification of This DT
Overview ofSCN1A Modification Sites with Functional and Structural Information
Sequence
MEQTVLVPPG PDSFNFFTRE SLAAIERRIA EEKAKNPKPD KKDDDENGPK PNSDLEAGKN 
LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVLNKGKAIF RFSATSALYI LTPFNPLRKI 
AIKILVHSLF SMLIMCTILT NCVFMTMSNP PDWTKNVEYT FTGIYTFESL IKIIARGFCL 
EDFTFLRDPW NWLDFTVITF AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL 
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCIQW PPTNASLEEH SIEKNITVNY 
NGTLINETVF EFDWKSYIQD SRYHYFLEGF LDALLCGNSS DAGQCPEGYM CVKAGRNPNY 
GYTSFDTFSW AFLSLFRLMT QDFWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA 
VVAMAYEEQN QATLEEAEQK EAEFQQMIEQ LKKQQEAAQQ AATATASEHS REPSAAGRLS 
DSSSEASKLS SKSAKERRNR RKKRKQKEQS GGEEKDEDEF QKSESEDSIR RKGFRFSIEG 
NRLTYEKRYS SPHQSLLSIR GSLFSPRRNS RTSLFSFRGR AKDVGSENDF ADDEHSTFED 
NESRRDSLFV PRRHGERRNS NLSQTSRSSR MLAVFPANGK MHSTVDCNGV VSLVGGPSVP 
TSPVGQLLPE VIIDKPATDD NGTTTETEMR KRRSSSFHVS MDFLEDPSQR QRAMSIASIL 
TNTVEELEES RQKCPPCWYK FSNIFLIWDC SPYWLKVKHV VNLVVMDPFV DLAITICIVL 
NTLFMAMEHY PMTDHFNNVL TVGNLVFTGI FTAEMFLKII AMDPYYYFQE GWNIFDGFIV 
TLSLVELGLA NVEGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII 
VFIFAVVGMQ LFGKSYKDCV CKIASDCQLP RWHMNDFFHS FLIVFRVLCG EWIETMWDCM 
EVAGQAMCLT VFMMVMVIGN LVVLNLFLAL LLSSFSADNL AATDDDNEMN NLQIAVDRMH 
KGVAYVKRKI YEFIQQSFIR KQKILDEIKP LDDLNNKKDS CMSNHTAEIG KDLDYLKDVN 
GTTSGIGTGS SVEKYIIDES DYMSFINNPS LTVTVPIAVG ESDFENLNTE DFSSESDLEE 
SKEKLNESSS SSEGSTVDIG APVEEQPVVE PEETLEPEAC FTEGCVQRFK CCQINVEEGR 
GKQWWNLRRT CFRIVEHNWF ETFIVFMILL SSGALAFEDI YIDQRKTIKT MLEYADKVFT 
YIFILEMLLK WVAYGYQTYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG AIKSLRTLRA 
LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCINTT 
TGDRFDIEDV NNHTDCLKLI ERNETARWKN VKVNFDNVGF GYLSLLQVAT FKGWMDIMYA 
AVDSRNVELQ PKYEESLYMY LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM 
TEEQKKYYNA MKKLGSKKPQ KPIPRPGNKF QGMVFDFVTR QVFDISIMIL ICLNMVTMMV 
ETDDQSEYVT TILSRINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV VVILSIVGMF 
LAELIEKYFV SPTLFRVIRL ARIGRILRLI KGAKGIRTLL FALMMSLPAL FNIGLLLFLV 
MFIYAIFGMS NFAYVKREVG IDDMFNFETF GNSMICLFQI TTSAGWDGLL APILNSKPPD 
CDPNKVNPGS SVKGDCGNPS VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL 
SEDDFEMFYE VWEKFDPDAT QFMEFEKLSQ FAAALEPPLN LPQPNKLQLI AMDLPMVSGD 
RIHCLDILFA FTKRVLGESG EMDALRIQME ERFMASNPSK VSYQPITTTL KRKQEEVSAV 
IIQRAYRRHL LKRTVKQASF TYNKNKIKGG ANLLIKEDMI IDRINENSIT EKTDLTMSTA 
ACPPSYDRVT KPIVEKHEQE GKDEKAKGK
PTM type
X-Acetylation X-Methylation X-N-glycosylation X-Oxidation X-Phosphorylation X-Phosphorylation X-SUMOylation X-Ubiquitination X-Ubiquitination X: Amino Acid

Acetylation

  Lysine

          4 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [1]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1506

Experimental Method

Co-Immunoprecipitation

Detailed Description

Acetylation at SCN1A Lysine 1506 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [2]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1936

Experimental Method

Co-Immunoprecipitation

Detailed Description

Acetylation at SCN1A Lysine 1936 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [3]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1946

Experimental Method

Co-Immunoprecipitation

Detailed Description

Acetylation at SCN1A Lysine 1946 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [4]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1948

Experimental Method

Co-Immunoprecipitation

Detailed Description

Acetylation at SCN1A Lysine 1948 has the potential to affect its expression or activity.

Methylation

  Arginine

          3 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Arginine

Modified Location

563

Related Enzyme

Protein arginine N-methyltransferase 1 (PRMT1)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Methylation at SCN1A Arginine 563 have been reported to have the potential to influence its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Arginine

Modified Location

570

Related Enzyme

Protein arginine N-methyltransferase 1 (PRMT1)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Methylation at SCN1A Arginine 570 have been reported to have the potential to influence its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Arginine

Modified Location

574

Related Enzyme

Protein arginine N-methyltransferase 1 (PRMT1)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Methylation at SCN1A Arginine 574 have been reported to have the potential to influence its expression or activity.

N-glycosylation

  Asparagine

          9 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

211

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 211 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

284

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 284 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

295

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 295 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

301

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 301 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

306

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 306 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

338

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 338 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

1378

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 1378 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

1392

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 1392 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SCN1A [6]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

1403

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SCN1A Asparagine 1403 has the potential to affect its expression or activity.

Oxidation

  Cystine

          2 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [7]

Role of PTM

Potential impacts

Modified Residue

Cystine

Modified Location

179

Experimental Method

Co-Immunoprecipitation

Detailed Description

Oxidation at SCN1A Cystine 179 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [7]

Role of PTM

Potential impacts

Modified Residue

Cystine

Modified Location

1982

Experimental Method

Co-Immunoprecipitation

Detailed Description

Oxidation at SCN1A Cystine 1982 has the potential to affect its expression or activity.

Phosphorylation

  Arginine

          2 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [8]

Role of PTM

Potential impacts

Modified Residue

Arginine

Modified Location

693

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Arginine 693 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [8]

Role of PTM

Potential impacts

Modified Residue

Arginine

Modified Location

710

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Arginine 710 has the potential to affect its expression or activity.

  Serine

        33 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Slowing the inactivation of sodium channels and reducing peak sodium currents [9]

Role of PTM

Protein Activity Modulation

Modified Residue

Serine

Modified Location

1516

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1516 have been reported to slow the inactivation of sodium channels and reducing peak sodium currents.

  PTM Phenomenon2

Have the potential to influence SCN1A [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

169

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 169 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

316

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 316 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

321

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 321 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SCN1A [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

374

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 374 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SCN1A [12]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

474

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 474 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SCN1A [13], [14]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

480

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 480 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SCN1A [13]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

482

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 482 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SCN1A [13]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

483

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 483 has the potential to affect its expression or activity.

  PTM Phenomenon10

Have the potential to influence SCN1A [15]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

487

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 487 has the potential to affect its expression or activity.

  PTM Phenomenon11

Have the potential to influence SCN1A [15]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

490

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 490 has the potential to affect its expression or activity.

  PTM Phenomenon12

Have the potential to influence SCN1A [15]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

491

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 491 has the potential to affect its expression or activity.

  PTM Phenomenon13

Have the potential to influence SCN1A [14]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

510

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 510 has the potential to affect its expression or activity.

  PTM Phenomenon14

Have the potential to influence SCN1A [14]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

523

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 523 has the potential to affect its expression or activity.

  PTM Phenomenon15

. [16]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

525

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 525 has the potential to affect its expression or activity.

  PTM Phenomenon16

. [17]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

525

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 525 has the potential to affect its expression or activity.

  PTM Phenomenon17

. [17]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

528

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 528 has the potential to affect its expression or activity.

  PTM Phenomenon18

Have the potential to influence SCN1A [14], [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

550

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 550 has the potential to affect its expression or activity.

  PTM Phenomenon19

Have the potential to influence SCN1A [18], [19]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

551

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 551 has the potential to affect its expression or activity.

  PTM Phenomenon20

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

555

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 555 has the potential to affect its expression or activity.

  PTM Phenomenon21

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

558

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 558 has the potential to affect its expression or activity.

  PTM Phenomenon22

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

562

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 562 has the potential to affect its expression or activity.

  PTM Phenomenon23

Have the potential to influence SCN1A [8], [19]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

565

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 565 has the potential to affect its expression or activity.

  PTM Phenomenon24

Have the potential to influence SCN1A [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

576

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 576 has the potential to affect its expression or activity.

  PTM Phenomenon25

. [16]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

607

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 607 has the potential to affect its expression or activity.

  PTM Phenomenon26

Have the potential to influence SCN1A [20], [21]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

718

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 718 has the potential to affect its expression or activity.

  PTM Phenomenon27

. [16]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

730

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 730 has the potential to affect its expression or activity.

  PTM Phenomenon28

Have the potential to influence SCN1A [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

856

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 856 has the potential to affect its expression or activity.

  PTM Phenomenon29

Have the potential to influence SCN1A [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

1037

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1037 has the potential to affect its expression or activity.

  PTM Phenomenon30

. [17]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

1063

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1063 has the potential to affect its expression or activity.

  PTM Phenomenon31

Have the potential to influence SCN1A [22]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

1566

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1566 has the potential to affect its expression or activity.

  PTM Phenomenon32

Have the potential to influence SCN1A [23]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

1631

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1631 has the potential to affect its expression or activity.

  PTM Phenomenon33

Have the potential to influence SCN1A [24]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

1918

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Serine 1918 has the potential to affect its expression or activity.

  Threonine

        18 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

297

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 297 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

303

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 303 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

308

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 308 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

544

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 544 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SCN1A [8], [20]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

721

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 721 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SCN1A [20], [21]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

723

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 723 has the potential to affect its expression or activity.

  PTM Phenomenon7

. [17]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1066

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1066 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SCN1A [22]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1562

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1562 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SCN1A [23]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1633

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1633 has the potential to affect its expression or activity.

  PTM Phenomenon10

. [17]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1908

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1908 has the potential to affect its expression or activity.

  PTM Phenomenon11

. [17]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1909

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1909 has the potential to affect its expression or activity.

  PTM Phenomenon12

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1909

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1909 has the potential to affect its expression or activity.

  PTM Phenomenon13

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1909

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1909 has the potential to affect its expression or activity.

  PTM Phenomenon14

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1934

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1934 has the potential to affect its expression or activity.

  PTM Phenomenon15

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1934

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1934 has the potential to affect its expression or activity.

  PTM Phenomenon16

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1934

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1934 has the potential to affect its expression or activity.

  PTM Phenomenon17

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1934

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1934 has the potential to affect its expression or activity.

  PTM Phenomenon18

. [25]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

1934

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Threonine 1934 has the potential to affect its expression or activity.

  Tyrosine

        16 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Increasing SCN1A expression at the cell surface [5]

Role of PTM

Surface Expression Modulation

Affected Drug/Substrate

Sodium

Results for Drug

Increasing the transport of sodium

Modified Residue

Tyrosine

Modified Location

1495

Related Enzyme

Tyrosine-protein kinase Fyn (FYN)

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1495 have been reported to increase its expression at the cell surface.

  PTM Phenomenon2

Impairing the function of SCN1A [5]

Role of PTM

Trafficking to Plasma Membrane

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Tyrosine

Modified Location

1498

Related Enzyme

Tyrosine-protein kinase Fyn (FYN)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1498 have been reported to impaire its transport function.

  PTM Phenomenon3

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Tyrosine

Modified Location

66

Related Enzyme

Tyrosine-protein kinase Fyn (FYN)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 66 have been reported to have the potential to influence its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

300

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 300 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SCN1A [11]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

317

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 317 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

545

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 545 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SCN1A [18]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

549

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 549 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Tyrosine

Modified Location

1497

Related Enzyme

Tyrosine-protein kinase Fyn (FYN)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1497 have been reported to have the potential to influence its expression or activity.

  PTM Phenomenon9

Have the potential to influence SCN1A [26], [27]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1507

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1507 has the potential to affect its expression or activity.

  PTM Phenomenon10

Have the potential to influence SCN1A [26], [28]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1508

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1508 has the potential to affect its expression or activity.

  PTM Phenomenon11

. [17]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1684

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1684 has the potential to affect its expression or activity.

  PTM Phenomenon12

. [17]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1684

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1684 has the potential to affect its expression or activity.

  PTM Phenomenon13

. [17]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1684

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1684 has the potential to affect its expression or activity.

  PTM Phenomenon14

. [17]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1694

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1694 has the potential to affect its expression or activity.

  PTM Phenomenon15

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Affecting the inward transport of sodium

Modified Residue

Tyrosine

Modified Location

1893

Related Enzyme

Tyrosine-protein kinase Fyn (FYN)

Experimental Material(s)

Human embryonic kidney 293 (HEK293) cells

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1893 have been reported to have the potential to influence its expression or activity.

  PTM Phenomenon16

. [17]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

1926

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SCN1A Tyrosine 1926 has the potential to affect its expression or activity.

SUMOylation

  Lysine

          4 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

. [29]

Role of PTM

Protein Activity Modulation

Modified Residue

Lysine

Modified Location

167

Experimental Material(s)

E. coli BL21

Experimental Method

Co-Immunoprecipitation

Detailed Description

SUMOylation at SCN1A Lysine 167 have been reported to facilitated the formation of NAC1 nuclear bodies.

  PTM Phenomenon2

. [29]

Role of PTM

Protein Activity Modulation

Modified Residue

Lysine

Modified Location

318

Experimental Material(s)

E. coli BL21

Experimental Method

Co-Immunoprecipitation

Detailed Description

SUMOylation at SCN1A Lysine 318 have been reported to facilitated the formation of NAC1 nuclear bodies.

  PTM Phenomenon3

. [29]

Role of PTM

Protein Activity Modulation

Modified Residue

Lysine

Modified Location

368

Experimental Material(s)

E. coli BL21

Experimental Method

Co-Immunoprecipitation

Detailed Description

SUMOylation at SCN1A Lysine 368 have been reported to facilitated the formation of NAC1 nuclear bodies.

  PTM Phenomenon4

. [29]

Role of PTM

Protein Activity Modulation

Modified Residue

Lysine

Modified Location

498

Experimental Material(s)

E. coli BL21

Experimental Method

Co-Immunoprecipitation

Detailed Description

SUMOylation at SCN1A Lysine 498 have been reported to facilitated the formation of NAC1 nuclear bodies.

Ubiquitination

  Lysine

          6 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SCN1A [5]

Role of PTM

Potential impacts

Affected Drug/Substrate

Sodium

Results for Drug

Decreasing the transport of sodium

Modified Residue

Lysine

Related Enzyme

E3 ubiquitin-protein ligase NEDD4-like (NEDD4L)

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine have been reported to has the potential to affect its expression or activity.

  PTM Phenomenon2

. [17]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

88

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine 88 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SCN1A [30]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

225

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine 225 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SCN1A [31]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

453

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine 453 has the potential to affect its expression or activity.

  PTM Phenomenon5

. [17]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1512

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine 1512 has the potential to affect its expression or activity.

  PTM Phenomenon6

. [17]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

1512

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SCN1A Lysine 1512 has the potential to affect its expression or activity.
References
1 Noradrenaline-Specific, Efficient Visualization in Brain Tissue Triggered by Unique Cascade Nucleophilic Substitution. Anal Chem. 2019 Feb 5;91(3):2255-2259.
2 Syntheses, characterization, and ethylene polymerization of titanium and zirconium complexes with [N, O] ligands. Dalton Trans. 2009 Nov 7;(41):8838-45.
3 Vanadium-based imido-alkoxide pro-catalysts bearing bisphenolate ligands for ethylene and epsilon-caprolactone polymerisation. Dalton Trans. 2009 Nov 7;(41):8911-22.
4 Effects of veratridine on Na and Ca currents in frog skeletal muscle. Gen Pharmacol. 1994 Dec;25(8):1661-6.
5 An update on transcriptional and post-translational regulation of brain voltage-gated sodium channels. Amino Acids. 2016 Mar;48(3):641-651.
6 dbPTM in 2022: an updated database for exploring regulatory networks and functional associations of protein post-translational modifications. Nucleic Acids Res. 2022 Jan 7;50(D1):D471-D479. (ID: SCN1A_HUMAN)
7 A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
8 Global Landscape and Dynamics of Parkin and USP30-Dependent Ubiquitylomes in iNeurons during Mitophagic Signaling. Mol Cell. 2020 Mar 5;77(5):1124-1142.e10.
9 UniProt: the Universal Protein Knowledgebase in 2023. Nucleic Acids Res. 2023 Jan 6;51(D1):D523-D531. (ID: P35498)
10 Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics. 2014 Jul;13(7):1690-704.
11 An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
12 Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers. Anal Chem. 2014 Jul 1;86(13):6363-71.
13 Quantitative phosphoproteomic profiling of human non-small cell lung cancer tumors. J Proteomics. 2013 Oct 8;91:286-96.
14 Refined phosphopeptide enrichment by phosphate additive and the analysis of human brain phosphoproteome. Proteomics. 2015 Jan;15(2-3):500-7.
15 Quantitative global phosphoproteomics of human umbilical vein endothelial cells after activation of the Rap signaling pathway. Mol Biosyst. 2013 Apr 5;9(4):732-49.
16 BioMuta and BioXpress: mutation and expression knowledgebases for cancer biomarker discovery. Nucleic Acids Res. 2018;46(D1):D1128-D1136.
17 15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
18 An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
19 Quantitative phosphoproteomics of Alzheimer's disease reveals cross-talk between kinases and small heat shock proteins. Proteomics. 2015 Jan;15(2-3):508-519.
20 Phosphoproteomics reveals ALK promote cell progress via RAS/ JNK pathway in neuroblastoma. Oncotarget. 2016 Nov 15;7(46):75968-75980.
21 Triomics Analysis of Imatinib-Treated Myeloma Cells Connects Kinase Inhibition to RNA Processing and Decreased Lipid Biosynthesis. Anal Chem. 2015 Nov 3;87(21):10995-1006.
22 iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
23 Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
24 Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501.
25 ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
26 Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
27 Phosphoproteomics Analysis Identifies Novel Candidate Substrates of the Nonreceptor Tyrosine Kinase, S rc- r elated Kinase Lacking C-terminal Regulatory Tyrosine and N-terminal M yristoylation S ites (SRMS). Mol Cell Proteomics. 2018 May;17(5):925-947.
28 Modulation of the cardiac sodium channel NaV1.5 by Fyn, a Src family tyrosine kinase. Circ Res. 2005 May 13;96(9):991-8.
29 Multi-SUMOylation of NAC1 is essential for the growth of prostate cancer cells. Biochem Biophys Res Commun. 2023;641:148-154.
30 Highly Multiplexed Quantitative Mass Spectrometry Analysis of Ubiquitylomes. Cell Syst. 2016 Oct 26;3(4):395-403.e4.
31 Quantitative Analysis of the Brain Ubiquitylome in Alzheimer's Disease. Proteomics. 2018 Oct;18(20):e1800108.

If you find any error in data or bug in web service, please kindly report it to Dr. Li and Dr. Fu.