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Q9C0H9 (SRCN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SRC kinase signaling inhibitor 1
Alternative name(s):
SNAP-25-interacting protein
Short name=SNIP
p130Cas-associated protein
p140Cap
Gene names
Name:SRCIN1
Synonyms:KIAA1684, P140
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1055 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a negative regulator of SRC by activating CSK which inhibits SRC activity and downstream signaling, leading to impaired cell spreading and migration. Regulates dendritic spine morphology. Involved in calcium-dependent exocytosis. May play a role in neurotransmitter release or synapse maintenance. Ref.6 Ref.7 Ref.10

Subunit structure

Interacts with the N-terminal coiled-coil region of SNAP25 By similarity. Interacts with BCAR1/p130Cas and SRC through its C-terminal domain. Interacts with CSK, CTTN, SORBS3/vinexin, SYP and MAPRE3/EB3. Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Cell junctionsynapse By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Note: Localized to the perinuclear region, lamellopodia, cortical actin and actin stress fibers but not to focal adhesions. Strongly expressed in axons and dendrites of the CA1 and CA3 hippocampal regions and of the dentate gyrus. Detected in both presynapses and postsynapses and in postsynaptic density fractions. Ref.6 Ref.10

Tissue specificity

Expressed in some primary breast carcinomas where its presence is significantly associated with increased tumor size. Not detected in normal breast tissue. Ref.8

Post-translational modification

Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands. Ref.6

Sequence similarities

Belongs to the SRCIN1 family.

Ontologies

Keywords
   Biological processExocytosis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processexocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of cell migration

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of dendritic spine morphogenesis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from direct assay Ref.6. Source: MGI

axon

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6Ref.7. Source: IntAct

protein kinase binding

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C0H9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9C0H9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1012-1055: ATKPSKEMSGSNETSSPVSEKPSASRTSIPVLTSFGARNSSISF → V
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9C0H9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-566: Missing.
     782-823: AAERDWEEKR...LKAIPDLDCA → VLGPGIVGGA...FFLGGGGPVP
     824-1055: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9C0H9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: MRGAWVHLHS...SDSEGGVSFA → MGNAPSQDPE...SASQTKLRSP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10551055SRC kinase signaling inhibitor 1
PRO_0000072011

Regions

Region519 – 56951Interaction with SNAP25 By similarity
Coiled coil433 – 46028 Potential
Coiled coil521 – 54626 Potential
Coiled coil588 – 65063 Potential
Compositional bias343 – 37634Pro-rich
Compositional bias828 – 88659Pro-rich

Amino acid modifications

Modified residue1131Phosphotyrosine By similarity
Modified residue2151Phosphoserine By similarity
Modified residue2681Phosphotyrosine By similarity
Modified residue3941Phosphoserine By similarity
Modified residue7791Phosphoserine By similarity
Modified residue8591Phosphoserine By similarity
Modified residue9151Phosphoserine By similarity

Natural variations

Alternative sequence1 – 566566Missing in isoform 3.
VSP_009366
Alternative sequence1 – 5252MRGAW…GVSFA → MGNAPSQDPERSSPPMLSAD DAEYPREYRTLGGGGGGGSG GRRFSNVGLVHTSERRHTVI AAQSLEALSGLQKADADRKR DAFMDHLKSKYPQHALALRG QQDRMREQPNYWSFKTRSSR HTQGAQPGLADQAAKLSYAS AESLETMSEAELPLGFSRMN RFRQSLPLSRSASQTKLRSP in isoform 4.
VSP_039240
Alternative sequence782 – 82342AAERD…DLDCA → VLGPGIVGGAMSQVHTFLRP SFLEWGVPILWVFFLGGGGP VP in isoform 3.
VSP_009367
Alternative sequence824 – 1055232Missing in isoform 3.
VSP_009368
Alternative sequence1012 – 105544ATKPS…SSISF → V in isoform 2.
VSP_050630

Experimental info

Sequence conflict3141Missing AA sequence Ref.6
Sequence conflict4811T → I in BAC86634. Ref.2
Sequence conflict5921L → I AA sequence Ref.6
Sequence conflict7051V → M AA sequence Ref.6
Sequence conflict713 – 7142LS → IN AA sequence Ref.6
Sequence conflict8431H → E AA sequence Ref.6
Sequence conflict8501R → K AA sequence Ref.6
Sequence conflict8671Y → R AA sequence Ref.6
Sequence conflict9581I → L AA sequence Ref.6
Sequence conflict9871Q → P AA sequence Ref.6
Sequence conflict9941S → G AA sequence Ref.6
Isoform 4:
Sequence conflict1771L → P in BAD03968. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: CAB346DA20883EBD

FASTA1,055112,453
        10         20         30         40         50         60 
MRGAWVHLHS GAASSLRPCR CGAGAAPKSS PRSPGGRRGD GSSDSEGGVS FAGVLFLQFG 

        70         80         90        100        110        120 
EETRRVHITH EVSSLDTLHA LIAHMFPQKL TMGMLKSPNT AILIKDEARN VFYELEDVRD 

       130        140        150        160        170        180 
IQDRSIIKIY RKEPLYAAFP GSHLTNGDLR REMVYASRES SPTRRLNNLS PAPHLASGSP 

       190        200        210        220        230        240 
PPGLPSGLPS GLQSGSPSRS RLSYAGGRPP SYAGSPVHHA AERLGGAPAA QGVSPSPSAI 

       250        260        270        280        290        300 
LERRDVKPDE DLASKAGGMV LVKGEGLYAD PYGLLHEGRL SLAAAAGDPF AYPGAGGLYK 

       310        320        330        340        350        360 
RGSVRSLSTY SAAALQSDLE DSLYKAAGGG GPLYGDGYGF RLPPSSPQKL ADVAAPPGGP 

       370        380        390        400        410        420 
PPPHSPYSGP PSRGSPVRQS FRKDSGSSSV FAESPGGKTR SAGSASTAGA PPSELFPGPG 

       430        440        450        460        470        480 
ERSLVGFGPP VPAKDTETRE RMEAMEKQIA SLTGLVQSAL LRGSEPETPS EKIEGSNGAA 

       490        500        510        520        530        540 
TPSAPCGSGG RSSGATPVSG PPPPSASSTP AGQPTAVSRL QMQLHLRGLQ NSASDLRGQL 

       550        560        570        580        590        600 
QQLRKLQLQN QESVRALLKR TEAELSMRVS EAARRQEDPL QRQRTLVEEE RLRYLNDEEL 

       610        620        630        640        650        660 
ITQQLNDLEK SVEKIQRDVS HNHRLVPGPE LEEKALVLKQ LGETLTELKA HFPGLQSKMR 

       670        680        690        700        710        720 
VVLRVEVEAV KFLKEEPQRL DGLLKRCRGV TDTLAQIRRQ VDEGVWPPPN NLLSQSPKKV 

       730        740        750        760        770        780 
TAETDFNKSV DFEMPPPSPP LNLHELSGPA EGASLTPKGG NPTKGLDTPG KRSVDKAVSV 

       790        800        810        820        830        840 
EAAERDWEEK RAALTQYSAK DINRLLEETQ AELLKAIPDL DCASKAHPGP APTPDHKPPK 

       850        860        870        880        890        900 
APHGQKAAPR TEPSGRRGSD ELTVPRYRTE KPSKSPPPPP PRRSFPSSHG LTTTRTGEVV 

       910        920        930        940        950        960 
VTSKKDSAFI KKAESEELEV QKPQVKLRRA VSEVARPAST PPIMASAIKD EDDEDRIIAE 

       970        980        990       1000       1010       1020 
LESGGGSVPP MKVVTPGASR LKAAQGQAGS PDKSKHGKQR AEYMRIQAQQ QATKPSKEMS 

      1030       1040       1050 
GSNETSSPVS EKPSASRTSI PVLTSFGARN SSISF 

« Hide

Isoform 2 [UniParc].

Checksum: 140EEB2BFB499E47
Show »

FASTA1,012108,025
Isoform 3 [UniParc].

Checksum: FA12D8010D0C52D4
Show »

FASTA25728,590
Isoform 4 [UniParc].

Checksum: 52BF566E715EF6FF
Show »

FASTA1,183127,105

References

« Hide 'large scale' references
[1]"Homo sapiens cDNA, SNIP homolog."
Sugiyama A., Inoue H., Oka M.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Cerebellum.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Eye.
[5]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-1055 (ISOFORM 1).
Tissue: Brain.
[6]"p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading."
Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E., Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.
Mol. Biol. Cell 15:787-800(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 306-325; 492-519; 583-593; 611-617; 700-719; 841-867; 884-895; 957-972; 983-1000 AND 1006-1017 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCAR1, PHOSPHORYLATION.
[7]"p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity."
Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A., Piva R., Cavallo F., Forni G., Silengo L., Tarone G., Turco E., Defilippi P.
EMBO J. 26:2843-2855(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CSK AND SRC.
[8]"SNIP/p140Cap mRNA expression is an unfavourable prognostic factor in breast cancer and is not expressed in normal breast tissue."
Kennedy S., Clynes M., Doolan P., Mehta J.P., Rani S., Crown J., O'Driscoll L.
Br. J. Cancer 98:1641-1645(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex."
Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R., Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.
J. Neurochem. 107:61-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORBS3 AND SYP.
[10]"Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity."
Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S., Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J., Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.
Neuron 61:85-100(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTTN AND MAPRE3, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB127405 mRNA. Translation: BAD03968.1.
AK126665 mRNA. Translation: BAC86634.1.
AC115090 Genomic DNA. No translation available.
AC129916 Genomic DNA. No translation available.
BC033233 mRNA. Translation: AAH33233.1.
AB051471 mRNA. Translation: BAB21775.1.
CCDSCCDS45660.1. [Q9C0H9-5]
RefSeqNP_079524.2. NM_025248.2. [Q9C0H9-5]
UniGeneHs.448872.

3D structure databases

ProteinModelPortalQ9C0H9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123275. 7 interactions.
IntActQ9C0H9. 4 interactions.
MINTMINT-4777404.
STRING9606.ENSP00000264659.

Chemistry

ChEMBLCHEMBL2150836.

PTM databases

PhosphoSiteQ9C0H9.

Polymorphism databases

DMDM296452948.

Proteomic databases

MaxQBQ9C0H9.
PaxDbQ9C0H9.
PRIDEQ9C0H9.

Protocols and materials databases

DNASU80725.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264659; ENSP00000264659; ENSG00000017373. [Q9C0H9-5]
ENST00000570888; ENSP00000461232; ENSG00000262199. [Q9C0H9-5]
GeneID80725.
KEGGhsa:80725.
UCSCuc002hqd.3. human. [Q9C0H9-5]
uc002hqf.1. human. [Q9C0H9-2]
uc002hqg.3. human. [Q9C0H9-4]

Organism-specific databases

CTD80725.
GeneCardsGC17M036686.
H-InvDBHIX0021064.
HGNCHGNC:29506. SRCIN1.
HPAHPA009701.
MIM610786. gene.
neXtProtNX_Q9C0H9.
PharmGKBPA165432823.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69680.
HOGENOMHOG000293351.
HOVERGENHBG019587.
InParanoidQ9C0H9.
OMARESHHPP.
PhylomeDBQ9C0H9.
TreeFamTF332255.

Gene expression databases

ArrayExpressQ9C0H9.
BgeeQ9C0H9.
GenevestigatorQ9C0H9.

Family and domain databases

InterProIPR026727. Srcin1.
[Graphical view]
PANTHERPTHR22741:SF5. PTHR22741:SF5. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSRCIN1. human.
GenomeRNAi80725.
NextBio71035.
PROQ9C0H9.
SOURCESearch...

Entry information

Entry nameSRCN1_HUMAN
AccessionPrimary (citable) accession number: Q9C0H9
Secondary accession number(s): Q75T46, Q8N4W8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM