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Q9C0H9

- SRCN1_HUMAN

UniProt

Q9C0H9 - SRCN1_HUMAN

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Protein
SRC kinase signaling inhibitor 1
Gene
SRCIN1, KIAA1684, P140
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein kinase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. exocytosis Source: UniProtKB-KW
  2. negative regulation of cell adhesion Source: Ensembl
  3. negative regulation of protein secretion Source: Ensembl
  4. negative regulation of protein tyrosine kinase activity Source: UniProtKB
  5. positive regulation of protein tyrosine kinase activity Source: UniProtKB
  6. regulation of cell migration Source: UniProtKB
  7. regulation of dendritic spine morphogenesis Source: UniProtKB
  8. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
SRC kinase signaling inhibitor 1
Alternative name(s):
SNAP-25-interacting protein
Short name:
SNIP
p130Cas-associated protein
p140Cap
Gene namesi
Name:SRCIN1
Synonyms:KIAA1684, P140
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:29506. SRCIN1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. axon Source: UniProtKB
  3. cell junction Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB
  5. dendrite Source: UniProtKB
  6. filopodium Source: Ensembl
  7. lamellipodium Source: Ensembl
  8. neuronal cell body Source: Ensembl
  9. postsynaptic density Source: UniProtKB
  10. postsynaptic membrane Source: UniProtKB-KW
  11. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165432823.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10551055SRC kinase signaling inhibitor 1
PRO_0000072011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphotyrosine By similarity
Modified residuei215 – 2151Phosphoserine By similarity
Modified residuei268 – 2681Phosphotyrosine By similarity
Modified residuei394 – 3941Phosphoserine By similarity
Modified residuei779 – 7791Phosphoserine By similarity
Modified residuei859 – 8591Phosphoserine By similarity
Modified residuei915 – 9151Phosphoserine By similarity

Post-translational modificationi

Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9C0H9.
PaxDbiQ9C0H9.
PRIDEiQ9C0H9.

PTM databases

PhosphoSiteiQ9C0H9.

Expressioni

Tissue specificityi

Expressed in some primary breast carcinomas where its presence is significantly associated with increased tumor size. Not detected in normal breast tissue.1 Publication

Gene expression databases

ArrayExpressiQ9C0H9.
BgeeiQ9C0H9.
GenevestigatoriQ9C0H9.

Organism-specific databases

HPAiHPA009701.

Interactioni

Subunit structurei

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/EB3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569453EBI-1393949,EBI-702093
SRCP129313EBI-1393949,EBI-621482

Protein-protein interaction databases

BioGridi123275. 7 interactions.
IntActiQ9C0H9. 4 interactions.
MINTiMINT-4777404.
STRINGi9606.ENSP00000264659.

Structurei

3D structure databases

ProteinModelPortaliQ9C0H9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni519 – 56951Interaction with SNAP25 By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili433 – 46028 Reviewed prediction
Add
BLAST
Coiled coili521 – 54626 Reviewed prediction
Add
BLAST
Coiled coili588 – 65063 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi343 – 37634Pro-rich
Add
BLAST
Compositional biasi828 – 88659Pro-rich
Add
BLAST

Sequence similaritiesi

Belongs to the SRCIN1 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG69680.
HOGENOMiHOG000293351.
HOVERGENiHBG019587.
InParanoidiQ9C0H9.
OMAiRESHHPP.
PhylomeDBiQ9C0H9.
TreeFamiTF332255.

Family and domain databases

InterProiIPR026727. Srcin1.
[Graphical view]
PANTHERiPTHR22741:SF5. PTHR22741:SF5. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9C0H9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRGAWVHLHS GAASSLRPCR CGAGAAPKSS PRSPGGRRGD GSSDSEGGVS     50
FAGVLFLQFG EETRRVHITH EVSSLDTLHA LIAHMFPQKL TMGMLKSPNT 100
AILIKDEARN VFYELEDVRD IQDRSIIKIY RKEPLYAAFP GSHLTNGDLR 150
REMVYASRES SPTRRLNNLS PAPHLASGSP PPGLPSGLPS GLQSGSPSRS 200
RLSYAGGRPP SYAGSPVHHA AERLGGAPAA QGVSPSPSAI LERRDVKPDE 250
DLASKAGGMV LVKGEGLYAD PYGLLHEGRL SLAAAAGDPF AYPGAGGLYK 300
RGSVRSLSTY SAAALQSDLE DSLYKAAGGG GPLYGDGYGF RLPPSSPQKL 350
ADVAAPPGGP PPPHSPYSGP PSRGSPVRQS FRKDSGSSSV FAESPGGKTR 400
SAGSASTAGA PPSELFPGPG ERSLVGFGPP VPAKDTETRE RMEAMEKQIA 450
SLTGLVQSAL LRGSEPETPS EKIEGSNGAA TPSAPCGSGG RSSGATPVSG 500
PPPPSASSTP AGQPTAVSRL QMQLHLRGLQ NSASDLRGQL QQLRKLQLQN 550
QESVRALLKR TEAELSMRVS EAARRQEDPL QRQRTLVEEE RLRYLNDEEL 600
ITQQLNDLEK SVEKIQRDVS HNHRLVPGPE LEEKALVLKQ LGETLTELKA 650
HFPGLQSKMR VVLRVEVEAV KFLKEEPQRL DGLLKRCRGV TDTLAQIRRQ 700
VDEGVWPPPN NLLSQSPKKV TAETDFNKSV DFEMPPPSPP LNLHELSGPA 750
EGASLTPKGG NPTKGLDTPG KRSVDKAVSV EAAERDWEEK RAALTQYSAK 800
DINRLLEETQ AELLKAIPDL DCASKAHPGP APTPDHKPPK APHGQKAAPR 850
TEPSGRRGSD ELTVPRYRTE KPSKSPPPPP PRRSFPSSHG LTTTRTGEVV 900
VTSKKDSAFI KKAESEELEV QKPQVKLRRA VSEVARPAST PPIMASAIKD 950
EDDEDRIIAE LESGGGSVPP MKVVTPGASR LKAAQGQAGS PDKSKHGKQR 1000
AEYMRIQAQQ QATKPSKEMS GSNETSSPVS EKPSASRTSI PVLTSFGARN 1050
SSISF 1055
Length:1,055
Mass (Da):112,453
Last modified:May 18, 2010 - v3
Checksum:iCAB346DA20883EBD
GO
Isoform 2 (identifier: Q9C0H9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1012-1055: ATKPSKEMSGSNETSSPVSEKPSASRTSIPVLTSFGARNSSISF → V

Note: No experimental confirmation available.

Show »
Length:1,012
Mass (Da):108,025
Checksum:i140EEB2BFB499E47
GO
Isoform 3 (identifier: Q9C0H9-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:257
Mass (Da):28,590
Checksum:iFA12D8010D0C52D4
GO
Isoform 4 (identifier: Q9C0H9-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,183
Mass (Da):127,105
Checksum:i52BF566E715EF6FF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 566566Missing in isoform 3.
VSP_009366Add
BLAST
Alternative sequencei1 – 5252MRGAW…GVSFA → MGNAPSQDPERSSPPMLSAD DAEYPREYRTLGGGGGGGSG GRRFSNVGLVHTSERRHTVI AAQSLEALSGLQKADADRKR DAFMDHLKSKYPQHALALRG QQDRMREQPNYWSFKTRSSR HTQGAQPGLADQAAKLSYAS AESLETMSEAELPLGFSRMN RFRQSLPLSRSASQTKLRSP in isoform 4.
VSP_039240Add
BLAST
Alternative sequencei782 – 82342AAERD…DLDCA → VLGPGIVGGAMSQVHTFLRP SFLEWGVPILWVFFLGGGGP VP in isoform 3.
VSP_009367Add
BLAST
Alternative sequencei824 – 1055232Missing in isoform 3.
VSP_009368Add
BLAST
Alternative sequencei1012 – 105544ATKPS…SSISF → V in isoform 2.
VSP_050630Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3141Missing AA sequence 1 Publication
Sequence conflicti481 – 4811T → I in BAC86634. 1 Publication
Sequence conflicti592 – 5921L → I AA sequence 1 Publication
Sequence conflicti705 – 7051V → M AA sequence 1 Publication
Sequence conflicti713 – 7142LS → IN AA sequence 1 Publication
Sequence conflicti843 – 8431H → E AA sequence 1 Publication
Sequence conflicti850 – 8501R → K AA sequence 1 Publication
Sequence conflicti867 – 8671Y → R AA sequence 1 Publication
Sequence conflicti958 – 9581I → L AA sequence 1 Publication
Sequence conflicti987 – 9871Q → P AA sequence 1 Publication
Sequence conflicti994 – 9941S → G AA sequence 1 Publication
Isoform 4 (identifier: Q9C0H9-5)
Sequence conflicti177 – 1771L → P in BAD03968. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45660.1. [Q9C0H9-5]
RefSeqiNP_079524.2. NM_025248.2. [Q9C0H9-5]
UniGeneiHs.448872.

Genome annotation databases

EnsembliENST00000264659; ENSP00000264659; ENSG00000017373. [Q9C0H9-5]
ENST00000570888; ENSP00000461232; ENSG00000262199. [Q9C0H9-5]
GeneIDi80725.
KEGGihsa:80725.
UCSCiuc002hqd.3. human. [Q9C0H9-5]
uc002hqf.1. human. [Q9C0H9-2]
uc002hqg.3. human. [Q9C0H9-4]

Polymorphism databases

DMDMi296452948.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45660.1. [Q9C0H9-5 ]
RefSeqi NP_079524.2. NM_025248.2. [Q9C0H9-5 ]
UniGenei Hs.448872.

3D structure databases

ProteinModelPortali Q9C0H9.
ModBasei Search...

Protein-protein interaction databases

BioGridi 123275. 7 interactions.
IntActi Q9C0H9. 4 interactions.
MINTi MINT-4777404.
STRINGi 9606.ENSP00000264659.

Chemistry

ChEMBLi CHEMBL2150836.

PTM databases

PhosphoSitei Q9C0H9.

Polymorphism databases

DMDMi 296452948.

Proteomic databases

MaxQBi Q9C0H9.
PaxDbi Q9C0H9.
PRIDEi Q9C0H9.

Protocols and materials databases

DNASUi 80725.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264659 ; ENSP00000264659 ; ENSG00000017373 . [Q9C0H9-5 ]
ENST00000570888 ; ENSP00000461232 ; ENSG00000262199 . [Q9C0H9-5 ]
GeneIDi 80725.
KEGGi hsa:80725.
UCSCi uc002hqd.3. human. [Q9C0H9-5 ]
uc002hqf.1. human. [Q9C0H9-2 ]
uc002hqg.3. human. [Q9C0H9-4 ]

Organism-specific databases

CTDi 80725.
GeneCardsi GC17M036686.
H-InvDB HIX0021064.
HGNCi HGNC:29506. SRCIN1.
HPAi HPA009701.
MIMi 610786. gene.
neXtProti NX_Q9C0H9.
PharmGKBi PA165432823.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69680.
HOGENOMi HOG000293351.
HOVERGENi HBG019587.
InParanoidi Q9C0H9.
OMAi RESHHPP.
PhylomeDBi Q9C0H9.
TreeFami TF332255.

Miscellaneous databases

ChiTaRSi SRCIN1. human.
GenomeRNAii 80725.
NextBioi 71035.
PROi Q9C0H9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9C0H9.
Bgeei Q9C0H9.
Genevestigatori Q9C0H9.

Family and domain databases

InterProi IPR026727. Srcin1.
[Graphical view ]
PANTHERi PTHR22741:SF5. PTHR22741:SF5. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: FUNCTION, INTERACTION WITH CTTN AND MAPRE3, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSRCN1_HUMAN
AccessioniPrimary (citable) accession number: Q9C0H9
Secondary accession number(s): Q75T46, Q8N4W8
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi