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Q9QXY2 (SRCN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:P140, Snip
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1197 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.1 Ref.3

Subunit structure

Interacts with BCAR1/p130Cas through its C-terminal domain and with CSK, CTTN and SRC By similarity. Also interacts with MAPRE3/EB3, SORBS3/vinexin and the N-terminal coiled-coil region of SNAP25. Ref.1 Ref.2 Ref.3 UniProtKB Q9C0H9

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell projectionaxon. Cell projectiondendrite. Cell junctionsynapse. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. 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 pre- and post-synapses and in post-synaptic density fractions. Ref.1 Ref.2 Ref.3

Tissue specificity

Expressed exclusively in brain. Abundant in telencephalon and expressed moderately in cerebellum, hypothalamus, thalamus, superior and inferior colliculi, and olfactory bulb. No expression detected in medulla oblongata, spinal cord or pituitary gland. Enriched in the neuropil rather than soma in the thalamus, corpus striatum and cerebral cortex. Detected in astrocytes. Ref.1 Ref.2

Developmental stage

In the embryo, expression increases dramatically between E14.5 and E18.5 (at protein level). Ref.2

Post-translational modification

Tyrosine-phosphorylated in response to EGF and to cell adhesion to integrin ligands By similarity. UniProtKB Q9C0H9

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
Reference proteome
Gene Ontology (GO)
   Biological processexocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of protein secretion

Inferred from mutant phenotype Ref.1. Source: RGD

negative regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentactin cytoskeleton

Inferred from direct assay Ref.1. Source: RGD

axon

Inferred from direct assay Ref.2. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from direct assay Ref.1. Source: RGD

lamellipodium

Inferred from direct assay Ref.1. Source: RGD

neuronal cell body

Inferred from direct assay Ref.1. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

postsynaptic density

Inferred from direct assay Ref.3. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synaptosome

Inferred from direct assay Ref.1. Source: RGD

   Molecular functionprotein domain specific binding

Inferred from direct assay Ref.1. Source: RGD

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Snap25P608813EBI-1394088,EBI-1027214

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9QXY2-1)

Also known as: SNIP-b;

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 Ref.1 (identifier: Q9QXY2-2)

Also known as: SNIP-a;

The sequence of this isoform differs from the canonical sequence as follows:
     1174-1197: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11971197SRC kinase signaling inhibitor 1
PRO_0000072013

Regions

Region681 – 73151Interaction with SNAP25
Coiled coil594 – 62128 Potential
Coiled coil685 – 70824 Potential
Coiled coil750 – 81263 Potential
Compositional bias990 – 104859Pro-rich

Amino acid modifications

Modified residue791Phosphoserine By similarity
Modified residue981Phosphoserine By similarity
Modified residue1751Phosphoserine By similarity
Modified residue2001Phosphoserine By similarity
Modified residue2601Phosphoserine By similarity
Modified residue2761Phosphotyrosine By similarity
Modified residue3421Phosphoserine By similarity
Modified residue3781Phosphoserine By similarity
Modified residue3971Phosphoserine By similarity
Modified residue4311Phosphotyrosine By similarity
Modified residue5471Phosphoserine By similarity
Modified residue5561Phosphoserine By similarity
Modified residue6371Phosphoserine By similarity
Modified residue6711Phosphothreonine By similarity
Modified residue9001Phosphoserine By similarity
Modified residue9411Phosphoserine By similarity
Modified residue10211Phosphoserine By similarity
Modified residue10771Phosphoserine By similarity

Natural variations

Alternative sequence1174 – 119724Missing in isoform 2. Ref.1
VSP_050633

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 8C9A2E630FB31C33

FASTA1,197129,744
        10         20         30         40         50         60 
MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR 

        70         80         90        100        110        120 
EYRTLGGGGS GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH 

       130        140        150        160        170        180 
LKSKYPQHAL ALRGQQDRMR EQQPNYWSFK TRSSRHTQGA QPGLADQAAK LSYASAESLE 

       190        200        210        220        230        240 
TMSEAELPLG FSRMNRFRQS LPLSRSASQT KLRSPGVLFL QFGEETRRVH ITHEVSSLDT 

       250        260        270        280        290        300 
LHALIAHMFP QKLTMGMLKS PNTAILIKDE ARNVFYELED VRDIQDRSII KIYRKEPLYA 

       310        320        330        340        350        360 
AFPGSHLTNG DLRREMVYAS RESSPTRRLN NLSPASHLAS SSPPPGLPSG LPSGLPSGSP 

       370        380        390        400        410        420 
SRSRLSYAGG RPPSYAGSPV HHAAERLGGA PTSQGVSPSP SAILERRDVK PDEDLAGKAG 

       430        440        450        460        470        480 
GMVLVKGEGL YADPYGLLHE GRLSLAAAAG DPFAYPGAGG LYKRGSVRSL STYSAAALQS 

       490        500        510        520        530        540 
DLEDSLYKAG AGGPLYGDGY GFRLPPSSPQ KLADVSAPSG GPPPPHSPYS GPPSRGSPVR 

       550        560        570        580        590        600 
QSFRKDSGSS SVFAESPGGK ARSTGASTAG APPSELFPGP GERSLVGFGP PVPAKDTETR 

       610        620        630        640        650        660 
ERMEAMEKQI ASLTGLVQSA LLRGSEPETP SEKIEGSNGA ATPSAPVCGS GSRSSGATPV 

       670        680        690        700        710        720 
SGPPPPAVSS TPAGQPTAVS RLQMQMHLRG LQNSASDLRG QLQQLRKLQL QNQESVRALL 

       730        740        750        760        770        780 
KRTEAELSMR VSEAARRQED PLQRQRTLVE EERLRYLNDE ELITQQLNDL EKSVEKIQRD 

       790        800        810        820        830        840 
VAHNHRLVPG PELEEKALVL KQLGETLTEL KAHFPGLQSK MRVVLRVEVE AVKFLKEEPQ 

       850        860        870        880        890        900 
RLDGLLKRCR VVTDTLAQIR RQVDEGVWPP PNNLLNQSPK KVAAETDFSK GLDFEIPPPS 

       910        920        930        940        950        960 
PPLNLHELSG PAEGTPLTPK SGNPTKGLDA PSKRNMDKAV SVEAAERDWE EKRAALTQYS 

       970        980        990       1000       1010       1020 
AKDINRLLEE TQAELLKAIP DLDCASKTHP GPTPTPDHKP PKAPHGQKAA PRTEPSGRRG 

      1030       1040       1050       1060       1070       1080 
SDELTVPRYR TEKPSKSPPP PPPRRSFPSS HGLTTTRTGE VVVTSKKDSV FIKKAESEEL 

      1090       1100       1110       1120       1130       1140 
EIQKPQVKLR RAVSEVVRPA STPPIMASAI KDEDDEERII AELESGGGSV PPMKVVTPGA 

      1150       1160       1170       1180       1190 
SRLKAAQGPA GSPDKGKHGK QRTEYMRIQA QQQVRVGYQA PRPLEGCTPR LCYMPLS 

« Hide

Isoform 2 (SNIP-a) [UniParc].

Checksum: B6DF0EEC27B69080
Show »

FASTA1,173127,055

References

[1]"SNIP, a novel SNAP-25-interacting protein implicated in regulated exocytosis."
Chin L.-S., Nugent R.D., Raynor M.C., Vavalle J.P., Li L.
J. Biol. Chem. 275:1191-1200(2000) [PubMed: 10625663] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNAP25.
[2]"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: 18662323] [Abstract]
Cited for: INTERACTION WITH SORBS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"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: 19146815] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPRE3, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156981 mRNA. Translation: AAF25003.1.
AF156982 mRNA. Translation: AAF25004.1.
IPIIPI00213633.
IPI00400480.
RefSeqNP_062251.1. NM_019378.1.
UniGeneRn.207205.

3D structure databases

ProteinModelPortalQ9QXY2.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QXY2. 4 interactions.
MINTMINT-139008.
STRINGQ9QXY2.

PTM databases

PhosphoSiteQ9QXY2.

Proteomic databases

PRIDEQ9QXY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016070; ENSRNOP00000016070; ENSRNOG00000011475.
GeneID56029.
KEGGrno:56029.
UCSCAF156981. rat.
NM_019378. rat.

Organism-specific databases

CTD80725.
RGD708439. Srcin1.

Phylogenomic databases

eggNOGroNOG12795.
GeneTreeENSGT00390000012399.
HOVERGENHBG019587.

Gene expression databases

ArrayExpressQ9QXY2.
GenevestigatorQ9QXY2.
GermOnlineENSRNOG00000011475. Rattus norvegicus.

Family and domain databases

ProtoNetSearch...

Other

NextBio611083.

Entry information

Entry nameSRCN1_RAT
AccessionPrimary (citable) accession number: Q9QXY2
Secondary accession number(s): Q9QXY3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families