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Protein

Src substrate cortactin

Gene

CTTN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in the invasiveness of cancer cells, and the formation of metastases (PubMed:16636290). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (PubMed:20861316). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (PubMed:23144454).By similarity4 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • profilin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085733-MONOMER.
ReactomeiR-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiQ14247.

Names & Taxonomyi

Protein namesi
Recommended name:
Src substrate cortactin
Alternative name(s):
Amplaxin
Oncogene EMS1
Gene namesi
Name:CTTN
Synonyms:EMS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3338. CTTN.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cell cortex Source: UniProtKB
  • clathrin-coated pit Source: UniProtKB
  • cortical cytoskeleton Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: ProtInc
  • dendritic spine Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: HPA
  • intracellular membrane-bounded organelle Source: HPA
  • lamellipodium Source: UniProtKB
  • mitotic spindle midzone Source: Ensembl
  • plasma membrane Source: HPA
  • podosome Source: UniProtKB-SubCell
  • ruffle Source: UniProtKB
  • voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2017.
OpenTargetsiENSG00000085733.
PharmGKBiPA27775.

Polymorphism and mutation databases

BioMutaiCTTN.
DMDMi215273892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000721891 – 550Src substrate cortactinAdd BLAST550

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87N6-acetyllysineCombined sources1
Modified residuei113PhosphoserineBy similarity1
Modified residuei119Omega-N-methylarginineBy similarity1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei144N6-acetyllysine; alternateBy similarity1
Cross-linki144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei150PhosphoserineCombined sources1
Modified residuei161N6-acetyllysineBy similarity1
Modified residuei181N6-acetyllysine; alternateBy similarity1
Cross-linki181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei198N6-acetyllysineCombined sources1
Cross-linki218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei235N6-acetyllysineCombined sources1
Modified residuei261PhosphoserineCombined sources1
Modified residuei272N6-acetyllysineCombined sources1
Modified residuei295N6-acetyllysineBy similarity1
Modified residuei304N6-acetyllysineCombined sources1
Modified residuei309N6-acetyllysineCombined sources1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei399PhosphothreonineCombined sources1
Modified residuei401PhosphothreonineCombined sources1
Modified residuei405PhosphoserineCombined sources1
Modified residuei411PhosphothreonineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei418PhosphoserineCombined sources1
Modified residuei421Phosphotyrosine; by SRCCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei438PhosphoserineCombined sources1
Modified residuei446PhosphotyrosineCombined sources1
Modified residuei447PhosphoserineCombined sources1
Modified residuei453PhosphotyrosineCombined sources1
Modified residuei470Phosphotyrosine; by FAK1By similarity1
Modified residuei486Phosphotyrosine; by SRC2 Publications1
Modified residuei489Phosphotyrosine; by SRCBy similarity1

Post-translational modificationi

Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associates with filamentous actin (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation (By similarity). Phosphorylated by PTK2/FAK1 in response to cell adhesion (By similarity). Phosphorylated by FER. Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated in response to FGR activation. Phosphorylation by SRC promotes MYLK binding.By similarity3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14247.
MaxQBiQ14247.
PeptideAtlasiQ14247.
PRIDEiQ14247.

2D gel databases

OGPiQ14247.

PTM databases

iPTMnetiQ14247.
PhosphoSitePlusiQ14247.
SwissPalmiQ14247.

Expressioni

Gene expression databases

BgeeiENSG00000085733.
CleanExiHS_CTTN.
ExpressionAtlasiQ14247. baseline and differential.
GenevisibleiQ14247. HS.

Organism-specific databases

HPAiCAB011235.
HPA057242.

Interactioni

Subunit structurei

Interacts with SHANK2 and SHANK3 (via its SH3 domain). Also interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2 (By similarity). Interacts with KCNA2 (via non-phosphorylated C-terminus) (PubMed:12151401). Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2 (By similarity). Interacts with ACTN1 (By similarity). Interacts with FER (PubMed:9722593). Forms a complex made of ABL1 and MYLK. Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Interacts with KCNH1 (PubMed:23144454).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB2P321212EBI-351886,EBI-714559
ASAP1Q9ULH17EBI-351886,EBI-346622
Cbll1Q9JIY28EBI-351886,EBI-7644904From a different organism.
DNM2P505705EBI-351886,EBI-346547
EGFRP005333EBI-351886,EBI-297353
HDAC6Q9UBN73EBI-351886,EBI-301697
Kcnma1Q084603EBI-351886,EBI-1633915From a different organism.
PTPN1P180312EBI-351886,EBI-968788
Srcin1Q9QWI6-22EBI-351886,EBI-775607From a different organism.
tirB7UM993EBI-351886,EBI-2504426From a different organism.
WASP427683EBI-351886,EBI-346375

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • profilin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108332. 114 interactors.
DIPiDIP-33190N.
IntActiQ14247. 64 interactors.
MINTiMINT-361929.

Structurei

Secondary structure

1550
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi497 – 499Combined sources3
Beta strandi506 – 510Combined sources5
Beta strandi518 – 523Combined sources6
Beta strandi526 – 534Combined sources9
Beta strandi537 – 542Combined sources6
Helixi543 – 545Combined sources3
Beta strandi546 – 548Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ProteinModelPortaliQ14247.
SMRiQ14247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14247.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati80 – 116Cortactin 1Add BLAST37
Repeati117 – 153Cortactin 2Add BLAST37
Repeati154 – 190Cortactin 3Add BLAST37
Repeati191 – 227Cortactin 4Add BLAST37
Repeati228 – 264Cortactin 5Add BLAST37
Repeati265 – 301Cortactin 6Add BLAST37
Repeati302 – 324Cortactin 7; truncatedAdd BLAST23
Domaini492 – 550SH3PROSITE-ProRule annotationAdd BLAST59

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili348 – 401Sequence analysisAdd BLAST54

Domaini

The SH3 motif may mediate binding to the cytoskeleton.Curated

Sequence similaritiesi

Contains 7 cortactin repeats.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain

Phylogenomic databases

GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ14247.
KOiK06106.
OMAiKDYSDGF.
OrthoDBiEOG091G0CPX.
PhylomeDBiQ14247.
TreeFamiTF318935.

Family and domain databases

InterProiIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF15. PTHR10829:SF15. 1 hit.
PfamiPF02218. HS1_rep. 7 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14247-1) [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

        10         20         30         40         50
MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ
60 70 80 90 100
EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV
110 120 130 140 150
GHEYQSKLSK HCSQVDSVRG FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS
160 170 180 190 200
QKDYSSGFGG KYGVQADRVD KSAVGFDYQG KTEKHESQRD YSKGFGGKYG
210 220 230 240 250
IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT DRQDKCALGW
260 270 280 290 300
DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ
310 320 330 340 350
DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI
360 370 380 390 400
RANFENLAKE KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ
410 420 430 440 450
TPPVSPAPQP TEERLPSSPV YEDAASFKAE LSYRGPVSGT EPEPVYSMEA
460 470 480 490 500
ADYREASSQQ GLAYATEAVY ESAEAPGHYP AEDSTYDEYE NDLGITAVAL
510 520 530 540 550
YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL FPANYVELRQ
Length:550
Mass (Da):61,586
Last modified:November 25, 2008 - v2
Checksum:i7799326C2B4383BB
GO
Isoform 2 (identifier: Q14247-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.
     538-550: YGLFPANYVELRQ → FRELAFSCVR...CLGTWVPECP

Note: No experimental confirmation available.
Show »
Length:634
Mass (Da):70,959
Checksum:i9F36B5AED4992281
GO
Isoform 3 (identifier: Q14247-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.

Show »
Length:513
Mass (Da):57,467
Checksum:i333C09D488528C40
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti495I → Y in AAA58455 (PubMed:1532244).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043120264 – 300Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST37
Alternative sequenceiVSP_043121538 – 550YGLFP…VELRQ → FRELAFSCVRVALVPIKCSR DLPGQARGLRSALWRVGRKD CPRRGASSRVSLLGRRGLGL MEVNPELSHPEHRSCHVRWE ICLCHTVTARRIRKLISFLR SREAGPVPSCSQVGGVSFQK VTWKCLGTWVPECP in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98343 mRNA. Translation: AAA58455.1.
AK291097 mRNA. Translation: BAF83786.1.
AP000487 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74766.1.
CH471076 Genomic DNA. Translation: EAW74768.1.
BC008799 mRNA. Translation: AAH08799.1.
BC033889 mRNA. Translation: AAH33889.1.
CCDSiCCDS41680.1. [Q14247-1]
CCDS53676.1. [Q14247-2]
CCDS8197.1. [Q14247-3]
PIRiA48063.
RefSeqiNP_001171669.1. NM_001184740.1. [Q14247-2]
NP_005222.2. NM_005231.3. [Q14247-1]
NP_612632.1. NM_138565.2. [Q14247-3]
UniGeneiHs.596164.

Genome annotation databases

EnsembliENST00000301843; ENSP00000301843; ENSG00000085733. [Q14247-1]
ENST00000346329; ENSP00000317189; ENSG00000085733. [Q14247-3]
ENST00000376561; ENSP00000365745; ENSG00000085733. [Q14247-2]
GeneIDi2017.
KEGGihsa:2017.
UCSCiuc001opu.4. human. [Q14247-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Cortactin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98343 mRNA. Translation: AAA58455.1.
AK291097 mRNA. Translation: BAF83786.1.
AP000487 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74766.1.
CH471076 Genomic DNA. Translation: EAW74768.1.
BC008799 mRNA. Translation: AAH08799.1.
BC033889 mRNA. Translation: AAH33889.1.
CCDSiCCDS41680.1. [Q14247-1]
CCDS53676.1. [Q14247-2]
CCDS8197.1. [Q14247-3]
PIRiA48063.
RefSeqiNP_001171669.1. NM_001184740.1. [Q14247-2]
NP_005222.2. NM_005231.3. [Q14247-1]
NP_612632.1. NM_138565.2. [Q14247-3]
UniGeneiHs.596164.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ProteinModelPortaliQ14247.
SMRiQ14247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108332. 114 interactors.
DIPiDIP-33190N.
IntActiQ14247. 64 interactors.
MINTiMINT-361929.

PTM databases

iPTMnetiQ14247.
PhosphoSitePlusiQ14247.
SwissPalmiQ14247.

Polymorphism and mutation databases

BioMutaiCTTN.
DMDMi215273892.

2D gel databases

OGPiQ14247.

Proteomic databases

EPDiQ14247.
MaxQBiQ14247.
PeptideAtlasiQ14247.
PRIDEiQ14247.

Protocols and materials databases

DNASUi2017.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301843; ENSP00000301843; ENSG00000085733. [Q14247-1]
ENST00000346329; ENSP00000317189; ENSG00000085733. [Q14247-3]
ENST00000376561; ENSP00000365745; ENSG00000085733. [Q14247-2]
GeneIDi2017.
KEGGihsa:2017.
UCSCiuc001opu.4. human. [Q14247-1]

Organism-specific databases

CTDi2017.
DisGeNETi2017.
GeneCardsiCTTN.
HGNCiHGNC:3338. CTTN.
HPAiCAB011235.
HPA057242.
MIMi164765. gene.
neXtProtiNX_Q14247.
OpenTargetsiENSG00000085733.
PharmGKBiPA27775.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ14247.
KOiK06106.
OMAiKDYSDGF.
OrthoDBiEOG091G0CPX.
PhylomeDBiQ14247.
TreeFamiTF318935.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085733-MONOMER.
ReactomeiR-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiQ14247.

Miscellaneous databases

ChiTaRSiCTTN. human.
EvolutionaryTraceiQ14247.
GeneWikiiCortactin.
GenomeRNAii2017.
PROiQ14247.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000085733.
CleanExiHS_CTTN.
ExpressionAtlasiQ14247. baseline and differential.
GenevisibleiQ14247. HS.

Family and domain databases

InterProiIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10829:SF15. PTHR10829:SF15. 1 hit.
PfamiPF02218. HS1_rep. 7 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRC8_HUMAN
AccessioniPrimary (citable) accession number: Q14247
Secondary accession number(s): Q8N707, Q96H99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 176 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.