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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 - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. actin filament polymerization Source: InterPro
  3. cell motility Source: UniProtKB
  4. dendritic spine maintenance Source: Ensembl
  5. focal adhesion assembly Source: UniProtKB
  6. intracellular protein transport Source: UniProtKB
  7. lamellipodium organization Source: UniProtKB
  8. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  9. neuron projection morphogenesis Source: UniProtKB
  10. positive regulation of actin filament polymerization Source: UniProtKB
  11. receptor-mediated endocytosis Source: UniProtKB
  12. regulation of axon extension Source: UniProtKB
  13. substrate-dependent cell migration, cell extension Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Endocytosis

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3338. CTTN.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cell projectionlamellipodium 1 Publication. Cell projectionruffle. Cell projectiondendrite By similarity. Cell projection By similarity. Cell membrane 1 Publication; Peripheral membrane protein Curated; Cytoplasmic side Curated. Cell projectionpodosome By similarity. Cell junction By similarity. Cell junctionfocal adhesion By similarity. Membraneclathrin-coated pit By similarity. Cell projectiondendritic spine By similarity. Cytoplasmcell cortex 1 Publication
Note: Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers (By similarity). In the presence of CTTNBP2, localizes at the cell cortex (By similarity). In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft (By similarity). Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity).By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. coated pit Source: UniProtKB
  3. cortical cytoskeleton Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytoskeleton Source: ProtInc
  6. dendritic spine Source: UniProtKB-SubCell
  7. extracellular vesicular exosome Source: UniProtKB
  8. focal adhesion Source: UniProtKB
  9. lamellipodium Source: UniProtKB
  10. mitotic spindle midzone Source: Ensembl
  11. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Src substrate cortactinPRO_0000072189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871N6-acetyllysine1 Publication
Modified residuei124 – 1241N6-acetyllysineBy similarity
Modified residuei144 – 1441N6-acetyllysineBy similarity
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei161 – 1611N6-acetyllysineBy similarity
Modified residuei181 – 1811N6-acetyllysineBy similarity
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysine1 Publication
Modified residuei261 – 2611Phosphoserine1 Publication
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-acetyllysineBy similarity
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei309 – 3091N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysineBy similarity
Modified residuei399 – 3991Phosphothreonine2 Publications
Modified residuei401 – 4011Phosphothreonine2 Publications
Modified residuei405 – 4051Phosphoserine9 Publications
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei418 – 4181Phosphoserine5 Publications
Modified residuei421 – 4211Phosphotyrosine; by SRC2 Publications
Modified residuei446 – 4461Phosphotyrosine1 Publication
Modified residuei447 – 4471Phosphoserine1 Publication
Modified residuei453 – 4531Phosphotyrosine1 Publication
Modified residuei470 – 4701Phosphotyrosine; by FAK1By similarity
Modified residuei486 – 4861Phosphotyrosine; by SRC2 Publications
Modified residuei489 – 4891Phosphotyrosine; by SRCBy similarity

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, Phosphoprotein

Proteomic databases

MaxQBiQ14247.
PaxDbiQ14247.
PRIDEiQ14247.

2D gel databases

OGPiQ14247.

PTM databases

PhosphoSiteiQ14247.

Expressioni

Gene expression databases

BgeeiQ14247.
CleanExiHS_CTTN.
ExpressionAtlasiQ14247. baseline and differential.
GenevestigatoriQ14247.

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

Protein-protein interaction databases

BioGridi108332. 85 interactions.
DIPiDIP-33190N.
IntActiQ14247. 39 interactions.
MINTiMINT-361929.
STRINGi9606.ENSP00000301843.

Structurei

Secondary structure

1
550
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi497 – 4993Combined sources
Beta strandi506 – 5105Combined sources
Beta strandi518 – 5236Combined sources
Beta strandi526 – 5349Combined sources
Beta strandi537 – 5426Combined sources
Helixi543 – 5453Combined sources
Beta strandi546 – 5483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ProteinModelPortaliQ14247.
SMRiQ14247. Positions 490-550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14247.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati80 – 11637Cortactin 1Add
BLAST
Repeati117 – 15337Cortactin 2Add
BLAST
Repeati154 – 19037Cortactin 3Add
BLAST
Repeati191 – 22737Cortactin 4Add
BLAST
Repeati228 – 26437Cortactin 5Add
BLAST
Repeati265 – 30137Cortactin 6Add
BLAST
Repeati302 – 32423Cortactin 7; truncatedAdd
BLAST
Domaini492 – 55059SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili348 – 40154Sequence AnalysisAdd
BLAST

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

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ14247.
KOiK06106.
OMAiWKATAGH.
OrthoDBiEOG7V49ZC.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti495 – 4951I → Y in AAA58455 (PubMed:1532244).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei264 – 30037Missing in isoform 2 and isoform 3. 2 PublicationsVSP_043120Add
BLAST
Alternative sequencei538 – 55013YGLFP…VELRQ → FRELAFSCVRVALVPIKCSR DLPGQARGLRSALWRVGRKD CPRRGASSRVSLLGRRGLGL MEVNPELSHPEHRSCHVRWE ICLCHTVTARRIRKLISFLR SREAGPVPSCSQVGGVSFQK VTWKCLGTWVPECP in isoform 2. 1 PublicationVSP_043121Add
BLAST

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.3. human. [Q14247-2]
uc001opv.4. human. [Q14247-1]
uc001opw.4. human. [Q14247-3]

Polymorphism databases

DMDMi215273892.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ProteinModelPortaliQ14247.
SMRiQ14247. Positions 490-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108332. 85 interactions.
DIPiDIP-33190N.
IntActiQ14247. 39 interactions.
MINTiMINT-361929.
STRINGi9606.ENSP00000301843.

PTM databases

PhosphoSiteiQ14247.

Polymorphism databases

DMDMi215273892.

2D gel databases

OGPiQ14247.

Proteomic databases

MaxQBiQ14247.
PaxDbiQ14247.
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.3. human. [Q14247-2]
uc001opv.4. human. [Q14247-1]
uc001opw.4. human. [Q14247-3]

Organism-specific databases

CTDi2017.
GeneCardsiGC11P070244.
HGNCiHGNC:3338. CTTN.
HPAiCAB011235.
HPA057242.
MIMi164765. gene.
neXtProtiNX_Q14247.
PharmGKBiPA27775.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiQ14247.
KOiK06106.
OMAiWKATAGH.
OrthoDBiEOG7V49ZC.
PhylomeDBiQ14247.
TreeFamiTF318935.

Miscellaneous databases

ChiTaRSiCTTN. human.
EvolutionaryTraceiQ14247.
GeneWikiiCortactin.
GenomeRNAii2017.
NextBioi8171.
PROiQ14247.
SOURCEiSearch...

Gene expression databases

BgeeiQ14247.
CleanExiHS_CTTN.
ExpressionAtlasiQ14247. baseline and differential.
GenevestigatoriQ14247.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and cloning of two overexpressed genes, U21B31/PRAD1 and EMS1, within the amplified chromosome 11q13 region in human carcinomas."
    Schuuring E.M.D., Verhoeven E., Mooi W.J., Michalides R.J.A.
    Oncogene 7:355-361(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  2. "The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites."
    Schuuring E.M.D., Verhoeven E., Litvinov S., Michalides R.J.A.
    Mol. Cell. Biol. 13:2891-2898(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Mammary gland.
  3. "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 3).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2 AND 3).
    Tissue: Placenta and Testis.
  7. "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER."
    Kim L., Wong T.W.
    J. Biol. Chem. 273:23542-23548(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FER, PHOSPHORYLATION OF CTTN, SUBCELLULAR LOCATION.
  8. "Novel interaction of cortactin with endothelial cell myosin light chain kinase."
    Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.
    Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYLK, PHOSPHORYLATION BY SRC.
  9. "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin."
    Hattan D., Nesti E., Cachero T.G., Morielli A.D.
    J. Biol. Chem. 277:38596-38606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA2, SUBCELLULAR LOCATION.
  10. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R."
    Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P., Shankara S., Nacht M., Teicher B., Stampfl J., Singh S., Vogelstein B., Kinzler K.W., St Croix B.
    Cancer Res. 64:8507-8511(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXDC2.
  12. "The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
    Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
    Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-486.
  13. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  17. "An essential role for cortactin in the modulation of the potassium channel Kv1.2."
    Williams M.R., Markey J.C., Doczi M.A., Morielli A.D.
    Proc. Natl. Acad. Sci. U.S.A. 104:17412-17417(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-486.
  18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND TYR-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; THR-411; SER-417 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: INTERACTION WITH SRCIN1.
  24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-418; TYR-421 AND TYR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-235; LYS-272; LYS-304 AND LYS-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
    Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
    Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYLK AND ABL1, FUNCTION.
  27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "The immunoinhibitory adapter protein SRC homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading."
    von Holleben M., Gohla A., Janssen K.P., Iritani B.M., Beer-Hammer S.
    J. Biol. Chem. 286:13489-13501(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SAMSN1.
  30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Cortactin controls surface expression of the voltage-gated potassium channel K(V)10.1."
    Herrmann S., Ninkovic M., Kohl T., Lorinczi E., Pardo L.A.
    J. Biol. Chem. 287:44151-44163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNH1.
  32. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-261; THR-399; THR-401; SER-405 AND SER-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  33. "Solution structures of the SH3 domain of human Src substrate cortactin."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 485-550.
  34. "Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis."
    Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.
    Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 490-550 IN COMPLEX WITH ASAP1, FUNCTION, INTERACTION WITH ASAP1 AND DNM2, SUBCELLULAR LOCATION.

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: March 4, 2015
This is version 156 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

External Data

Dasty 3

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 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.