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Q14247

- SRC8_HUMAN

UniProt

Q14247 - SRC8_HUMAN

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Protein

Src substrate cortactin

Gene
CTTN, EMS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Contributes to the organization of the actin cytoskeleton and cell structure. In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

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. Cell projectionlamellipodium. Cell projectionruffle. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity
Note: 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.4 Publications

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: ProtInc
  4. dendritic spine Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProt
  6. lamellipodium Source: UniProtKB
  7. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

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-acetyllysine By similarity
Modified residuei144 – 1441N6-acetyllysine By similarity
Modified residuei161 – 1611N6-acetyllysine By similarity
Modified residuei181 – 1811N6-acetyllysine By similarity
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-acetyllysine By similarity
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei309 – 3091N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine By similarity
Modified residuei399 – 3991Phosphothreonine1 Publication
Modified residuei401 – 4011Phosphothreonine1 Publication
Modified residuei405 – 4051Phosphoserine8 Publications
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei418 – 4181Phosphoserine5 Publications
Modified residuei421 – 4211Phosphotyrosine; by SRC2 Publications
Modified residuei446 – 4461Phosphotyrosine1 Publication
Modified residuei453 – 4531Phosphotyrosine1 Publication
Modified residuei486 – 4861Phosphotyrosine; by SRC1 Publication
Modified residuei489 – 4891Phosphotyrosine; by SRC

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 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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14247.
PaxDbiQ14247.
PRIDEiQ14247.

2D gel databases

OGPiQ14247.

PTM databases

PhosphoSiteiQ14247.

Expressioni

Gene expression databases

ArrayExpressiQ14247.
BgeeiQ14247.
CleanExiHS_CTTN.
GenevestigatoriQ14247.

Organism-specific databases

HPAiCAB011235.

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 PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts with DNM2 and FER. 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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASAP1Q9ULH17EBI-351886,EBI-346622
Cbll1Q9JIY28EBI-351886,EBI-7644904From a different organism.
DNM2P505705EBI-351886,EBI-346547
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. 81 interactions.
IntActiQ14247. 34 interactions.
MINTiMINT-361929.
STRINGi9606.ENSP00000301843.

Structurei

Secondary structure

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

3D structure databases

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

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 – 55059SH3Add
BLAST

Domaini

The SH3 motif may mediate binding to the cytoskeleton.

Sequence similaritiesi

Contains 7 cortactin repeats.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG123488.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
KOiK06106.
OMAiHESQQDY.
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. Align

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

MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ    50
EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV 100
GHEYQSKLSK HCSQVDSVRG FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS 150
QKDYSSGFGG KYGVQADRVD KSAVGFDYQG KTEKHESQRD YSKGFGGKYG 200
IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT DRQDKCALGW 250
DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ 300
DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI 350
RANFENLAKE KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ 400
TPPVSPAPQP TEERLPSSPV YEDAASFKAE LSYRGPVSGT EPEPVYSMEA 450
ADYREASSQQ GLAYATEAVY ESAEAPGHYP AEDSTYDEYE NDLGITAVAL 500
YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL FPANYVELRQ 550
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei264 – 30037Missing in isoform 2 and isoform 3. VSP_043120Add
BLAST
Alternative sequencei538 – 55013YGLFP…VELRQ → FRELAFSCVRVALVPIKCSR DLPGQARGLRSALWRVGRKD CPRRGASSRVSLLGRRGLGL MEVNPELSHPEHRSCHVRWE ICLCHTVTARRIRKLISFLR SREAGPVPSCSQVGGVSFQK VTWKCLGTWVPECP in isoform 2. VSP_043121Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti495 – 4951I → Y in AAA58455. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS41680.1. [Q14247-1 ]
CCDS53676.1. [Q14247-2 ]
CCDS8197.1. [Q14247-3 ]
PIRi A48063.
RefSeqi NP_001171669.1. NM_001184740.1. [Q14247-2 ]
NP_005222.2. NM_005231.3. [Q14247-1 ]
NP_612632.1. NM_138565.2. [Q14247-3 ]
UniGenei Hs.596164.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X69 NMR - A 485-550 [» ]
2D1X X-ray 1.90 A/B/C/D 490-550 [» ]
ProteinModelPortali Q14247.
SMRi Q14247. Positions 490-550.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108332. 81 interactions.
IntActi Q14247. 34 interactions.
MINTi MINT-361929.
STRINGi 9606.ENSP00000301843.

PTM databases

PhosphoSitei Q14247.

Polymorphism databases

DMDMi 215273892.

2D gel databases

OGPi Q14247.

Proteomic databases

MaxQBi Q14247.
PaxDbi Q14247.
PRIDEi Q14247.

Protocols and materials databases

DNASUi 2017.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301843 ; ENSP00000301843 ; ENSG00000085733 . [Q14247-1 ]
ENST00000346329 ; ENSP00000317189 ; ENSG00000085733 . [Q14247-3 ]
ENST00000376561 ; ENSP00000365745 ; ENSG00000085733 . [Q14247-2 ]
GeneIDi 2017.
KEGGi hsa:2017.
UCSCi uc001opu.3. human. [Q14247-2 ]
uc001opv.4. human. [Q14247-1 ]
uc001opw.4. human. [Q14247-3 ]

Organism-specific databases

CTDi 2017.
GeneCardsi GC11P070244.
HGNCi HGNC:3338. CTTN.
HPAi CAB011235.
MIMi 164765. gene.
neXtProti NX_Q14247.
PharmGKBi PA27775.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG123488.
HOGENOMi HOG000006523.
HOVERGENi HBG005994.
KOi K06106.
OMAi HESQQDY.
OrthoDBi EOG7V49ZC.
PhylomeDBi Q14247.
TreeFami TF318935.

Miscellaneous databases

ChiTaRSi CTTN. human.
EvolutionaryTracei Q14247.
GeneWikii Cortactin.
GenomeRNAii 2017.
NextBioi 8171.
PROi Q14247.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14247.
Bgeei Q14247.
CleanExi HS_CTTN.
Genevestigatori Q14247.

Family and domain databases

InterProi IPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10829:SF15. PTHR10829:SF15. 1 hit.
Pfami PF02218. HS1_rep. 7 hits.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  10. "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.
  11. "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.
  12. "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].
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND TYR-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  18. "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.
  19. 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.
  20. "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].
  21. Cited for: INTERACTION WITH SRCIN1.
  22. "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.
  23. "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].
  24. "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.
  25. "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.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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.
  28. "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].
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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.
  31. "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: September 3, 2014
This is version 150 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

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