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Q14247

- SRC8_HUMAN

UniProt

Q14247 - SRC8_HUMAN

Protein

Src substrate cortactin

Gene

CTTN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    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

    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.By similarity

    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

    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-acetyllysineBy similarity
    Modified residuei144 – 1441N6-acetyllysineBy similarity
    Modified residuei161 – 1611N6-acetyllysineBy similarity
    Modified residuei181 – 1811N6-acetyllysineBy similarity
    Modified residuei198 – 1981N6-acetyllysine1 Publication
    Modified residuei235 – 2351N6-acetyllysine1 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 – 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.By similarity13 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.By similarity7 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
    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. 82 interactions.
    DIPiDIP-33190N.
    IntActiQ14247. 38 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.
    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

    Domaini

    The SH3 motif may mediate binding to the cytoskeleton.

    Sequence similaritiesi

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

    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

    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:
    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. 82 interactions.
    DIPi DIP-33190N.
    IntActi Q14247. 38 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

    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: October 1, 2014
    This is version 151 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