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Q60598

- SRC8_MOUSE

UniProt

Q60598 - SRC8_MOUSE

Protein

Src substrate cortactin

Gene

Cttn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 By similarity. Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density By similarity. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases.By similarity2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of extrinsic apoptotic signaling pathway Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Src substrate cortactin
    Gene namesi
    Name:Cttn
    Synonyms:Ems1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:99695. Cttn.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle. Cytoplasmcell cortex. Cell projectiondendritic spine By similarity. Cell projectiondendrite By similarity
    Note: Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. 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: MGI
    2. cytoplasm Source: MGI
    3. dendritic spine Source: UniProtKB-SubCell
    4. lamellipodium Source: UniProtKB
    5. mitotic spindle midzone Source: UniProt
    6. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546Src substrate cortactinPRO_0000072190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871N6-acetyllysine1 Publication
    Modified residuei124 – 1241N6-acetyllysine1 Publication
    Modified residuei144 – 1441N6-acetyllysine1 Publication
    Modified residuei161 – 1611N6-acetyllysine1 Publication
    Modified residuei181 – 1811N6-acetyllysine1 Publication
    Modified residuei198 – 1981N6-acetyllysine1 Publication
    Modified residuei235 – 2351N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysine1 Publication
    Modified residuei295 – 2951N6-acetyllysine1 Publication
    Modified residuei304 – 3041N6-acetyllysineBy similarity
    Modified residuei309 – 3091N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-acetyllysine1 Publication
    Modified residuei401 – 4011Phosphothreonine2 Publications
    Modified residuei405 – 4051Phosphoserine2 Publications
    Modified residuei407 – 4071Phosphoserine2 Publications
    Modified residuei417 – 4171PhosphoserineBy similarity
    Modified residuei418 – 4181PhosphoserineBy similarity
    Modified residuei421 – 4211PhosphotyrosineBy similarity
    Modified residuei442 – 4421PhosphotyrosineBy similarity
    Modified residuei482 – 4821Phosphotyrosine; by SRC2 Publications
    Modified residuei485 – 4851Phosphotyrosine; by SRC2 Publications

    Post-translational modificationi

    Phosphorylated by FER. Phosphorylated in response to FGR activation. Phosphorylation by SRC promotes MYLK binding By similarity. Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. 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 associate with filamentous actin.By similarity3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ60598.
    PaxDbiQ60598.
    PRIDEiQ60598.

    PTM databases

    PhosphoSiteiQ60598.

    Expressioni

    Tissue specificityi

    Expressed in most tissues, except in B-lymphocytes or plasma cells.

    Gene expression databases

    ArrayExpressiQ60598.
    BgeeiQ60598.
    CleanExiMM_CTTN.
    GenevestigatoriQ60598.

    Interactioni

    Subunit structurei

    Interacts with SHANK2 and SHANK3 (via its SH3 domain). 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 with ABL1 and MYLK By similarity. Interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2. 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 similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTR3P611574EBI-397955,EBI-351419From a different organism.
    Actr3Q99JY95EBI-397955,EBI-773994
    Cbll1Q9JIY24EBI-397955,EBI-7644904
    Cfl1P455922EBI-397955,EBI-917556From a different organism.
    Dnm2P390542EBI-397955,EBI-642337
    HDAC6Q9UBN73EBI-397955,EBI-301697From a different organism.
    Kcnma1Q084602EBI-397955,EBI-1633915
    MTSS1O433122EBI-397955,EBI-473954From a different organism.
    WASLQ951072EBI-397955,EBI-6162776From a different organism.
    WaslQ91YD94EBI-397955,EBI-642417
    WIPF1O435163EBI-397955,EBI-346356From a different organism.

    Protein-protein interaction databases

    BioGridi198978. 8 interactions.
    DIPiDIP-31562N.
    IntActiQ60598. 38 interactions.
    MINTiMINT-100616.

    Structurei

    Secondary structure

    1
    546
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi493 – 4953
    Beta strandi514 – 5196
    Beta strandi522 – 5309
    Beta strandi533 – 5386
    Helixi539 – 5413
    Beta strandi542 – 5443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9Xmodel-A1-546[»]
    3ULRX-ray1.65B487-546[»]
    ProteinModelPortaliQ60598.
    SMRiQ60598. Positions 487-546.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Domaini488 – 54659SH3PROSITE-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.
    GeneTreeiENSGT00530000062953.
    HOGENOMiHOG000006523.
    HOVERGENiHBG005994.
    InParanoidiQ3UGC2.
    KOiK06106.
    OMAiHESQQDY.
    OrthoDBiEOG7V49ZC.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q60598-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ    50
    EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDRSAV 100
    GHEYQSKLSK HCSQVDSVRG FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS 150
    QKDYSSGFGG KYGVQADRVD KSAVGFDYQG KTEKHESQKD YSKGFGGKYG 200
    IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT DRQDKCALGW 250
    DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSSAVGFDYK ERLAKHESQQ 300
    DYAKGFGGKY GVQKDRMDKN ASTFEEVVQV PSAYQKTVPI EAVTSKTSNI 350
    RANFENLAKE REQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKKQ 400
    TPPASPSPQP IEDRPPSSPI YEDAAPFKAE PSYRGSEPEP EYSIEAAGIP 450
    EAGSQQGLTY TSEPVYETTE APGHYQAEDD TYDGYESDLG ITAIALYDYQ 500
    AAGDDEISFD PDDIITNIEM IDDGWWRGVC KGRYGLFPAN YVELRQ 546
    Length:546
    Mass (Da):61,250
    Last modified:July 27, 2011 - v2
    Checksum:i8F5CA026ACCD6D4F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91A → R AA sequence (PubMed:7693700)Curated
    Sequence conflicti298 – 2981S → P in AAA19689. (PubMed:7516062)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03184 mRNA. Translation: AAA19689.1.
    AK146856 mRNA. Translation: BAE27485.1.
    AK148010 mRNA. Translation: BAE28287.1.
    AK168699 mRNA. Translation: BAE40543.1.
    CH466531 Genomic DNA. Translation: EDL18251.1.
    CCDSiCCDS22049.1.
    PIRiI48899.
    RefSeqiNP_031829.2. NM_007803.5.
    XP_006508535.1. XM_006508472.1.
    UniGeneiMm.205601.
    Mm.490123.

    Genome annotation databases

    EnsembliENSMUST00000103079; ENSMUSP00000099368; ENSMUSG00000031078.
    GeneIDi13043.
    KEGGimmu:13043.
    UCSCiuc009kqh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03184 mRNA. Translation: AAA19689.1 .
    AK146856 mRNA. Translation: BAE27485.1 .
    AK148010 mRNA. Translation: BAE28287.1 .
    AK168699 mRNA. Translation: BAE40543.1 .
    CH466531 Genomic DNA. Translation: EDL18251.1 .
    CCDSi CCDS22049.1.
    PIRi I48899.
    RefSeqi NP_031829.2. NM_007803.5.
    XP_006508535.1. XM_006508472.1.
    UniGenei Mm.205601.
    Mm.490123.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F9X model - A 1-546 [» ]
    3ULR X-ray 1.65 B 487-546 [» ]
    ProteinModelPortali Q60598.
    SMRi Q60598. Positions 487-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198978. 8 interactions.
    DIPi DIP-31562N.
    IntActi Q60598. 38 interactions.
    MINTi MINT-100616.

    PTM databases

    PhosphoSitei Q60598.

    Proteomic databases

    MaxQBi Q60598.
    PaxDbi Q60598.
    PRIDEi Q60598.

    Protocols and materials databases

    DNASUi 13043.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103079 ; ENSMUSP00000099368 ; ENSMUSG00000031078 .
    GeneIDi 13043.
    KEGGi mmu:13043.
    UCSCi uc009kqh.2. mouse.

    Organism-specific databases

    CTDi 2017.
    MGIi MGI:99695. Cttn.

    Phylogenomic databases

    eggNOGi NOG123488.
    GeneTreei ENSGT00530000062953.
    HOGENOMi HOG000006523.
    HOVERGENi HBG005994.
    InParanoidi Q3UGC2.
    KOi K06106.
    OMAi HESQQDY.
    OrthoDBi EOG7V49ZC.
    TreeFami TF318935.

    Miscellaneous databases

    NextBioi 282940.
    PROi Q60598.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60598.
    Bgeei Q60598.
    CleanExi MM_CTTN.
    Genevestigatori Q60598.

    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. "The protein tyrosine kinase substrate cortactin is differentially expressed in murine B lymphoid tumors."
      Miglarese M.R., Mannion-Henderson J., Wu H., Parsons J.T., Bender T.P.
      Oncogene 9:1989-1997(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Murine cortactin is phosphorylated in response to fibroblast growth factor-1 on tyrosine residues late in the G1 phase of the BALB/c 3T3 cell cycle."
      Zhan X., Hu X., Hampton B., Burgess W.H., Friesel R., Maciag T.
      J. Biol. Chem. 268:24427-24431(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 125-138; 273-289 AND 534-543.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion and Heart.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
      Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
      Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1; FGFR4 AND GAP43.
    6. "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly interacts with cortactin and mAbp1 to modulate cell shape."
      Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B., Gorski J.L.
      Hum. Mol. Genet. 12:1981-1993(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FGD1.
    7. "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
      Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
      J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIN BUNDLE FORMATION, PHOSPHORYLATION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. Cited for: PHOSPHORYLATION AT TYR-482 AND TYR-485.
    10. "Cortactin-binding protein 2 modulates the mobility of cortactin and regulates dendritic spine formation and maintenance."
      Chen Y.K., Hsueh Y.P.
      J. Neurosci. 32:1043-1055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTTNBP2, SUBCELLULAR LOCATION.
    11. "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic distribution of the striatin-PP2A complex."
      Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.
      Mol. Biol. Cell 23:4383-4392(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTTNBP2NL, SUBCELLULAR LOCATION.
    12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-124; LYS-144; LYS-161; LYS-181; LYS-198; LYS-235; LYS-272; LYS-295; LYS-309 AND LYS-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    13. "Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex."
      Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.
      Acta Crystallogr. F 68:154-158(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 487-546 IN COMPLEX WITH ABL2, INTERACTION WITH ABL2.

    Entry informationi

    Entry nameiSRC8_MOUSE
    AccessioniPrimary (citable) accession number: Q60598
    Secondary accession number(s): Q3UGC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3