Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q64010

- CRK_MOUSE

UniProt

Q64010 - CRK_MOUSE

Protein

Adapter molecule crk

Gene

Crk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei237 – 2371Proline switchBy similarity

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein phosphorylated amino acid binding Source: MGI
    4. SH3/SH2 adaptor activity Source: BHF-UCL

    GO - Biological processi

    1. ephrin receptor signaling pathway Source: UniProtKB
    2. positive regulation of signal transduction Source: GOC
    3. regulation of actin cytoskeleton organization Source: UniProtKB
    4. regulation of Rac protein signal transduction Source: Ensembl
    5. regulation of Rho GTPase activity Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198634. Regulation of signaling by CBL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adapter molecule crk
    Alternative name(s):
    Proto-oncogene c-Crk
    p38
    Gene namesi
    Name:Crk
    Synonyms:Crko
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:88508. Crk.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Translocated to the plasma membrane upon cell adhesion.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 304303Adapter molecule crkPRO_0000079352Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei41 – 411PhosphoserineBy similarity
    Modified residuei74 – 741PhosphoserineBy similarity
    Modified residuei83 – 831PhosphoserineBy similarity
    Modified residuei221 – 2211Phosphotyrosine; by ABL12 Publications
    Modified residuei239 – 2391PhosphotyrosineBy similarity

    Post-translational modificationi

    Isoform Crk-II is phosphorylated by KIT. Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.2 Publications
    Proline isomerization at Pro-237 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ64010.
    PaxDbiQ64010.
    PRIDEiQ64010.

    PTM databases

    PhosphoSiteiQ64010.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ64010.
    BgeeiQ64010.
    CleanExiMM_CRK.
    GenevestigatoriQ64010.

    Interactioni

    Subunit structurei

    Interacts with ABL1, C3G, DOCK3, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IGF1RP080693EBI-2906540,EBI-475981From a different organism.

    Protein-protein interaction databases

    BioGridi198887. 25 interactions.
    DIPiDIP-57059N.
    IntActiQ64010. 22 interactions.
    MINTiMINT-4599411.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi136 – 1416
    Beta strandi147 – 1504
    Beta strandi158 – 1636
    Beta strandi165 – 1739
    Beta strandi179 – 1835
    Helixi184 – 1863
    Beta strandi187 – 1893
    Beta strandi238 – 2447
    Beta strandi252 – 2543
    Beta strandi262 – 2687
    Beta strandi271 – 2733
    Beta strandi275 – 2795
    Beta strandi282 – 2865
    Helixi288 – 2903
    Beta strandi291 – 2944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B07X-ray2.50A134-190[»]
    1CKAX-ray1.50A134-190[»]
    1CKBX-ray1.90A134-190[»]
    1JU5NMR-B217-228[»]
    1M30NMR-A134-191[»]
    1M3ANMR-A135-191[»]
    1M3BNMR-A134-191[»]
    1M3CNMR-A132-191[»]
    2GGRNMR-A230-304[»]
    ProteinModelPortaliQ64010.
    SMRiQ64010. Positions 1-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ64010.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 118106SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 19261SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 29660SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.By similarity
    The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB.

    Sequence similaritiesi

    Belongs to the CRK family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 2 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG292767.
    GeneTreeiENSGT00390000001475.
    HOGENOMiHOG000236288.
    HOVERGENiHBG105616.
    InParanoidiQ64010.
    KOiK04438.
    OMAiVIYERRF.
    OrthoDBiEOG7NW69P.
    PhylomeDBiQ64010.
    TreeFamiTF321436.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 3 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Crk-II (identifier: Q64010-1) [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

    MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS    50
    VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL 100
    LEFYKIHYLD TTTLIEPVAR SRQGSGVILR QEEAEYVRAL FDFNGNDEED 150
    LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL 200
    IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA RVIQKRVPNA 250
    YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD 300
    EDFS 304
    Length:304
    Mass (Da):33,815
    Last modified:November 1, 1996 - v1
    Checksum:i5491896FC7A89065
    GO
    Isoform Crk-I (identifier: Q64010-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         205-304: Missing.

    Show »
    Length:204
    Mass (Da):22,847
    Checksum:i35B7AC1188657461
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei205 – 304100Missing in isoform Crk-I. 1 PublicationVSP_004174Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72408 mRNA. Translation: AAB30755.1.
    AK028488 mRNA. Translation: BAC25976.1.
    CCDSiCCDS25055.1. [Q64010-1]
    RefSeqiNP_598417.2. NM_133656.5. [Q64010-1]
    UniGeneiMm.280125.

    Genome annotation databases

    EnsembliENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776. [Q64010-1]
    GeneIDi12928.
    KEGGimmu:12928.
    UCSCiuc007keq.1. mouse. [Q64010-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72408 mRNA. Translation: AAB30755.1 .
    AK028488 mRNA. Translation: BAC25976.1 .
    CCDSi CCDS25055.1. [Q64010-1 ]
    RefSeqi NP_598417.2. NM_133656.5. [Q64010-1 ]
    UniGenei Mm.280125.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B07 X-ray 2.50 A 134-190 [» ]
    1CKA X-ray 1.50 A 134-190 [» ]
    1CKB X-ray 1.90 A 134-190 [» ]
    1JU5 NMR - B 217-228 [» ]
    1M30 NMR - A 134-191 [» ]
    1M3A NMR - A 135-191 [» ]
    1M3B NMR - A 134-191 [» ]
    1M3C NMR - A 132-191 [» ]
    2GGR NMR - A 230-304 [» ]
    ProteinModelPortali Q64010.
    SMRi Q64010. Positions 1-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198887. 25 interactions.
    DIPi DIP-57059N.
    IntActi Q64010. 22 interactions.
    MINTi MINT-4599411.

    PTM databases

    PhosphoSitei Q64010.

    Proteomic databases

    MaxQBi Q64010.
    PaxDbi Q64010.
    PRIDEi Q64010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017920 ; ENSMUSP00000017920 ; ENSMUSG00000017776 . [Q64010-1 ]
    GeneIDi 12928.
    KEGGi mmu:12928.
    UCSCi uc007keq.1. mouse. [Q64010-1 ]

    Organism-specific databases

    CTDi 1398.
    MGIi MGI:88508. Crk.

    Phylogenomic databases

    eggNOGi NOG292767.
    GeneTreei ENSGT00390000001475.
    HOGENOMi HOG000236288.
    HOVERGENi HBG105616.
    InParanoidi Q64010.
    KOi K04438.
    OMAi VIYERRF.
    OrthoDBi EOG7NW69P.
    PhylomeDBi Q64010.
    TreeFami TF321436.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198634. Regulation of signaling by CBL.

    Miscellaneous databases

    EvolutionaryTracei Q64010.
    NextBioi 282592.
    PROi Q64010.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64010.
    Bgeei Q64010.
    CleanExi MM_CRK.
    Genevestigatori Q64010.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 3 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells."
      Ogawa S., Toyoshima H., Kozutsumi H., Hagiwara K., Sakai R., Tanaka T., Hirano N., Mano H., Yazaki Y., Hirai H.
      Oncogene 9:1669-1678(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRK-I AND CRK-II).
      Tissue: Liver.
    2. "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] (ISOFORM CRK-II).
      Strain: C57BL/6J.
      Tissue: Skin.
    3. "c-Abl kinase regulates the protein binding activity of c-Crk."
      Feller S.M., Knudsen B., Hanafusa H.
      EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-221, INTERACTION WITH ABL1.
    4. "An eps homology (EH) domain protein that binds to the ral-GTPase target, RalBP1."
      Yamaguchi A., Urano T., Goi T., Feig L.A.
      J. Biol. Chem. 272:31230-31234(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH REPS1.
      Tissue: Muscle.
    5. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
      Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
      J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT1.
    6. "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
      Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
      Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDEF1/ASAP1.
    7. "Isolation and characterization of novel presenilin binding protein."
      Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q., Dargusch R., Schubert D., Kimura H.
      J. Neurochem. 75:109-116(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK3.
      Tissue: Brain.
    8. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
      Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
      J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHA3.
    9. "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk."
      Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.
      Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
    10. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
      Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
      J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBLB.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk."
      Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D., Hanafusa H., Kuriyan J.
      Structure 3:215-226(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 134-190.
    14. "Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors."
      Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.
      Science 282:2088-2092(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-191.

    Entry informationi

    Entry nameiCRK_MOUSE
    AccessioniPrimary (citable) accession number: Q64010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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