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Q60749

- KHDR1_MOUSE

UniProt

Q60749 - KHDR1_MOUSE

Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 1

Gene

Khdrbs1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species.3 Publications

    GO - Molecular functioni

    1. poly(A) binding Source: MGI
    2. poly(U) RNA binding Source: MGI
    3. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB
    5. SH3/SH2 adaptor activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell surface receptor signaling pathway Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: MGI
    4. positive regulation of RNA export from nucleus Source: UniProtKB
    5. positive regulation of signal transduction Source: GOC
    6. positive regulation of translational initiation Source: UniProtKB
    7. regulation of RNA export from nucleus Source: MGI
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KH domain-containing, RNA-binding, signal transduction-associated protein 1
    Alternative name(s):
    GAP-associated tyrosine phosphoprotein p62
    Src-associated in mitosis 68 kDa protein
    Short name:
    Sam68
    p21 Ras GTPase-activating protein-associated p62
    p68
    Gene namesi
    Name:Khdrbs1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:893579. Khdrbs1.

    Subcellular locationi

    Nucleus 1 Publication. Membrane 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. Grb2-Sos complex Source: Ensembl
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1PRO_0000050125Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201PhosphoserineBy similarity
    Modified residuei21 – 211N6-acetyllysine1 Publication
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei45 – 451Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei45 – 451Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei52 – 521Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei52 – 521Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei58 – 581PhosphoserineBy similarity
    Modified residuei113 – 1131Phosphoserine1 Publication
    Modified residuei175 – 1751N6-acetyllysineBy similarity
    Modified residuei291 – 2911Omega-N-methylated arginine; by PRMT1By similarity
    Modified residuei304 – 3041Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei304 – 3041Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei310 – 3101Omega-N-methylarginine; alternateBy similarity
    Modified residuei310 – 3101Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei315 – 3151Omega-N-methylarginine; alternateBy similarity
    Modified residuei315 – 3151Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei320 – 3201Dimethylated arginine; alternateBy similarity
    Modified residuei320 – 3201Omega-N-methylarginine; alternateBy similarity
    Modified residuei320 – 3201Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei325 – 3251Omega-N-methylarginine; alternateBy similarity
    Modified residuei325 – 3251Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei331 – 3311Dimethylated arginine; alternateBy similarity
    Modified residuei331 – 3311Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei340 – 3401Omega-N-methylarginine; alternateBy similarity
    Modified residuei340 – 3401Omega-N-methylated arginine; by PRMT1; alternateBy similarity
    Modified residuei346 – 3461Omega-N-methylated arginine; by PRMT1By similarity
    Modified residuei435 – 4351Phosphotyrosine; by PTK6By similarity
    Modified residuei440 – 4401Phosphotyrosine; by PTK6By similarity
    Modified residuei443 – 4431Phosphotyrosine; by PTK6By similarity

    Post-translational modificationi

    Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1.1 Publication
    Acetylated. Positively correlates with ability to bind RNA By similarity.By similarity
    Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ60749.
    PaxDbiQ60749.
    PRIDEiQ60749.

    PTM databases

    PhosphoSiteiQ60749.

    Expressioni

    Gene expression databases

    BgeeiQ60749.
    GenevestigatoriQ60749.

    Interactioni

    Subunit structurei

    Self-associates to form homooligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions. Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA By similarity. Interacts with PTK6 (via SH3 and SH2 domains). Does not interact with TPR By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CrebbpP454817EBI-519077,EBI-296306
    FynP3968813EBI-519077,EBI-524514
    Prmt1Q9JIF02EBI-519077,EBI-519055

    Protein-protein interaction databases

    BioGridi203068. 14 interactions.
    DIPiDIP-2861N.
    IntActiQ60749. 12 interactions.
    MINTiMINT-1613905.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60749.
    SMRiQ60749. Positions 98-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini171 – 19727KHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 418Pro-richSequence Analysis
    Compositional biasi44 – 5512Arg/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi59 – 8931Pro-richSequence AnalysisAdd
    BLAST
    Compositional biasi282 – 29211Arg/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi295 – 3017Pro-richSequence Analysis
    Compositional biasi302 – 33231Arg/Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi334 – 36330Pro-richSequence AnalysisAdd
    BLAST

    Domaini

    The KH domain is required for binding to RNA.1 Publication
    The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methylation on these motifs can modulate protein-protein interactions By similarity.By similarity

    Sequence similaritiesi

    Belongs to the KHDRBS family.Sequence Analysis
    Contains 1 KH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiCOG5176.
    GeneTreeiENSGT00550000074434.
    HOVERGENiHBG079164.
    InParanoidiB2KG38.
    KOiK13198.
    OMAiFMELSYL.
    OrthoDBiEOG75MVX3.
    PhylomeDBiQ60749.
    TreeFamiTF314878.

    Family and domain databases

    Gene3Di3.30.1370.10. 1 hit.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF00013. KH_1. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60749-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG    50
    PRGGARASPA TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE 100
    NKYLPELMAE KDSLDPSFTH AMQLLSVEIE KIQKGESKKD DEENYLDLFS 150
    HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK 200
    GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE 250
    VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV 300
    PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA 350
    GIQRIPLPPT PAPETYEDYG YDDTYAEQSY EGYEGYYSQS QGESEYYDYG 400
    HGELQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY 443
    Length:443
    Mass (Da):48,371
    Last modified:April 12, 2005 - v2
    Checksum:iD33DE960BEA9E5AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041L → P in AAA64997. (PubMed:7799925)Curated
    Sequence conflicti147 – 1471D → N AA sequence (PubMed:7512695)Curated
    Sequence conflicti174 – 1741G → R in AAA86693. (PubMed:7541765)Curated
    Sequence conflicti197 – 1971V → VS in AAA86693. (PubMed:7541765)Curated
    Sequence conflicti225 – 2306MDLHVF → LGENGL AA sequence (PubMed:7512695)Curated
    Sequence conflicti327 – 3271A → S in AAA86693. (PubMed:7541765)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17961 mRNA. Translation: AAA86693.1.
    U17046 mRNA. Translation: AAA64997.1.
    AK050520 mRNA. Translation: BAC34303.1.
    AK152084 mRNA. Translation: BAE30934.1.
    AL669834 Genomic DNA. Translation: CAM13766.1.
    CU210913 Genomic DNA. Translation: CAQ51789.1.
    BC002051 mRNA. Translation: AAH02051.1.
    CCDSiCCDS18703.1.
    PIRiI49140.
    S43974.
    RefSeqiNP_035447.3. NM_011317.4.
    UniGeneiMm.489797.
    Mm.8256.

    Genome annotation databases

    EnsembliENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790.
    ENSMUST00000129342; ENSMUSP00000115402; ENSMUSG00000028790.
    GeneIDi20218.
    KEGGimmu:20218.
    UCSCiuc008uyd.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17961 mRNA. Translation: AAA86693.1 .
    U17046 mRNA. Translation: AAA64997.1 .
    AK050520 mRNA. Translation: BAC34303.1 .
    AK152084 mRNA. Translation: BAE30934.1 .
    AL669834 Genomic DNA. Translation: CAM13766.1 .
    CU210913 Genomic DNA. Translation: CAQ51789.1 .
    BC002051 mRNA. Translation: AAH02051.1 .
    CCDSi CCDS18703.1.
    PIRi I49140.
    S43974.
    RefSeqi NP_035447.3. NM_011317.4.
    UniGenei Mm.489797.
    Mm.8256.

    3D structure databases

    ProteinModelPortali Q60749.
    SMRi Q60749. Positions 98-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203068. 14 interactions.
    DIPi DIP-2861N.
    IntActi Q60749. 12 interactions.
    MINTi MINT-1613905.

    PTM databases

    PhosphoSitei Q60749.

    Proteomic databases

    MaxQBi Q60749.
    PaxDbi Q60749.
    PRIDEi Q60749.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000066257 ; ENSMUSP00000066516 ; ENSMUSG00000028790 .
    ENSMUST00000129342 ; ENSMUSP00000115402 ; ENSMUSG00000028790 .
    GeneIDi 20218.
    KEGGi mmu:20218.
    UCSCi uc008uyd.2. mouse.

    Organism-specific databases

    CTDi 10657.
    MGIi MGI:893579. Khdrbs1.

    Phylogenomic databases

    eggNOGi COG5176.
    GeneTreei ENSGT00550000074434.
    HOVERGENi HBG079164.
    InParanoidi B2KG38.
    KOi K13198.
    OMAi FMELSYL.
    OrthoDBi EOG75MVX3.
    PhylomeDBi Q60749.
    TreeFami TF314878.

    Miscellaneous databases

    ChiTaRSi KHDRBS1. mouse.
    NextBioi 297827.
    PROi Q60749.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q60749.
    Genevestigatori Q60749.

    Family and domain databases

    Gene3Di 3.30.1370.10. 1 hit.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF00013. KH_1. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and cDNA sequence of a murine protein homologous to the human p62 tyrosine phosphoprotein that associates with the Ras GTPase-activating protein p120 GAP."
      Agger R., Freimuth P.
      Gene 158:307-308(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-120 AND 139-150.
      Strain: BALB/c X DBA/2Imported.
      Tissue: Dendritic cell1 Publication.
    2. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1."
      Richard S., Yu D., Blumer K.J., Hausladen D., Olszowy M.W., Connelly P.A., Shaw A.S.
      Mol. Cell. Biol. 15:186-197(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYN; GRB2 AND PLCG1.
      Tissue: ThymusImported.
    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/6JImported.
      Tissue: Bone marrow and PancreasImported.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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].
      Strain: FVB/NImported.
      Tissue: Mammary glandImported.
    6. Cited for: PROTEIN SEQUENCE OF 57-71; 103-131; 139-152; 158-165; 222-230; 273-282 AND 433-443, FUNCTION, PHOSPHORYLATION AT SER-113, INTERACTION WITH SRC.
    7. "Self-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain."
      Chen T., Damaj B.B., Herrera C., Lasko P., Richard S.
      Mol. Cell. Biol. 17:5707-5718(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, HOMOOLIGOMERIZATION.
    8. "A mammalian germ cell-specific RNA-binding protein interacts with ubiquitously expressed proteins involved in splice site selection."
      Elliott D.J., Bourgeois C.F., Klink A., Stevenin J., Cooke H.J.
      Proc. Natl. Acad. Sci. U.S.A. 97:5717-5722(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBMY1A1.
    9. "Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68."
      Hong W., Resnick R.J., Rakowski C., Shalloway D., Taylor S.J., Blobel G.A.
      Mol. Cancer Res. 1:48-55(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBP.
    10. "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1."
      Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.
      Mol. Biol. Cell 14:274-287(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT1.
    11. "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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKHDR1_MOUSE
    AccessioniPrimary (citable) accession number: Q60749
    Secondary accession number(s): A2ACH3
    , B2KG38, Q3U8T3, Q60735, Q7M4N5, Q99M33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3