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P49710

- HCLS1_MOUSE

UniProt

P49710 - HCLS1_MOUSE

Protein

Hematopoietic lineage cell-specific protein

Gene

Hcls1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein complex binding Source: MGI
    3. SH3 domain binding Source: MGI

    GO - Biological processi

    1. actin filament polymerization Source: InterPro
    2. cellular response to cytokine stimulus Source: Ensembl
    3. erythrocyte differentiation Source: UniProtKB
    4. negative regulation of leukocyte apoptotic process Source: Ensembl
    5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. positive regulation of cell proliferation Source: UniProtKB
    7. positive regulation of granulocyte differentiation Source: BHF-UCL
    8. positive regulation of macrophage differentiation Source: BHF-UCL
    9. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    10. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    11. positive regulation of protein kinase B signaling Source: Ensembl
    12. positive regulation of transcription factor import into nucleus Source: Ensembl
    13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
    15. regulation of actin filament polymerization Source: Ensembl
    16. response to hormone Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hematopoietic lineage cell-specific protein
    Alternative name(s):
    Hematopoietic cell-specific LYN substrate 1
    LckBP1
    Gene namesi
    Name:Hcls1
    Synonyms:Hs1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:104568. Hcls1.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. mitochondrion Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: Ensembl
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi388 – 3881Y → F: Strongly reduces phosphorylation by FES. Abolishes phosphorylation by FES; when associated with F-405. 1 Publication
    Mutagenesisi405 – 4051Y → F: Minor effect on phosphorylation by FES. Abolishes phosphorylation by FES; when associated with F-388. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Hematopoietic lineage cell-specific proteinPRO_0000083922Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-acetyllysineBy similarity
    Modified residuei103 – 1031PhosphotyrosineBy similarity
    Modified residuei123 – 1231N6-acetyllysineBy similarity
    Modified residuei140 – 1401Phosphotyrosine1 Publication
    Modified residuei192 – 1921N6-acetyllysineBy similarity
    Modified residuei198 – 1981PhosphotyrosineBy similarity
    Modified residuei222 – 2221Phosphotyrosine; by FGRBy similarity
    Modified residuei241 – 2411N6-acetyllysineBy similarity
    Modified residuei275 – 2751PhosphoserineBy similarity
    Modified residuei388 – 3881Phosphotyrosine; by SYK and FES1 Publication
    Modified residuei405 – 4051Phosphotyrosine; by SYK and FES1 Publication

    Post-translational modificationi

    Phosphorylated by LYN, FYN and FGR after cross-linking of surface IgM on B-cells. Phosphorylation by LYN, FYN and FGR requires prior phosphorylation by SYK By similarity. Binds to LCK in vivo, and is tyrosine phosphorylated upon TCR stimulation. Phosphorylated by FES.By similarity2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49710.
    PaxDbiP49710.
    PRIDEiP49710.

    PTM databases

    PhosphoSiteiP49710.

    Miscellaneous databases

    PMAP-CutDBP49710.

    Expressioni

    Tissue specificityi

    Expressed only in tissues and cells of hematopoietic origin.

    Gene expression databases

    ArrayExpressiP49710.
    BgeeiP49710.
    CleanExiMM_HCLS1.
    GenevestigatoriP49710.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain) with FGR By similarity. Associates with the SH2 and SH3 domains of LCK. Binding to he LCK SH3 domain occurs constitutively, while binding to the LCK SH2 domain occurs only upon TCR stimulation. A similar binding pattern was observed with LYN, but not with FYN in which the FYN SH2 region associates upon TCR stimulation but the FYN SH3 region does not associate regardless of TCR stimulation. Directly associates with HAX1, through binding to its C-terminal region. Interacts with HS1BP3. Interacts with FES/FPS. Forms a multiprotein complex with LYN and ANKRD54.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LynP2591110EBI-924601,EBI-643537

    Protein-protein interaction databases

    BioGridi200250. 2 interactions.
    IntActiP49710. 4 interactions.
    MINTiMINT-84934.

    Structurei

    3D structure databases

    ProteinModelPortaliP49710.
    SMRiP49710. Positions 431-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati79 – 11537Cortactin 1Add
    BLAST
    Repeati116 – 15237Cortactin 2Add
    BLAST
    Repeati153 – 18937Cortactin 3Add
    BLAST
    Repeati190 – 21223Cortactin 4; truncatedAdd
    BLAST
    Domaini429 – 48658SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 6640Involved in HAX-1 bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 4 cortactin repeats.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG123488.
    GeneTreeiENSGT00530000062953.
    HOGENOMiHOG000006523.
    HOVERGENiHBG005994.
    InParanoidiQ922I8.
    KOiK06106.
    OMAiEMDRHEQ.
    OrthoDBiEOG7V49ZC.
    TreeFamiTF318935.

    Family and domain databases

    InterProiIPR028534. HS1.
    IPR003134. Hs1_Cortactin.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10829:SF5. PTHR10829:SF5. 1 hit.
    PfamiPF02218. HS1_rep. 4 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51090. CORTACTIN. 4 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49710-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE    50
    HINIHQLRNK VSEEHDILKK KELESGPKAS HGYGGRFGVE RDRMDKSAVG 100
    HEYVADVEKH SSQTDAARGF GGKYGVERDR ADKSAVGFDY KGEVEKHASQ 150
    KDYSHGFGGR YGVEKDKRDK AALGYDYKGE TEKHESQRDY AKGFGGQYGI 200
    QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGARGLKA KFESLAEEKR 250
    KREEEEKAQQ MARQQQERKA VVKMSREVQQ PSMPVEEPAA PAQLPKKISS 300
    EVWPPAESHL PPESQPVRSR REYPVPSLPT RQSPLQNHLE DNEEPPALPP 350
    RTPEGLQVVE EPVYEAAPEL EPEPEPDYEP EPETEPDYED VGELDRQDED 400
    AEGDYEDVLE PEDTPSLSYQ AGPSAGAGGA GISAIALYDY QGEGSDELSF 450
    DPDDIITDIE MVDEGWWRGQ CRGHFGLFPA NYVKLL 486
    Length:486
    Mass (Da):54,240
    Last modified:July 27, 2011 - v2
    Checksum:i0EE14FEFA0A31412
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861R → Q in BAA07701. (PubMed:7535527)Curated
    Sequence conflicti86 – 861R → Q in CAA59265. (PubMed:7628441)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42120 mRNA. Translation: BAA07701.1.
    X84797 mRNA. Translation: CAA59265.1.
    BC007469 mRNA. Translation: AAH07469.1.
    CCDSiCCDS37336.1.
    PIRiI49760.
    RefSeqiNP_032251.2. NM_008225.2.
    UniGeneiMm.4091.

    Genome annotation databases

    EnsembliENSMUST00000023531; ENSMUSP00000023531; ENSMUSG00000022831.
    GeneIDi15163.
    KEGGimmu:15163.
    UCSCiuc007zdi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42120 mRNA. Translation: BAA07701.1 .
    X84797 mRNA. Translation: CAA59265.1 .
    BC007469 mRNA. Translation: AAH07469.1 .
    CCDSi CCDS37336.1.
    PIRi I49760.
    RefSeqi NP_032251.2. NM_008225.2.
    UniGenei Mm.4091.

    3D structure databases

    ProteinModelPortali P49710.
    SMRi P49710. Positions 431-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200250. 2 interactions.
    IntActi P49710. 4 interactions.
    MINTi MINT-84934.

    PTM databases

    PhosphoSitei P49710.

    Proteomic databases

    MaxQBi P49710.
    PaxDbi P49710.
    PRIDEi P49710.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023531 ; ENSMUSP00000023531 ; ENSMUSG00000022831 .
    GeneIDi 15163.
    KEGGi mmu:15163.
    UCSCi uc007zdi.2. mouse.

    Organism-specific databases

    CTDi 3059.
    MGIi MGI:104568. Hcls1.

    Phylogenomic databases

    eggNOGi NOG123488.
    GeneTreei ENSGT00530000062953.
    HOGENOMi HOG000006523.
    HOVERGENi HBG005994.
    InParanoidi Q922I8.
    KOi K06106.
    OMAi EMDRHEQ.
    OrthoDBi EOG7V49ZC.
    TreeFami TF318935.

    Miscellaneous databases

    NextBioi 287660.
    PMAP-CutDB P49710.
    PROi P49710.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49710.
    Bgeei P49710.
    CleanExi MM_HCLS1.
    Genevestigatori P49710.

    Family and domain databases

    InterProi IPR028534. HS1.
    IPR003134. Hs1_Cortactin.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10829:SF5. PTHR10829:SF5. 1 hit.
    Pfami PF02218. HS1_rep. 4 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51090. CORTACTIN. 4 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56(lck)."
      Takemoto Y., Furuta M., Li X.-K., Strong-Sparks W.J., Hashimoto Y.
      EMBO J. 14:3403-3414(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thymocyte.
    3. "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/N.
      Tissue: Mammary tumor.
    4. "Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules."
      Takemoto Y., Sato M., Furuta M., Hashimoto Y.
      Int. Immunol. 8:1699-1705(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LCK, BINDING PATTERN OF SERVERAL SRC KINASES.
      Strain: BALB/c.
    5. "Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3."
      Takemoto Y., Furuta M., Sato M., Kubo M., Hashimoto Y.
      Int. Immunol. 11:1957-1964(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HS1BP3.
    6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    7. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
      Samuels A.L., Klinken S.P., Ingley E.
      Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD54.
    8. "Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for coupling to the FcepsilonRI pathway in mast cells."
      McPherson V.A., Everingham S., Karisch R., Smith J.A., Udell C.M., Zheng J., Jia Z., Craig A.W.
      Mol. Cell. Biol. 29:389-401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FES/FPS, PHOSPHORYLATION AT TYR-388 AND TYR-405, MUTAGENESIS OF TYR-388 AND TYR-405.

    Entry informationi

    Entry nameiHCLS1_MOUSE
    AccessioniPrimary (citable) accession number: P49710
    Secondary accession number(s): Q922I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 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, 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