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P14317

- HCLS1_HUMAN

UniProt

P14317 - HCLS1_HUMAN

Protein

Hematopoietic lineage cell-specific protein

Gene

HCLS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (11 Jan 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.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase binding Source: BHF-UCL
    3. RNA polymerase II transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. actin filament polymerization Source: InterPro
    2. cellular response to cytokine stimulus Source: BHF-UCL
    3. erythrocyte differentiation Source: UniProtKB
    4. intracellular signal transduction Source: ProtInc
    5. negative regulation of leukocyte apoptotic process Source: BHF-UCL
    6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
    8. positive regulation of cell proliferation Source: UniProtKB
    9. positive regulation of granulocyte differentiation Source: BHF-UCL
    10. positive regulation of macrophage differentiation Source: Ensembl
    11. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    12. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    13. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    14. positive regulation of protein kinase B signaling Source: BHF-UCL
    15. positive regulation of transcription factor import into nucleus Source: BHF-UCL
    16. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    17. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
    18. regulation of actin filament polymerization Source: BHF-UCL
    19. regulation of transcription, DNA-templated Source: ProtInc
    20. 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
    p75
    Gene namesi
    Name:HCLS1
    Synonyms:HS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4844. HCLS1.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29220.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Hematopoietic lineage cell-specific proteinPRO_0000083921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-acetyllysine1 Publication
    Modified residuei103 – 1031Phosphotyrosine
    Modified residuei123 – 1231N6-acetyllysine1 Publication
    Modified residuei140 – 1401PhosphotyrosineBy similarity
    Modified residuei192 – 1921N6-acetyllysine1 Publication
    Modified residuei198 – 1981Phosphotyrosine2 Publications
    Modified residuei222 – 2221Phosphotyrosine; by FGR2 Publications
    Modified residuei241 – 2411N6-acetyllysine1 Publication
    Modified residuei275 – 2751Phosphoserine1 Publication
    Modified residuei308 – 3081Phosphothreonine1 Publication
    Modified residuei378 – 3781Phosphotyrosine; by SYK and FESBy similarity
    Modified residuei397 – 3971Phosphotyrosine; by SYK and FESBy similarity

    Post-translational modificationi

    Phosphorylated by FES By similarity. 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 or FES.By similarity6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP14317.
    PaxDbiP14317.
    PRIDEiP14317.

    PTM databases

    PhosphoSiteiP14317.

    Miscellaneous databases

    PMAP-CutDBP14317.

    Expressioni

    Tissue specificityi

    Expressed only in tissues and cells of hematopoietic origin.

    Developmental stagei

    Expressed in early stage of myeloid and erythroid differentiation.

    Gene expression databases

    ArrayExpressiP14317.
    BgeeiP14317.
    CleanExiHS_HCLS1.
    GenevestigatoriP14317.

    Organism-specific databases

    HPAiHPA019143.

    Interactioni

    Subunit structurei

    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 By similarity. Interacts (via SH2 domain) with FGR. Forms a multiprotein complex with LYN and ANKRD54 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WIPF1O435162EBI-750369,EBI-346356

    Protein-protein interaction databases

    BioGridi109309. 21 interactions.
    IntActiP14317. 14 interactions.
    MINTiMINT-1343660.
    STRINGi9606.ENSP00000320176.

    Structurei

    3D structure databases

    ProteinModelPortaliP14317.
    SMRiP14317. Positions 429-484.
    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
    Domaini428 – 48659SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 6640Involved in HAX-1 bindingAdd
    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.
    HOGENOMiHOG000006523.
    HOVERGENiHBG005994.
    InParanoidiP14317.
    KOiK06106.
    OMAiEMDRHEQ.
    OrthoDBiEOG7V49ZC.
    PhylomeDBiP14317.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14317-1) [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

    MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE    50
    HINIHQLRNK VSEEHDVLRK KEMESGPKAS HGYGGRFGVE RDRMDKSAVG 100
    HEYVAEVEKH SSQTDAAKGF GGKYGVERDR ADKSAVGFDY KGEVEKHTSQ 150
    KDYSRGFGGR YGVEKDKWDK AALGYDYKGE TEKHESQRDY AKGFGGQYGI 200
    QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGTRGLKA KFESMAEEKR 250
    KREEEEKAQQ VARRQQERKA VTKRSPEAPQ PVIAMEEPAV PAPLPKKISS 300
    EAWPPVGTPP SSESEPVRTS REHPVPLLPI RQTLPEDNEE PPALPPRTLE 350
    GLQVEEEPVY EAEPEPEPEP EPEPENDYED VEEMDRHEQE DEPEGDYEEV 400
    LEPEDSSFSS ALAGSSGCPA GAGAGAVALG ISAVAVYDYQ GEGSDELSFD 450
    PDDVITDIEM VDEGWWRGRC HGHFGLFPAN YVKLLE 486
    Length:486
    Mass (Da):54,014
    Last modified:January 11, 2011 - v3
    Checksum:i20AE72A28DA33DFB
    GO
    Isoform 2 (identifier: P14317-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-209: SAVGFDYKGE...IQKDRVDKSA → ITLVALVAGT...RPQLIRRRRP
         210-486: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:209
    Mass (Da):24,008
    Checksum:i41DA8B0C0178CA56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2422KF → FK AA sequence (PubMed:8713105)Curated
    Sequence conflicti486 – 4861E → D in CAG33075. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti235 – 2351T → A.5 Publications
    Corresponds to variant rs2070179 [ dbSNP | Ensembl ].
    VAR_055006
    Natural varianti361 – 3611E → K.
    Corresponds to variant rs2070180 [ dbSNP | Ensembl ].
    VAR_055007
    Natural varianti436 – 4361V → L.5 Publications
    Corresponds to variant rs9869984 [ dbSNP | Ensembl ].
    VAR_056910

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 20976SAVGF…VDKSA → ITLVALVAGTGWRRINGTKQ LWDMTTRERRRNTSPREIMP RALVASMESRRTEWIRALSA SMKWRPRPQLIRRRRP in isoform 2. 1 PublicationVSP_056429Add
    BLAST
    Alternative sequencei210 – 486277Missing in isoform 2. 1 PublicationVSP_056430Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16663 mRNA. Translation: CAA34651.1.
    BT006824 mRNA. Translation: AAP35470.1.
    AK298663 mRNA. Translation: BAG60831.1.
    AK312750 mRNA. Translation: BAG35617.1.
    CR456794 mRNA. Translation: CAG33075.1.
    AC133750 Genomic DNA. No translation available.
    BC016758 mRNA. Translation: AAH16758.1.
    CCDSiCCDS3003.1.
    PIRiS07633.
    UniGeneiHs.14601.

    Genome annotation databases

    EnsembliENST00000314583; ENSP00000320176; ENSG00000180353.
    ENST00000495491; ENSP00000418299; ENSG00000180353.
    KEGGihsa:3059.
    UCSCiuc003eeh.4. human.

    Polymorphism databases

    DMDMi317373440.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16663 mRNA. Translation: CAA34651.1 .
    BT006824 mRNA. Translation: AAP35470.1 .
    AK298663 mRNA. Translation: BAG60831.1 .
    AK312750 mRNA. Translation: BAG35617.1 .
    CR456794 mRNA. Translation: CAG33075.1 .
    AC133750 Genomic DNA. No translation available.
    BC016758 mRNA. Translation: AAH16758.1 .
    CCDSi CCDS3003.1.
    PIRi S07633.
    UniGenei Hs.14601.

    3D structure databases

    ProteinModelPortali P14317.
    SMRi P14317. Positions 429-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109309. 21 interactions.
    IntActi P14317. 14 interactions.
    MINTi MINT-1343660.
    STRINGi 9606.ENSP00000320176.

    PTM databases

    PhosphoSitei P14317.

    Polymorphism databases

    DMDMi 317373440.

    Proteomic databases

    MaxQBi P14317.
    PaxDbi P14317.
    PRIDEi P14317.

    Protocols and materials databases

    DNASUi 3059.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314583 ; ENSP00000320176 ; ENSG00000180353 .
    ENST00000495491 ; ENSP00000418299 ; ENSG00000180353 .
    KEGGi hsa:3059.
    UCSCi uc003eeh.4. human.

    Organism-specific databases

    CTDi 3059.
    GeneCardsi GC03M121350.
    HGNCi HGNC:4844. HCLS1.
    HPAi HPA019143.
    MIMi 601306. gene.
    neXtProti NX_P14317.
    PharmGKBi PA29220.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG123488.
    HOGENOMi HOG000006523.
    HOVERGENi HBG005994.
    InParanoidi P14317.
    KOi K06106.
    OMAi EMDRHEQ.
    OrthoDBi EOG7V49ZC.
    PhylomeDBi P14317.
    TreeFami TF318935.

    Miscellaneous databases

    ChiTaRSi HCLS1. human.
    GenomeRNAii 3059.
    NextBioi 12103.
    PMAP-CutDB P14317.
    PROi P14317.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14317.
    Bgeei P14317.
    CleanExi HS_HCLS1.
    Genevestigatori P14317.

    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. "Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage."
      Kitamura D., Kaneko H., Miyagoe Y., Ariyasu T., Watanabe T.
      Nucleic Acids Res. 17:9367-9379(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-235 AND LEU-436.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-235 AND LEU-436.
    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] (ISOFORMS 1 AND 2), VARIANTS ALA-235 AND LEU-436.
      Tissue: Spleen.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-235 AND LEU-436.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1), VARIANTS ALA-235 AND LEU-436.
      Tissue: Lymph.
    7. "Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling."
      Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S., Toyoshima K., Kitamura D., Watanabe T., Yamamoto T.
      Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-26; 79-95; 134-146; 208-223 AND 274-289, INTERACTION WITH LYN, SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Tissue: B-cell lymphoma.
    8. "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
      Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
      Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 97-108; 193-201 AND 240-248.
    9. "SH2 domains mediate the sequential phosphorylation of HS1 protein by p72syk and Src-related protein tyrosine kinases."
      Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.
      Biochemistry 35:5327-5332(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, PHOSPHORYLATION BY SYK; LYN; FYN AND FGR.
    10. "HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases."
      Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., Watanabe T.
      J. Immunol. 158:2736-2744(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAX1.
    11. "Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein-tyrosine kinase."
      Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A., Marin O., Pinna L.A.
      J. Biol. Chem. 274:7557-7564(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FGR.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 TYR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-275 AND THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-41; LYS-123; LYS-192 AND LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHCLS1_HUMAN
    AccessioniPrimary (citable) accession number: P14317
    Secondary accession number(s): B4DQ69
    , Q53Y93, Q6IBK9, Q9UDK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3