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Protein

Hematopoietic lineage cell-specific protein

Gene

Hcls1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 complex binding Source: MGI
  2. protein kinase binding Source: MGI
  3. RNA polymerase II transcription factor binding Source: MGI
  4. SH3 domain binding Source: MGI

GO - Biological processi

  1. actin filament polymerization Source: InterPro
  2. cellular response to cytokine stimulus Source: MGI
  3. erythrocyte differentiation Source: UniProtKB
  4. negative regulation of leukocyte apoptotic process Source: MGI
  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: MGI
  10. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  11. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  12. positive regulation of protein kinase B signaling Source: MGI
  13. positive regulation of transcription factor import into nucleus Source: MGI
  14. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
  16. regulation of actin filament polymerization Source: MGI
  17. response to hormone Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:104568. Hcls1.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrion Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. transcription factor complex Source: MGI
Complete GO annotation...

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 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 similarity1 Publication

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

BgeeiP49710.
CleanExiMM_HCLS1.
ExpressionAtlasiP49710. baseline and differential.
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.
InParanoidiP49710.
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

        10         20         30         40         50
MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE
60 70 80 90 100
HINIHQLRNK VSEEHDILKK KELESGPKAS HGYGGRFGVE RDRMDKSAVG
110 120 130 140 150
HEYVADVEKH SSQTDAARGF GGKYGVERDR ADKSAVGFDY KGEVEKHASQ
160 170 180 190 200
KDYSHGFGGR YGVEKDKRDK AALGYDYKGE TEKHESQRDY AKGFGGQYGI
210 220 230 240 250
QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGARGLKA KFESLAEEKR
260 270 280 290 300
KREEEEKAQQ MARQQQERKA VVKMSREVQQ PSMPVEEPAA PAQLPKKISS
310 320 330 340 350
EVWPPAESHL PPESQPVRSR REYPVPSLPT RQSPLQNHLE DNEEPPALPP
360 370 380 390 400
RTPEGLQVVE EPVYEAAPEL EPEPEPDYEP EPETEPDYED VGELDRQDED
410 420 430 440 450
AEGDYEDVLE PEDTPSLSYQ AGPSAGAGGA GISAIALYDY QGEGSDELSF
460 470 480
DPDDIITDIE MVDEGWWRGQ CRGHFGLFPA NYVKLL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP49710.

Proteomic databases

MaxQBiP49710.
PaxDbiP49710.
PRIDEiP49710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3059.
MGIiMGI:104568. Hcls1.

Phylogenomic databases

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiP49710.
KOiK06106.
OMAiEMDRHEQ.
OrthoDBiEOG7V49ZC.
TreeFamiTF318935.

Miscellaneous databases

NextBioi287660.
PMAP-CutDBP49710.
PROiP49710.
SOURCEiSearch...

Gene expression databases

BgeeiP49710.
CleanExiMM_HCLS1.
ExpressionAtlasiP49710. baseline and differential.
GenevestigatoriP49710.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 127 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.