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Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1)

 HCLS1_MOUSE             Reviewed;         486 AA.
P49710; Q922I8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=Hematopoietic lineage cell-specific protein;
AltName: Full=Hematopoietic cell-specific LYN substrate 1;
AltName: Full=LckBP1;
Name=Hcls1; Synonyms=Hs1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7535527; DOI=10.1006/bbrc.1995.1452;
Kitamura D., Kaneko H., Taniuchi I., Yamamura K., Watanabe T.;
"Molecular cloning and characterization of mouse HS1.";
Biochem. Biophys. Res. Commun. 208:1137-1146(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymocyte;
PubMed=7628441;
Takemoto Y., Furuta M., Li X.-K., Strong-Sparks W.J., Hashimoto Y.;
"LckBP1, a proline-rich protein expressed in haematopoietic lineage
cells, directly associates with the SH3 domain of protein tyrosine
kinase p56(lck).";
EMBO J. 14:3403-3414(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH LCK, AND BINDING PATTERN OF SERVERAL SRC KINASES.
STRAIN=BALB/cJ;
PubMed=8943564; DOI=10.1093/intimm/8.11.1699;
Takemoto Y., Sato M., Furuta M., Hashimoto Y.;
"Distinct binding patterns of HS1 to the Src SH2 and SH3 domains
reflect possible mechanisms of recruitment and activation of
downstream molecules.";
Int. Immunol. 8:1699-1705(1996).
[5]
INTERACTION WITH HS1BP3.
PubMed=10590261; DOI=10.1093/intimm/11.12.1957;
Takemoto Y., Furuta M., Sato M., Kubo M., Hashimoto Y.;
"Isolation and characterization of a novel HS1 SH3 domain binding
protein, HS1BP3.";
Int. Immunol. 11:1957-1964(1999).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
INTERACTION WITH ANKRD54.
PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
Samuels A.L., Klinken S.P., Ingley E.;
"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
influences erythropoietin-induced differentiation.";
Blood 113:3845-3856(2009).
[8]
INTERACTION WITH FES/FPS, PHOSPHORYLATION AT TYR-388 AND TYR-405, AND
MUTAGENESIS OF TYR-388 AND TYR-405.
PubMed=19001085; DOI=10.1128/MCB.00904-08;
McPherson V.A., Everingham S., Karisch R., Smith J.A., Udell C.M.,
Zheng J., Jia Z., Craig A.W.;
"Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase
for coupling to the FcepsilonRI pathway in mast cells.";
Mol. Cell. Biol. 29:389-401(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330 AND SER-333, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:10590261,
ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19064729,
ECO:0000269|PubMed:8943564}.
-!- INTERACTION:
P25911:Lyn; NbExp=10; IntAct=EBI-924601, EBI-643537;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed only in tissues and cells of
hematopoietic origin.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:19001085}.
-----------------------------------------------------------------------
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EMBL; D42120; BAA07701.1; -; mRNA.
EMBL; X84797; CAA59265.1; -; mRNA.
EMBL; BC007469; AAH07469.1; -; mRNA.
CCDS; CCDS37336.1; -.
PIR; I49760; I49760.
RefSeq; NP_032251.2; NM_008225.2.
UniGene; Mm.4091; -.
ProteinModelPortal; P49710; -.
SMR; P49710; -.
BioGrid; 200250; 2.
IntAct; P49710; 4.
MINT; P49710; -.
STRING; 10090.ENSMUSP00000023531; -.
MoonDB; P49710; Predicted.
iPTMnet; P49710; -.
PhosphoSitePlus; P49710; -.
SwissPalm; P49710; -.
EPD; P49710; -.
MaxQB; P49710; -.
PaxDb; P49710; -.
PeptideAtlas; P49710; -.
PRIDE; P49710; -.
Ensembl; ENSMUST00000023531; ENSMUSP00000023531; ENSMUSG00000022831.
GeneID; 15163; -.
KEGG; mmu:15163; -.
UCSC; uc007zdi.2; mouse.
CTD; 3059; -.
MGI; MGI:104568; Hcls1.
eggNOG; ENOG410IFV2; Eukaryota.
eggNOG; ENOG410XTAK; LUCA.
GeneTree; ENSGT00530000062953; -.
HOGENOM; HOG000006523; -.
HOVERGEN; HBG005994; -.
InParanoid; P49710; -.
KO; K06106; -.
OMA; YEDVEEM; -.
OrthoDB; EOG091G0CPX; -.
TreeFam; TF318935; -.
PMAP-CutDB; P49710; -.
PRO; PR:P49710; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022831; Expressed in 89 organ(s), highest expression level in spleen.
CleanEx; MM_HCLS1; -.
ExpressionAtlas; P49710; baseline and differential.
Genevisible; P49710; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0003779; F:actin binding; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:BHF-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
InterPro; IPR028534; HS1.
InterPro; IPR003134; Hs1_Cortactin.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10829:SF5; PTHR10829:SF5; 2.
Pfam; PF02218; HS1_rep; 4.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51090; CORTACTIN; 4.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Mitochondrion; Phosphoprotein;
Reference proteome; Repeat; SH3 domain.
CHAIN 1 486 Hematopoietic lineage cell-specific
protein.
/FTId=PRO_0000083922.
REPEAT 79 115 Cortactin 1.
REPEAT 116 152 Cortactin 2.
REPEAT 153 189 Cortactin 3.
REPEAT 190 212 Cortactin 4; truncated.
DOMAIN 429 486 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 27 66 Involved in HAX-1 binding. {ECO:0000250}.
MOD_RES 41 41 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 140 140 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 192 192 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 198 198 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 222 222 Phosphotyrosine; by FGR.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 241 241 N6-acetyllysine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:P14317}.
MOD_RES 330 330 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 388 388 Phosphotyrosine; by SYK and FES.
{ECO:0000305|PubMed:19001085}.
MOD_RES 405 405 Phosphotyrosine; by SYK and FES.
{ECO:0000305|PubMed:19001085}.
MUTAGEN 388 388 Y->F: Strongly reduces phosphorylation by
FES. Abolishes phosphorylation by FES;
when associated with F-405.
{ECO:0000269|PubMed:19001085}.
MUTAGEN 405 405 Y->F: Minor effect on phosphorylation by
FES. Abolishes phosphorylation by FES;
when associated with F-388.
{ECO:0000269|PubMed:19001085}.
CONFLICT 86 86 R -> Q (in Ref. 1; BAA07701 and 2;
CAA59265). {ECO:0000305}.
SEQUENCE 486 AA; 54240 MW; 0EE14FEFA0A31412 CRC64;
MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE HINIHQLRNK
VSEEHDILKK KELESGPKAS HGYGGRFGVE RDRMDKSAVG HEYVADVEKH SSQTDAARGF
GGKYGVERDR ADKSAVGFDY KGEVEKHASQ KDYSHGFGGR YGVEKDKRDK AALGYDYKGE
TEKHESQRDY AKGFGGQYGI QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGARGLKA
KFESLAEEKR KREEEEKAQQ MARQQQERKA VVKMSREVQQ PSMPVEEPAA PAQLPKKISS
EVWPPAESHL PPESQPVRSR REYPVPSLPT RQSPLQNHLE DNEEPPALPP RTPEGLQVVE
EPVYEAAPEL EPEPEPDYEP EPETEPDYED VGELDRQDED AEGDYEDVLE PEDTPSLSYQ
AGPSAGAGGA GISAIALYDY QGEGSDELSF DPDDIITDIE MVDEGWWRGQ CRGHFGLFPA
NYVKLL


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