Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hematopoietic lineage cell-specific protein

Gene

HCLS1

Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

  1. protein kinase binding Source: BHF-UCL
  2. 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
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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 – 2751Phosphoserine2 Publications
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 similarity3 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

BgeeiP14317.
CleanExiHS_HCLS1.
ExpressionAtlasiP14317. baseline and differential.
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.
GeneTreeiENSGT00530000062953.
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. AlignAdd to basket

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

        10         20         30         40         50
MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE
60 70 80 90 100
HINIHQLRNK VSEEHDVLRK KEMESGPKAS HGYGGRFGVE RDRMDKSAVG
110 120 130 140 150
HEYVAEVEKH SSQTDAAKGF GGKYGVERDR ADKSAVGFDY KGEVEKHTSQ
160 170 180 190 200
KDYSRGFGGR YGVEKDKWDK AALGYDYKGE TEKHESQRDY AKGFGGQYGI
210 220 230 240 250
QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGTRGLKA KFESMAEEKR
260 270 280 290 300
KREEEEKAQQ VARRQQERKA VTKRSPEAPQ PVIAMEEPAV PAPLPKKISS
310 320 330 340 350
EAWPPVGTPP SSESEPVRTS REHPVPLLPI RQTLPEDNEE PPALPPRTLE
360 370 380 390 400
GLQVEEEPVY EAEPEPEPEP EPEPENDYED VEEMDRHEQE DEPEGDYEEV
410 420 430 440 450
LEPEDSSFSS ALAGSSGCPA GAGAGAVALG ISAVAVYDYQ GEGSDELSFD
460 470 480
PDDVITDIEM VDEGWWRGRC HGHFGLFPAN YVKLLE
Length:486
Mass (Da):54,014
Last modified:January 10, 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 (Ref. 4) Curated

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:
EMBLi
GenBanki
DDBJi
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. [P14317-1]
PIRiS07633.
RefSeqiNP_001278970.1. NM_001292041.1.
NP_005326.2. NM_005335.5.
UniGeneiHs.14601.

Genome annotation databases

EnsembliENST00000314583; ENSP00000320176; ENSG00000180353. [P14317-1]
ENST00000495491; ENSP00000418299; ENSG00000180353. [P14317-2]
GeneIDi3059.
KEGGihsa:3059.
UCSCiuc003eeh.4. human. [P14317-1]

Polymorphism databases

DMDMi317373440.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P14317-1]
PIRiS07633.
RefSeqiNP_001278970.1. NM_001292041.1.
NP_005326.2. NM_005335.5.
UniGeneiHs.14601.

3D structure databases

ProteinModelPortaliP14317.
SMRiP14317. Positions 429-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP14317.

Polymorphism databases

DMDMi317373440.

Proteomic databases

MaxQBiP14317.
PaxDbiP14317.
PRIDEiP14317.

Protocols and materials databases

DNASUi3059.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314583; ENSP00000320176; ENSG00000180353. [P14317-1]
ENST00000495491; ENSP00000418299; ENSG00000180353. [P14317-2]
GeneIDi3059.
KEGGihsa:3059.
UCSCiuc003eeh.4. human. [P14317-1]

Organism-specific databases

CTDi3059.
GeneCardsiGC03M121350.
HGNCiHGNC:4844. HCLS1.
HPAiHPA019143.
MIMi601306. gene.
neXtProtiNX_P14317.
PharmGKBiPA29220.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG123488.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000006523.
HOVERGENiHBG005994.
InParanoidiP14317.
KOiK06106.
OMAiEMDRHEQ.
OrthoDBiEOG7V49ZC.
PhylomeDBiP14317.
TreeFamiTF318935.

Miscellaneous databases

ChiTaRSiHCLS1. human.
GenomeRNAii3059.
NextBioi12103.
PMAP-CutDBP14317.
PROiP14317.
SOURCEiSearch...

Gene expression databases

BgeeiP14317.
CleanExiHS_HCLS1.
ExpressionAtlasiP14317. baseline and differential.
GenevestigatoriP14317.

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. "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(1988) [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 (APR-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(2003) [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 (MAY-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(2005) [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(2003) [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(1992) [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(1995) [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(1995) [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(1996) [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(1998) [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(2003) [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(2008) [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(2008) [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].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: December 31, 1989
Last sequence update: January 10, 2011
Last modified: March 3, 2015
This is version 164 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

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.