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

HCLS1-binding protein 3

Gene

HS1BP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be a modulator of IL-2 signaling.By similarity

GO - Molecular functioni

  1. phosphatidylinositol binding Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
HCLS1-binding protein 3
Alternative name(s):
HS1-binding protein 3
Short name:
HSP1BP-3
Gene namesi
Name:HS1BP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:24979. HS1BP3.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392HCLS1-binding protein 3PRO_0000313802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei3 – 31Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine2 Publications
Modified residuei194 – 1941Phosphoserine2 Publications
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei337 – 3371N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ53T59.
PaxDbiQ53T59.
PeptideAtlasiQ53T59.
PRIDEiQ53T59.

PTM databases

PhosphoSiteiQ53T59.

Expressioni

Gene expression databases

BgeeiQ53T59.
CleanExiHS_HS1BP3.
ExpressionAtlasiQ53T59. baseline and differential.
GenevestigatoriQ53T59.

Organism-specific databases

HPAiHPA035050.

Interactioni

Subunit structurei

Binds HCLS1. Interacts with the SH3 domain of HCLS1 in vitro (By similarity).By similarity

Protein-protein interaction databases

BioGridi122141. 5 interactions.
STRINGi9606.ENSP00000305193.

Structurei

3D structure databases

ProteinModelPortaliQ53T59.
SMRiQ53T59. Positions 19-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 142124PXPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi196 – 1994Poly-Glu
Compositional biasi212 – 23726Pro-richAdd
BLAST
Compositional biasi324 – 35229Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG27752.
GeneTreeiENSGT00390000013092.
HOGENOMiHOG000112839.
HOVERGENiHBG098900.
InParanoidiQ53T59.
OMAiIRDHDTP.
PhylomeDBiQ53T59.
TreeFamiTF335484.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
[Graphical view]
PfamiPF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53T59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSPAVLVTS RRLQNAHTGL DLTVPQHQEV RGKMMSGHVE YQILVVTRLA
60 70 80 90 100
AFKSAKHRPE DVVQFLVSKK YSEIEEFYQK LSSRYAAASL PPLPRKVLFV
110 120 130 140 150
GESDIRERRA VFNEILRCVS KDAELAGSPE LLEFLGTRSP GAAGLTSRDS
160 170 180 190 200
SVLDGTDSQT GNDEEAFDFF EEQDQVAEEG PPVQSLKGED AEESLEEEEA
210 220 230 240 250
LDPLGIMRSK KPKKHPKVAV KAKPSPRLTI FDEEVDPDEG LFGPGRKLSP
260 270 280 290 300
QDPSEDVSSV DPLKLFDDPD LGGAIPLGDS LLLPAACESG GPTPSLSHRD
310 320 330 340 350
ASKELFRVEE DLDQILNLGA EPKPKPQLKP KPPVAAKPVI PRKPAVPPKA
360 370 380 390
GPAEAVAGQQ KPQEQIQAMD EMDILQYIQD HDTPAQAAPS LF
Length:392
Mass (Da):42,780
Last modified:May 24, 2005 - v1
Checksum:i2A360915F833FAE8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti260 – 2601V → M.2 Publications
Corresponds to variant rs2305458 [ dbSNP | Ensembl ].
VAR_037741
Natural varianti273 – 2731G → R.
Corresponds to variant rs35589938 [ dbSNP | Ensembl ].
VAR_037742
Natural varianti348 – 3481P → R.
Corresponds to variant rs35579164 [ dbSNP | Ensembl ].
VAR_037743
Natural varianti388 – 3881A → T.1 Publication
Corresponds to variant rs3732149 [ dbSNP | Ensembl ].
VAR_037744

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK314383 mRNA. Translation: BAG37009.1.
AC012065 Genomic DNA. Translation: AAX93235.1.
CH471053 Genomic DNA. Translation: EAX00814.1.
CH471053 Genomic DNA. Translation: EAX00816.1.
BC050636 mRNA. Translation: AAH50636.1.
CCDSiCCDS1700.1.
RefSeqiNP_071905.3. NM_022460.3.
UniGeneiHs.531785.

Genome annotation databases

EnsembliENST00000304031; ENSP00000305193; ENSG00000118960.
GeneIDi64342.
KEGGihsa:64342.
UCSCiuc002rdw.1. human.

Polymorphism databases

DMDMi74726842.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK314383 mRNA. Translation: BAG37009.1.
AC012065 Genomic DNA. Translation: AAX93235.1.
CH471053 Genomic DNA. Translation: EAX00814.1.
CH471053 Genomic DNA. Translation: EAX00816.1.
BC050636 mRNA. Translation: AAH50636.1.
CCDSiCCDS1700.1.
RefSeqiNP_071905.3. NM_022460.3.
UniGeneiHs.531785.

3D structure databases

ProteinModelPortaliQ53T59.
SMRiQ53T59. Positions 19-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122141. 5 interactions.
STRINGi9606.ENSP00000305193.

PTM databases

PhosphoSiteiQ53T59.

Polymorphism databases

DMDMi74726842.

Proteomic databases

MaxQBiQ53T59.
PaxDbiQ53T59.
PeptideAtlasiQ53T59.
PRIDEiQ53T59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304031; ENSP00000305193; ENSG00000118960.
GeneIDi64342.
KEGGihsa:64342.
UCSCiuc002rdw.1. human.

Organism-specific databases

CTDi64342.
GeneCardsiGC02M020760.
HGNCiHGNC:24979. HS1BP3.
HPAiHPA035050.
MIMi609359. gene.
neXtProtiNX_Q53T59.
PharmGKBiPA162391602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG27752.
GeneTreeiENSGT00390000013092.
HOGENOMiHOG000112839.
HOVERGENiHBG098900.
InParanoidiQ53T59.
OMAiIRDHDTP.
PhylomeDBiQ53T59.
TreeFamiTF335484.

Miscellaneous databases

ChiTaRSiHS1BP3. human.
GenomeRNAii64342.
NextBioi66275.
PROiQ53T59.
SOURCEiSearch...

Gene expression databases

BgeeiQ53T59.
CleanExiHS_HS1BP3.
ExpressionAtlasiQ53T59. baseline and differential.
GenevestigatoriQ53T59.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
[Graphical view]
PfamiPF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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], VARIANT MET-260.
    Tissue: Uterus.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS MET-260 AND THR-388.
    Tissue: Brain.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiH1BP3_HUMAN
AccessioniPrimary (citable) accession number: Q53T59
Secondary accession number(s): B2RAW2
, D6W529, Q86VC2, Q8N367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 24, 2005
Last modified: March 4, 2015
This is version 79 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.