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Q53T59

- H1BP3_HUMAN

UniProt

Q53T59 - H1BP3_HUMAN

Protein

HCLS1-binding protein 3

Gene

HS1BP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: InterPro

    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 – 1391Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphoserine2 Publications
    Modified residuei337 – 3371N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ53T59.
    PaxDbiQ53T59.
    PeptideAtlasiQ53T59.
    PRIDEiQ53T59.

    PTM databases

    PhosphoSiteiQ53T59.

    Expressioni

    Gene expression databases

    ArrayExpressiQ53T59.
    BgeeiQ53T59.
    CleanExiHS_HS1BP3.
    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. 2 interactions.
    STRINGi9606.ENSP00000305193.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53T59.
    SMRiQ53T59. Positions 20-136.
    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.
    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

    MQSPAVLVTS RRLQNAHTGL DLTVPQHQEV RGKMMSGHVE YQILVVTRLA    50
    AFKSAKHRPE DVVQFLVSKK YSEIEEFYQK LSSRYAAASL PPLPRKVLFV 100
    GESDIRERRA VFNEILRCVS KDAELAGSPE LLEFLGTRSP GAAGLTSRDS 150
    SVLDGTDSQT GNDEEAFDFF EEQDQVAEEG PPVQSLKGED AEESLEEEEA 200
    LDPLGIMRSK KPKKHPKVAV KAKPSPRLTI FDEEVDPDEG LFGPGRKLSP 250
    QDPSEDVSSV DPLKLFDDPD LGGAIPLGDS LLLPAACESG GPTPSLSHRD 300
    ASKELFRVEE DLDQILNLGA EPKPKPQLKP KPPVAAKPVI PRKPAVPPKA 350
    GPAEAVAGQQ KPQEQIQAMD EMDILQYIQD HDTPAQAAPS LF 392
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1700.1.
    RefSeqi NP_071905.3. NM_022460.3.
    UniGenei Hs.531785.

    3D structure databases

    ProteinModelPortali Q53T59.
    SMRi Q53T59. Positions 20-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122141. 2 interactions.
    STRINGi 9606.ENSP00000305193.

    PTM databases

    PhosphoSitei Q53T59.

    Polymorphism databases

    DMDMi 74726842.

    Proteomic databases

    MaxQBi Q53T59.
    PaxDbi Q53T59.
    PeptideAtlasi Q53T59.
    PRIDEi Q53T59.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304031 ; ENSP00000305193 ; ENSG00000118960 .
    GeneIDi 64342.
    KEGGi hsa:64342.
    UCSCi uc002rdw.1. human.

    Organism-specific databases

    CTDi 64342.
    GeneCardsi GC02M020760.
    HGNCi HGNC:24979. HS1BP3.
    HPAi HPA035050.
    MIMi 609359. gene.
    neXtProti NX_Q53T59.
    PharmGKBi PA162391602.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG27752.
    HOGENOMi HOG000112839.
    HOVERGENi HBG098900.
    InParanoidi Q53T59.
    OMAi IRDHDTP.
    PhylomeDBi Q53T59.
    TreeFami TF335484.

    Miscellaneous databases

    ChiTaRSi HS1BP3. human.
    GenomeRNAii 64342.
    NextBioi 66275.
    PROi Q53T59.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53T59.
    Bgeei Q53T59.
    CleanExi HS_HS1BP3.
    Genevestigatori Q53T59.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    [Graphical view ]
    Pfami PF00787. PX. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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].

    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: October 1, 2014
    This is version 76 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