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Q9BW71

- HIRP3_HUMAN

UniProt

Q9BW71 - HIRP3_HUMAN

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Protein

HIRA-interacting protein 3

Gene
HIRIP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones.1 Publication

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. chromatin assembly or disassembly Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
HIRA-interacting protein 3
Gene namesi
Name:HIRIP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4917. HIRIP3.

Subcellular locationi

Nucleus
Note: Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis.1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29294.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556HIRA-interacting protein 3PRO_0000083989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei84 – 841Phosphothreonine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei100 – 1001Phosphoserine1 Publication
Modified residuei125 – 1251Phosphoserine4 Publications
Modified residuei142 – 1421Phosphoserine2 Publications
Modified residuei143 – 1431Phosphoserine2 Publications
Modified residuei159 – 1591Phosphoserine4 Publications
Modified residuei160 – 1601Phosphoserine4 Publications
Modified residuei196 – 1961Phosphoserine5 Publications
Modified residuei199 – 1991Phosphoserine4 Publications
Modified residuei223 – 2231Phosphoserine4 Publications
Modified residuei227 – 2271Phosphoserine6 Publications
Modified residuei289 – 2891Phosphoserine3 Publications
Modified residuei291 – 2911Phosphoserine3 Publications
Modified residuei330 – 3301Phosphoserine3 Publications
Modified residuei332 – 3321Phosphoserine3 Publications
Modified residuei333 – 3331Phosphoserine3 Publications
Modified residuei357 – 3571Phosphoserine2 Publications
Modified residuei358 – 3581Phosphothreonine2 Publications
Modified residuei359 – 3591Phosphoserine2 Publications
Modified residuei363 – 3631Phosphoserine3 Publications
Modified residuei370 – 3701Phosphoserine3 Publications
Modified residuei372 – 3721Phosphoserine2 Publications
Modified residuei550 – 5501Phosphoserine1 Publication
Modified residuei551 – 5511Phosphoserine1 Publication
Modified residuei555 – 5551Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CK2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BW71.
PaxDbiQ9BW71.
PRIDEiQ9BW71.

PTM databases

PhosphoSiteiQ9BW71.

Expressioni

Tissue specificityi

Widely expressed. Isoform 1 is predominant in skeletal muscle. Isoform 2 is predominant in liver and heart.1 Publication

Gene expression databases

ArrayExpressiQ9BW71.
BgeeiQ9BW71.
CleanExiHS_HIRIP3.
GenevestigatoriQ9BW71.

Interactioni

Subunit structurei

Interacts with HIRA. Weak interaction with histones H2B and H3. Interacts with CK2.2 Publications

Protein-protein interaction databases

BioGridi114053. 29 interactions.
IntActiQ9BW71. 6 interactions.
MINTiMINT-1411245.
STRINGi9606.ENSP00000279392.

Structurei

3D structure databases

ProteinModelPortaliQ9BW71.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi129 – 253125Glu-richAdd
BLAST
Compositional biasi398 – 4036Poly-Ser

Phylogenomic databases

eggNOGiNOG25729.
HOGENOMiHOG000112903.
HOVERGENiHBG066199.
InParanoidiQ9BW71.
OMAiDPERKRF.
OrthoDBiEOG790G1V.
PhylomeDBiQ9BW71.
TreeFamiTF331753.

Family and domain databases

InterProiIPR019098. Histone_chaperone_domain_CHZ.
[Graphical view]
PfamiPF09649. CHZ. 1 hit.
[Graphical view]
SMARTiSM01082. CHZ. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BW71-1) [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

MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL    50
KRLVEEELLK MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES 100
ESGSEASSPD YFGPPAKNGV AAEVSPAKEE NPRRASKAVE ESSDEERQRD 150
LPAQRGEESS EEEEKGYKGK TRKKPVVKKQ APGKASVSRK QAREESEESE 200
AEPVQRTAKK VEGNKGTKSL KESEQESEEE ILAQKKEQRE EEVEEEEKEE 250
DEEKGDWKPR TRSNGRRKSA REERSCKQKS QAKRLLGDSD SEEEQKEAAS 300
SGDDSGRDRE PPVQRKSEDR TQLKGGKRLS GSSEDEEDSG KGEPTAKGSR 350
KMARLGSTSG EESDLEREVS DSEAGGGPQG ERKNRSSKKS SRKGRTRSSS 400
SSSDGSPEAK GGKAGSGRRG EDHPAVMRLK RYIRACGAHR NYKKLLGSCC 450
SHKERLSILR AELEALGMKG TPSLGKCRAL KEQREEAAEV ASLDVANIIS 500
GSGRPRRRTA WNPLGEAAPP GELYRRTLDS DEERPRPAPP DWSHMRGIIS 550
SDGESN 556
Length:556
Mass (Da):61,957
Last modified:October 17, 2006 - v3
Checksum:iACABE2E0032B8C13
GO
Isoform 2 (identifier: Q9BW71-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-413: Missing.

Show »
Length:243
Mass (Da):27,612
Checksum:i6DE219CC60F3BAB8
GO
Isoform 3 (identifier: Q9BW71-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-175: ESGSEASSPD...GYKGKTRKKP → GWLRSPWRGP...GPEGAEGGGS
     176-556: Missing.

Note: No experimental confirmation available.

Show »
Length:175
Mass (Da):19,709
Checksum:i8E6D1E89AC91F6BF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti496 – 4961A → V.
Corresponds to variant rs35431046 [ dbSNP | Ensembl ].
VAR_051033
Natural varianti521 – 5211G → W.
Corresponds to variant rs11643314 [ dbSNP | Ensembl ].
VAR_028115

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 413313Missing in isoform 2. VSP_003877Add
BLAST
Alternative sequencei101 – 17575ESGSE…TRKKP → GWLRSPWRGPPGCDEAEALH SGLWCPSKLQEAVGLLLLTQ GAPEYPPGRTGSARHEGYPF PREVSGPEGAEGGGS in isoform 3. VSP_046024Add
BLAST
Alternative sequencei176 – 556381Missing in isoform 3. VSP_046025Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581L → P in CAA11273. 1 Publication
Sequence conflicti58 – 581L → P in CAA11274. 1 Publication
Sequence conflicti58 – 581L → P in CAA11275. 1 Publication
Sequence conflicti58 – 581L → P1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223349 mRNA. Translation: CAA11273.1.
AJ223350 mRNA. Translation: CAA11274.1.
AJ223351 mRNA. Translation: CAA11275.2.
BX393533 mRNA. No translation available.
AC093512 Genomic DNA. No translation available.
BC000588 mRNA. Translation: AAH00588.1.
CCDSiCCDS10664.1. [Q9BW71-1]
CCDS58449.1. [Q9BW71-3]
RefSeqiNP_001184252.1. NM_001197323.1. [Q9BW71-3]
NP_003600.2. NM_003609.4. [Q9BW71-1]
UniGeneiHs.567370.

Genome annotation databases

EnsembliENST00000279392; ENSP00000279392; ENSG00000149929. [Q9BW71-1]
ENST00000564026; ENSP00000456824; ENSG00000149929. [Q9BW71-3]
GeneIDi8479.
KEGGihsa:8479.
UCSCiuc002dve.3. human. [Q9BW71-1]

Polymorphism databases

DMDMi116242511.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ223349 mRNA. Translation: CAA11273.1 .
AJ223350 mRNA. Translation: CAA11274.1 .
AJ223351 mRNA. Translation: CAA11275.2 .
BX393533 mRNA. No translation available.
AC093512 Genomic DNA. No translation available.
BC000588 mRNA. Translation: AAH00588.1 .
CCDSi CCDS10664.1. [Q9BW71-1 ]
CCDS58449.1. [Q9BW71-3 ]
RefSeqi NP_001184252.1. NM_001197323.1. [Q9BW71-3 ]
NP_003600.2. NM_003609.4. [Q9BW71-1 ]
UniGenei Hs.567370.

3D structure databases

ProteinModelPortali Q9BW71.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114053. 29 interactions.
IntActi Q9BW71. 6 interactions.
MINTi MINT-1411245.
STRINGi 9606.ENSP00000279392.

PTM databases

PhosphoSitei Q9BW71.

Polymorphism databases

DMDMi 116242511.

Proteomic databases

MaxQBi Q9BW71.
PaxDbi Q9BW71.
PRIDEi Q9BW71.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000279392 ; ENSP00000279392 ; ENSG00000149929 . [Q9BW71-1 ]
ENST00000564026 ; ENSP00000456824 ; ENSG00000149929 . [Q9BW71-3 ]
GeneIDi 8479.
KEGGi hsa:8479.
UCSCi uc002dve.3. human. [Q9BW71-1 ]

Organism-specific databases

CTDi 8479.
GeneCardsi GC16M030005.
HGNCi HGNC:4917. HIRIP3.
MIMi 603365. gene.
neXtProti NX_Q9BW71.
PharmGKBi PA29294.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG25729.
HOGENOMi HOG000112903.
HOVERGENi HBG066199.
InParanoidi Q9BW71.
OMAi DPERKRF.
OrthoDBi EOG790G1V.
PhylomeDBi Q9BW71.
TreeFami TF331753.

Miscellaneous databases

GeneWikii HIRIP3.
GenomeRNAii 8479.
NextBioi 31725.
PROi Q9BW71.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BW71.
Bgeei Q9BW71.
CleanExi HS_HIRIP3.
Genevestigatori Q9BW71.

Family and domain databases

InterProi IPR019098. Histone_chaperone_domain_CHZ.
[Graphical view ]
Pfami PF09649. CHZ. 1 hit.
[Graphical view ]
SMARTi SM01082. CHZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA."
    Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y., Almouzni G., Lipinski M.
    Mol. Cell. Biol. 18:5546-5556(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH HIRA, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2."
    Assrir N., Filhol O., Galisson F., Lipinski M.
    Biol. Chem. 388:391-398(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CK2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  3. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Neuroblastoma.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Skin.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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 THR-84; SER-87; SER-196; SER-227 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-100; SER-159; SER-160; SER-223; SER-227; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-125; SER-196; SER-199; SER-223; SER-227; SER-363; SER-370 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-159; SER-160; SER-196; SER-199; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-550; SER-551 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHIRP3_HUMAN
AccessioniPrimary (citable) accession number: Q9BW71
Secondary accession number(s): H3BSR3, O75707, O75708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 109 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

External Data

Dasty 3

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