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Q9BW71 (HIRP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HIRA-interacting protein 3
Gene names
Name:HIRIP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with HIRA. Weak interaction with histones H2B and H3. Interacts with CK2. Ref.1 Ref.2

Subcellular location

Nucleus. Note: Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis. Ref.2

Tissue specificity

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

Post-translational modification

Phosphorylated by CK2. Ref.2

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin assembly or disassembly

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BW71-1)

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.
Isoform 2 (identifier: Q9BW71-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-413: Missing.
Isoform 3 (identifier: Q9BW71-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556HIRA-interacting protein 3
PRO_0000083989

Regions

Compositional bias129 – 253125Glu-rich
Compositional bias398 – 4036Poly-Ser

Amino acid modifications

Modified residue271Phosphoserine Ref.11
Modified residue841Phosphothreonine Ref.7
Modified residue871Phosphoserine Ref.7
Modified residue981Phosphoserine Ref.9
Modified residue1001Phosphoserine Ref.9
Modified residue1251Phosphoserine Ref.6 Ref.11 Ref.12 Ref.14
Modified residue1421Phosphoserine Ref.6 Ref.14
Modified residue1431Phosphoserine Ref.6 Ref.14
Modified residue1591Phosphoserine Ref.6 Ref.9 Ref.12 Ref.14
Modified residue1601Phosphoserine Ref.6 Ref.9 Ref.12 Ref.14
Modified residue1961Phosphoserine Ref.6 Ref.7 Ref.11 Ref.12 Ref.14
Modified residue1991Phosphoserine Ref.6 Ref.11 Ref.12 Ref.14
Modified residue2231Phosphoserine Ref.6 Ref.9 Ref.11 Ref.14
Modified residue2271Phosphoserine Ref.6 Ref.7 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue2891Phosphoserine Ref.6 Ref.12 Ref.14
Modified residue2911Phosphoserine Ref.6 Ref.12 Ref.14
Modified residue3301Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue3321Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue3331Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue3571Phosphoserine Ref.9 Ref.14
Modified residue3581Phosphothreonine Ref.9 Ref.14
Modified residue3591Phosphoserine Ref.9 Ref.14
Modified residue3631Phosphoserine Ref.9 Ref.11 Ref.14
Modified residue3701Phosphoserine Ref.7 Ref.11 Ref.14
Modified residue3721Phosphoserine Ref.9 Ref.11
Modified residue5501Phosphoserine Ref.12
Modified residue5511Phosphoserine Ref.12
Modified residue5551Phosphoserine Ref.12

Natural variations

Alternative sequence101 – 413313Missing in isoform 2.
VSP_003877
Alternative sequence101 – 17575ESGSE…TRKKP → GWLRSPWRGPPGCDEAEALH SGLWCPSKLQEAVGLLLLTQ GAPEYPPGRTGSARHEGYPF PREVSGPEGAEGGGS in isoform 3.
VSP_046024
Alternative sequence176 – 556381Missing in isoform 3.
VSP_046025
Natural variant4961A → V.
Corresponds to variant rs35431046 [ dbSNP | Ensembl ].
VAR_051033
Natural variant5211G → W.
Corresponds to variant rs11643314 [ dbSNP | Ensembl ].
VAR_028115

Experimental info

Sequence conflict581L → P in CAA11273. Ref.1
Sequence conflict581L → P in CAA11274. Ref.1
Sequence conflict581L → P in CAA11275. Ref.1
Sequence conflict581L → P Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: ACABE2E0032B8C13

FASTA55661,957
        10         20         30         40         50         60 
MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL KRLVEEELLK 

        70         80         90        100        110        120 
MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES ESGSEASSPD YFGPPAKNGV 

       130        140        150        160        170        180 
AAEVSPAKEE NPRRASKAVE ESSDEERQRD LPAQRGEESS EEEEKGYKGK TRKKPVVKKQ 

       190        200        210        220        230        240 
APGKASVSRK QAREESEESE AEPVQRTAKK VEGNKGTKSL KESEQESEEE ILAQKKEQRE 

       250        260        270        280        290        300 
EEVEEEEKEE DEEKGDWKPR TRSNGRRKSA REERSCKQKS QAKRLLGDSD SEEEQKEAAS 

       310        320        330        340        350        360 
SGDDSGRDRE PPVQRKSEDR TQLKGGKRLS GSSEDEEDSG KGEPTAKGSR KMARLGSTSG 

       370        380        390        400        410        420 
EESDLEREVS DSEAGGGPQG ERKNRSSKKS SRKGRTRSSS SSSDGSPEAK GGKAGSGRRG 

       430        440        450        460        470        480 
EDHPAVMRLK RYIRACGAHR NYKKLLGSCC SHKERLSILR AELEALGMKG TPSLGKCRAL 

       490        500        510        520        530        540 
KEQREEAAEV ASLDVANIIS GSGRPRRRTA WNPLGEAAPP GELYRRTLDS DEERPRPAPP 

       550 
DWSHMRGIIS SDGESN 

« Hide

Isoform 2 [UniParc].

Checksum: 6DE219CC60F3BAB8
Show »

FASTA24327,612
Isoform 3 [UniParc].

Checksum: 8E6D1E89AC91F6BF
Show »

FASTA17519,709

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10664.1. [Q9BW71-1]
CCDS58449.1. [Q9BW71-3]
RefSeqNP_001184252.1. NM_001197323.1. [Q9BW71-3]
NP_003600.2. NM_003609.4. [Q9BW71-1]
UniGeneHs.567370.

3D structure databases

ProteinModelPortalQ9BW71.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114053. 29 interactions.
IntActQ9BW71. 6 interactions.
MINTMINT-1411245.
STRING9606.ENSP00000279392.

PTM databases

PhosphoSiteQ9BW71.

Polymorphism databases

DMDM116242511.

Proteomic databases

MaxQBQ9BW71.
PaxDbQ9BW71.
PRIDEQ9BW71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279392; ENSP00000279392; ENSG00000149929. [Q9BW71-1]
ENST00000564026; ENSP00000456824; ENSG00000149929. [Q9BW71-3]
GeneID8479.
KEGGhsa:8479.
UCSCuc002dve.3. human. [Q9BW71-1]

Organism-specific databases

CTD8479.
GeneCardsGC16M030005.
HGNCHGNC:4917. HIRIP3.
MIM603365. gene.
neXtProtNX_Q9BW71.
PharmGKBPA29294.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG25729.
HOGENOMHOG000112903.
HOVERGENHBG066199.
InParanoidQ9BW71.
OMADPERKRF.
OrthoDBEOG790G1V.
PhylomeDBQ9BW71.
TreeFamTF331753.

Gene expression databases

ArrayExpressQ9BW71.
BgeeQ9BW71.
CleanExHS_HIRIP3.
GenevestigatorQ9BW71.

Family and domain databases

InterProIPR019098. Histone_chaperone_domain_CHZ.
[Graphical view]
PfamPF09649. CHZ. 1 hit.
[Graphical view]
SMARTSM01082. CHZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHIRIP3.
GenomeRNAi8479.
NextBio31725.
PROQ9BW71.
SOURCESearch...

Entry information

Entry nameHIRP3_HUMAN
AccessionPrimary (citable) accession number: Q9BW71
Secondary accession number(s): H3BSR3, O75707, O75708
Entry history
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 statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM