Q9BW71 (HIRP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
HIRA-interacting protein 3

Gene names

Name:

HIRIP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin assembly or disassembly Traceable author statement Ref.1. Source: ProtInc
Cellular_component	nucleus Inferred from direct assay Ref.2. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 556	556	HIRA-interacting protein 3		PRO_0000083989
Regions
	Compositional bias	129 – 253	125	Glu-rich
	Compositional bias	398 – 403	6	Poly-Ser
Amino acid modifications
	Modified residue	27	1	Phosphoserine Ref.10
	Modified residue	84	1	Phosphothreonine Ref.7
	Modified residue	87	1	Phosphoserine Ref.7
	Modified residue	98	1	Phosphoserine Ref.9
	Modified residue	100	1	Phosphoserine Ref.9
	Modified residue	125	1	Phosphoserine Ref.6 Ref.10 Ref.11 Ref.13
	Modified residue	142	1	Phosphoserine Ref.6 Ref.13
	Modified residue	143	1	Phosphoserine Ref.6 Ref.13
	Modified residue	159	1	Phosphoserine Ref.6 Ref.9 Ref.11 Ref.13
	Modified residue	160	1	Phosphoserine Ref.6 Ref.9 Ref.11 Ref.13
	Modified residue	196	1	Phosphoserine Ref.6 Ref.7 Ref.10 Ref.11 Ref.13
	Modified residue	199	1	Phosphoserine Ref.6 Ref.10 Ref.11 Ref.13
	Modified residue	223	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.13
	Modified residue	227	1	Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13
	Modified residue	289	1	Phosphoserine Ref.6 Ref.11 Ref.13
	Modified residue	291	1	Phosphoserine Ref.6 Ref.11 Ref.13
	Modified residue	330	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	332	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	333	1	Phosphoserine Ref.9 Ref.11 Ref.13
	Modified residue	357	1	Phosphoserine Ref.9 Ref.13
	Modified residue	358	1	Phosphothreonine Ref.9 Ref.13
	Modified residue	359	1	Phosphoserine Ref.9 Ref.13
	Modified residue	363	1	Phosphoserine Ref.9 Ref.10 Ref.13
	Modified residue	370	1	Phosphoserine Ref.7 Ref.10 Ref.13
	Modified residue	372	1	Phosphoserine Ref.9 Ref.10
	Modified residue	550	1	Phosphoserine Ref.11
	Modified residue	551	1	Phosphoserine Ref.11
	Modified residue	555	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	101 – 413	313	Missing in isoform 2.		VSP_003877
	Alternative sequence	101 – 175	75	ESGSE…TRKKP → GWLRSPWRGPPGCDEAEALH SGLWCPSKLQEAVGLLLLTQ GAPEYPPGRTGSARHEGYPF PREVSGPEGAEGGGS in isoform 3.		VSP_046024
	Alternative sequence	176 – 556	381	Missing in isoform 3.		VSP_046025
	Natural variant	496	1	A → V. Corresponds to variant rs35431046 [ dbSNP | Ensembl ].		VAR_051033
	Natural variant	521	1	G → W. Corresponds to variant rs11643314 [ dbSNP | Ensembl ].		VAR_028115
Experimental info
	Sequence conflict	58	1	L → P in CAA11273. Ref.1
	Sequence conflict	58	1	L → P in CAA11274. Ref.1
	Sequence conflict	58	1	L → P in CAA11275. Ref.1
	Sequence conflict	58	1	L → P Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: ACABE2E0032B8C13	FASTA	556	61,957
	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
	Isoform 2 [UniParc]. Checksum: 6DE219CC60F3BAB8	FASTA	243	27,612
	10 20 30 40 50 60 MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL KRLVEEELLK 70 80 90 100 110 120 MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES AGSGRRGEDH PAVMRLKRYI 130 140 150 160 170 180 RACGAHRNYK KLLGSCCSHK ERLSILRAEL EALGMKGTPS LGKCRALKEQ REEAAEVASL 190 200 210 220 230 240 DVANIISGSG RPRRRTAWNP LGEAAPPGEL YRRTLDSDEE RPRPAPPDWS HMRGIISSDG ESN
	Isoform 3 [UniParc]. Checksum: 8E6D1E89AC91F6BF	FASTA	175	19,709
	10 20 30 40 50 60 MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL KRLVEEELLK 70 80 90 100 110 120 MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES GWLRSPWRGP PGCDEAEALH 130 140 150 160 170 SGLWCPSKLQ EAVGLLLLTQ GAPEYPPGRT GSARHEGYPF PREVSGPEGA EGGGS

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00304875. IPI00413871.
RefSeq	NP_001184252.1. NM_001197323.1. NP_003600.2. NM_003609.4.
UniGene	Hs.567370.
3D structure databases
ProteinModelPortal	Q9BW71.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BW71. 4 interactions.
MINT	MINT-1411245.
STRING	9606.ENSP00000279392.
PTM databases
PhosphoSite	Q9BW71.
Polymorphism databases
DMDM	116242511.
Proteomic databases
PaxDb	Q9BW71.
PRIDE	Q9BW71.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000279392; ENSP00000279392; ENSG00000149929. ENST00000564026; ENSP00000456824; ENSG00000149929.
GeneID	8479.
KEGG	hsa:8479.
UCSC	uc002dve.3. human.
Organism-specific databases
CTD	8479.
GeneCards	GC16M030005.
HGNC	HGNC:4917. HIRIP3.
MIM	603365. gene.
neXtProt	NX_Q9BW71.
PharmGKB	PA29294.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG25729.
HOGENOM	HOG000112903.
HOVERGEN	HBG066199.
InParanoid	Q9BW71.
OMA	FRFNSES.
OrthoDB	EOG4M65HN.
PhylomeDB	Q9BW71.
Gene expression databases
ArrayExpress	Q9BW71.
Bgee	Q9BW71.
CleanEx	HS_HIRIP3.
Genevestigator	Q9BW71.
GermOnline	ENSG00000149929. Homo sapiens.
Family and domain databases
InterPro	IPR019098. Histone_chaperone_domain_CHZ. [Graphical view]
Pfam	PF09649. CHZ. 1 hit. [Graphical view]
SMART	SM01082. CHZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8479.
NextBio	31725.
SOURCE	Search...

Entry information

Entry name

HIRP3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.