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P54198 (HIRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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:
Protein HIRA
Alternative name(s):
TUP1-like enhancer of split protein 1
Gene names
Name:HIRA
Synonyms:DGCR1, HIR, TUPLE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1017 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. Ref.9 Ref.11 Ref.12

Subunit structure

Interacts with histone H3F3B, PAX3 and PAX7 By similarity. Interacts with CCNA1, HIRIP3, NFU1/HIRIP5 and histone H2B. Part of a complex which includes ASF1A, CABIN1, histone H3.3, histone H4 and UBN1. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16

Subcellular location

Nucleus. NucleusPML body. Note: Primarily, though not exclusively, localized to the nucleus. Localizes to PML bodies immediately prior to onset of senescence. Ref.7 Ref.8 Ref.9 Ref.12

Tissue specificity

Expressed at high levels in kidney, pancreas and skeletal muscle and at lower levels in brain, heart, liver, lung, and placenta. Ref.6

Developmental stage

Expressed during embryogenesis.

Post-translational modification

Sumoylated. Ref.13

Phosphorylated by CDK2/CCNA1 and CDK2/CCNE1 on Thr-555 in vitro. Also phosphorylated on Thr-555 and Ser-687 in vivo. Ref.8

Sequence similarities

Belongs to the WD repeat HIR1 family.

Contains 7 WD repeats.

Sequence caution

The sequence CAA53044.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA54721.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA57436.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication-independent nucleosome assembly

Inferred from direct assay Ref.11. Source: UniProt

anatomical structure morphogenesis

Traceable author statement Ref.1. Source: ProtInc

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

gastrulation

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 9731536. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear chromatin

Inferred from direct assay Ref.11. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.7. Source: ProtInc

protein complex

Inferred from direct assay Ref.11. Source: UniProt

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11342215Ref.7. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 9731536. Source: ProtInc

transcription corepressor activity

Traceable author statement PubMed 9731536. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P54198-1)

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 Short (identifier: P54198-2)

The sequence of this isoform differs from the canonical sequence as follows:
     593-799: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10171017Protein HIRA
PRO_0000051019

Regions

Repeat11 – 5343WD 1
Repeat68 – 10740WD 2
Repeat129 – 16840WD 3
Repeat172 – 21140WD 4
Repeat220 – 26344WD 5
Repeat266 – 32257WD 6
Repeat326 – 36742WD 7
Region421 – 729309Interaction with CCNA1
Region421 – 47959Interaction with ASF1A
Region439 – 47537Required for repression of histone gene transcription
Region593 – 826234Interaction with histone H2B
Region594 – 739146Interaction with PAX3 By similarity
Region738 – 1017280Interaction with histone H4
Region740 – 82889Interaction with PAX3 By similarity
Compositional bias408 – 4125Poly-Gln
Compositional bias640 – 6434Poly-Lys
Compositional bias805 – 8084Poly-Val

Amino acid modifications

Modified residue5491Phosphoserine Ref.17
Modified residue5551Phosphothreonine; by CDK2 Ref.8
Modified residue5571Phosphoserine Ref.17
Modified residue5761Phosphothreonine Ref.17
Modified residue5841Phosphoserine Ref.14
Modified residue5861Phosphothreonine Ref.14 Ref.17 Ref.18
Modified residue6101Phosphoserine Ref.19
Modified residue6111Phosphoserine Ref.19
Modified residue6121Phosphoserine Ref.19
Modified residue6141Phosphoserine Ref.19
Modified residue6611Phosphoserine Ref.18 Ref.19
Modified residue6871Phosphoserine Ref.8

Natural variations

Alternative sequence593 – 799207Missing in isoform Short.
VSP_006772

Experimental info

Mutagenesis449 – 45810Missing: Impairs binding to ASF1A. Ref.20
Mutagenesis458 – 4603RRR → AKK: Abrogates binding to ASF1A. Ref.20
Mutagenesis458 – 4603RRR → KKK: Impairs binding to ASF1A. Ref.20
Mutagenesis458 – 4592RR → AK: Impairs binding to ASF1A. Ref.20
Mutagenesis4581R → A: Impairs binding to ASF1A.
Mutagenesis4581R → K: Impairs binding to ASF1A; when associated with K-460.
Mutagenesis459 – 46810Missing: Abrogates binding to ASF1A. Ref.20
Mutagenesis4591R → A: Abrogates binding to ASF1A. Ref.20
Mutagenesis4601R → A: Abrogates binding to ASF1A. Ref.20
Mutagenesis4601R → K: Impairs binding to ASF1A; when associated with K-458. Ref.20
Mutagenesis4611I → D: Abrogates binding to ASF1A. Ref.20
Mutagenesis4641L → D: Impairs binding to ASF1A. Ref.20
Mutagenesis4661I → D: Impairs binding to ASF1A. Ref.20
Mutagenesis5551T → A: Impairs phosphorylation by CDK2. Ref.8
Mutagenesis628 – 6314KRKL → AAAA: Impairs binding to CCNA1 and phosphorylation by CDK2. Ref.8
Sequence conflict91V → G in CAA54721. Ref.1
Sequence conflict8891I → N in CAA54721. Ref.1
Sequence conflict8891I → N in CAA57436. Ref.1
Sequence conflict8891I → N in CAA61979. Ref.2
Sequence conflict9901L → M in CAA53044. Ref.5

Secondary structure

..... 1017
Helix Strand Turn

Details...

Sequences

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

Last modified February 21, 2006. Version 2.
Checksum: 475784B2FF9D16D6

FASTA1,017111,835
        10         20         30         40         50         60 
MKLLKPTWVN HNGKPIFSVD IHPDGTKFAT GGQGQDSGKV VIWNMSPVLQ EDDEKDENIP 

        70         80         90        100        110        120 
KMLCQMDNHL ACVNCVRWSN SGMYLASGGD DKLIMVWKRA TYIGPSTVFG SSGKLANVEQ 

       130        140        150        160        170        180 
WRCVSILRNH SGDVMDVAWS PHDAWLASCS VDNTVVIWNA VKFPEILATL RGHSGLVKGL 

       190        200        210        220        230        240 
TWDPVGKYIA SQADDRSLKV WRTLDWQLET SITKPFDECG GTTHVLRLSW SPDGHYLVSA 

       250        260        270        280        290        300 
HAMNNSGPTA QIIEREGWKT NMDFVGHRKA VTVVKFNPKI FKKKQKNGSS AKPSCPYCCC 

       310        320        330        340        350        360 
AVGSKDRSLS VWLTCLKRPL VVIHELFDKS IMDISWTLNG LGILVCSMDG SVAFLDFSQD 

       370        380        390        400        410        420 
ELGDPLSEEE KSRIHQSTYG KSLAIMTEAQ LSTAVIENPE MLKYQRRQQQ QQLDQKSAAT 

       430        440        450        460        470        480 
REMGSATSVA GVVNGESLED IRKNLLKKQV ETRTADGRRR ITPLCIAQLD TGDFSTAFFN 

       490        500        510        520        530        540 
SIPLSGSLAG TMLSSHSSPQ LLPLDSSTPN SFGASKPCTE PVVAASARPA GDSVNKDSMN 

       550        560        570        580        590        600 
ATSTPAALSP SVLTTPSKIE PMKAFDSRFT ERSKATPGAP ALTSMTPTAV ERLKEQNLVK 

       610        620        630        640        650        660 
ELRPRDLLES SSDSDEKVPL AKASSLSKRK LELEVETVEK KKKGRPRKDS RLMPVSLSVQ 

       670        680        690        700        710        720 
SPAALTAEKE AMCLSAPALA LKLPIPSPQR AFTLQVSSDP SMYIEVENEV TVVGGVKLSR 

       730        740        750        760        770        780 
LKCNREGKEW ETVLTSRILT AAGSCDVVCV ACEKRMLSVF STCGRRLLSP ILLPSPISTL 

       790        800        810        820        830        840 
HCTGSYVMAL TAAATLSVWD VHRQVVVVKE ESLHSILAGS DMTVSQILLT QHGIPVMNLS 

       850        860        870        880        890        900 
DGKAYCFNPS LSTWNLVSDK QDSLAQCADF RSSLPSQDAM LCSGPLAIIQ GRTSNSGRQA 

       910        920        930        940        950        960 
ARLFSVPHVV QQETTLAYLE NQVAAALTLQ SSHEYRHWLL VYARYLVNEG FEYRLREICK 

       970        980        990       1000       1010 
DLLGPVHYST GSQWESTVVG LRKRELLKEL LPVIGQNLRF QRLFTECQEQ LDILRDK 

« Hide

Isoform Short [UniParc].

Checksum: A169BFDCE4C8D4D7
Show »

FASTA81089,299

References

« Hide 'large scale' references
[1]"A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region."
Lamour V., Lecluse Y., Desmaze C., Spector M., Bodescot M., Aurias A., Osley M.A., Lipinski M.
Hum. Mol. Genet. 4:791-799(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Brain.
[2]"Structural organization of the WD repeat protein-encoding gene HIRA in the DiGeorge syndrome critical region of human chromosome 22."
Lorain S., Demczuk S., Lamour V., Toth S., Aurias A., Roe B.A., Lipinski M.
Genome Res. 6:43-50(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG).
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[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] (ISOFORM LONG).
Tissue: Eye and Lymph.
[5]"Isolation of a putative transcriptional regulator from the region of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital heart disease."
Halford S., Wadey R., Roberts C., Daw S.C.M., Whiting J.A., O'Donnell H., Dunham I., Bentley D., Lindsay E., Baldini A., Francis F., Lehrach H., Williamson R., Wilson D.I., Goodship J., Cross I., Burn J., Scambler P.J.
Hum. Mol. Genet. 2:2099-2107(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-1017 (ISOFORM SHORT).
Tissue: Fetal brain.
[6]"The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is expressed in embryonic structures affected in human CATCH22 patients."
Wilming L.G., Snoeren C.A.S., van Rijswijk A., Grosveld F., Meijers C.
Hum. Mol. Genet. 6:247-258(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"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: INTERACTION WITH HIRIP3; HISTONE H2B; HISTONE H4 AND NFU1, SUBCELLULAR LOCATION.
[8]"HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression."
Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S., Lipinski M., Adams P.D.
Mol. Cell. Biol. 21:1854-1865(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCNA1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-555 AND SER-687, MUTAGENESIS OF THR-555 AND 628-LYS--LEU-631.
[9]"Coupling of DNA synthesis and histone synthesis in S phase independent of cyclin/cdk2 activity."
Nelson D.M., Ye X., Hall C., Santos H., Ma T., Kao G.D., Yen T.J., Harper J.W., Adams P.D.
Mol. Cell. Biol. 22:7459-7472(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Structure and function of the conserved core of histone deposition protein Asf1."
Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R., Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.
Curr. Biol. 13:2148-2158(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASF1A.
[11]"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis."
Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.
Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ASF1A; CABIN1; HISTONE H3.3 AND UBN1.
[12]"Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.
Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ASF1A, SUBCELLULAR LOCATION.
[13]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[14]"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-584 AND THR-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the HIRA/ASF1a chromatin-remodeling pathway in senescent cells."
Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M., Ceulemans H., Schultz D., Marmorstein R., Adams P.D.
Mol. Cell. Biol. 29:758-770(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBN1.
[17]"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-549; SER-557; THR-576 AND THR-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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 THR-586 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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-610; SER-611; SER-612; SER-614 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly."
Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A., Dunbrack R., Adams P.D., Marmorstein R.
Nat. Struct. Mol. Biol. 13:921-929(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 425-472 IN COMPLEX WITH ASF1A, MUTAGENESIS OF 449-GLN--ARG-458; 459-ARG--GLN-468; ARG-459; ARG-460; ILE-461; LEU-464 AND ILE-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81844 mRNA. Translation: CAA57436.1. Different initiation.
X77633 mRNA. Translation: CAA54721.1. Different initiation.
X89887 mRNA. Translation: CAA61979.1.
X91501 Genomic DNA. Translation: CAA62800.1.
CR456503 mRNA. Translation: CAG30389.1.
BC032721 mRNA. Translation: AAH32721.1.
BC039835 mRNA. Translation: AAH39835.1.
X75296 mRNA. Translation: CAA53044.1. Different initiation.
CCDSCCDS13759.1. [P54198-1]
PIRI37465.
S45344.
RefSeqNP_003316.3. NM_003325.3. [P54198-1]
UniGeneHs.474206.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I32X-ray2.70E/F425-472[»]
ProteinModelPortalP54198.
SMRP54198. Positions 16-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113141. 20 interactions.
DIPDIP-29240N.
IntActP54198. 7 interactions.
MINTMINT-3020150.
STRING9606.ENSP00000263208.

PTM databases

PhosphoSiteP54198.

Polymorphism databases

DMDM88984228.

Proteomic databases

MaxQBP54198.
PaxDbP54198.
PeptideAtlasP54198.
PRIDEP54198.

Protocols and materials databases

DNASU7290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263208; ENSP00000263208; ENSG00000100084. [P54198-1]
ENST00000340170; ENSP00000345350; ENSG00000100084. [P54198-2]
ENST00000593536; ENSP00000470269; ENSG00000268569. [P54198-2]
ENST00000599450; ENSP00000471552; ENSG00000268569. [P54198-1]
GeneID7290.
KEGGhsa:7290.
UCSCuc002zpf.1. human. [P54198-1]
uc010grn.1. human. [P54198-2]

Organism-specific databases

CTD7290.
GeneCardsGC22M019318.
HGNCHGNC:4916. HIRA.
HPACAB039243.
CAB039244.
MIM600237. gene.
neXtProtNX_P54198.
Orphanet567. 22q11.2 deletion syndrome.
PharmGKBPA29293.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000007670.
HOVERGENHBG005969.
InParanoidP54198.
KOK11293.
OMALEDIRKX.
PhylomeDBP54198.
TreeFamTF323161.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkP54198.

Gene expression databases

ArrayExpressP54198.
BgeeP54198.
CleanExHS_HIRA.
GenevestigatorP54198.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR011494. Hira.
IPR019015. HIRA_B_motif.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF07569. Hira. 1 hit.
PF09453. HIRA_B. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHIRA. human.
EvolutionaryTraceP54198.
GeneWikiHIRA.
GenomeRNAi7290.
NextBio28503.
PROP54198.
SOURCESearch...

Entry information

Entry nameHIRA_HUMAN
AccessionPrimary (citable) accession number: P54198
Secondary accession number(s): Q05BU9, Q8IXN2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 21, 2006
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM