CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein HIRA 
Protein Synonyms/Alias
 TUP1-like enhancer of split protein 1 
Gene Name
 HIRA 
Gene Synonyms/Alias
 DGCR1; HIR; TUPLE1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27DIHPDGTKFATGGQGubiquitination[1, 2]
114TVFGSSGKLANVEQWubiquitination[3]
178RGHSGLVKGLTWDPVubiquitination[1, 2, 3]
187LTWDPVGKYIASQADubiquitination[3, 4]
214QLETSITKPFDECGGubiquitination[3]
259IIEREGWKTNMDFVGubiquitination[3]
275RKAVTVVKFNPKIFKubiquitination[3]
279TVVKFNPKIFKKKQKubiquitination[3]
292QKNGSSAKPSCPYCCubiquitination[3]
381IHQSTYGKSLAIMTEubiquitination[3]
416QQQQLDQKSAATREMubiquitination[3]
728LKCNREGKEWETVLTubiquitination[3]
754VVCVACEKRMLSVFSubiquitination[3]
860TWNLVSDKQDSLAQCubiquitination[3]
988LRKRELLKELLPVIGubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 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. 
Sequence Annotation
 REPEAT 11 53 WD 1.
 REPEAT 68 107 WD 2.
 REPEAT 129 168 WD 3.
 REPEAT 172 211 WD 4.
 REPEAT 220 263 WD 5.
 REPEAT 266 322 WD 6.
 REPEAT 326 367 WD 7.
 REPEAT 772 809 WD 8.
 REGION 421 729 Interaction with CCNA1.
 REGION 421 479 Interaction with ASF1A.
 REGION 439 475 Required for repression of histone gene
 REGION 593 826 Interaction with histone H2B.
 REGION 594 739 Interaction with PAX3 (By similarity).
 REGION 738 1017 Interaction with histone H4.
 REGION 740 828 Interaction with PAX3 (By similarity).
 MOD_RES 549 549 Phosphoserine.
 MOD_RES 555 555 Phosphothreonine; by CDK2.
 MOD_RES 557 557 Phosphoserine.
 MOD_RES 576 576 Phosphothreonine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 586 586 Phosphothreonine.
 MOD_RES 610 610 Phosphoserine.
 MOD_RES 611 611 Phosphoserine.
 MOD_RES 612 612 Phosphoserine.
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 661 661 Phosphoserine.
 MOD_RES 687 687 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1017 AA 
Protein Sequence
MKLLKPTWVN HNGKPIFSVD IHPDGTKFAT GGQGQDSGKV VIWNMSPVLQ EDDEKDENIP 60
KMLCQMDNHL ACVNCVRWSN SGMYLASGGD DKLIMVWKRA TYIGPSTVFG SSGKLANVEQ 120
WRCVSILRNH SGDVMDVAWS PHDAWLASCS VDNTVVIWNA VKFPEILATL RGHSGLVKGL 180
TWDPVGKYIA SQADDRSLKV WRTLDWQLET SITKPFDECG GTTHVLRLSW SPDGHYLVSA 240
HAMNNSGPTA QIIEREGWKT NMDFVGHRKA VTVVKFNPKI FKKKQKNGSS AKPSCPYCCC 300
AVGSKDRSLS VWLTCLKRPL VVIHELFDKS IMDISWTLNG LGILVCSMDG SVAFLDFSQD 360
ELGDPLSEEE KSRIHQSTYG KSLAIMTEAQ LSTAVIENPE MLKYQRRQQQ QQLDQKSAAT 420
REMGSATSVA GVVNGESLED IRKNLLKKQV ETRTADGRRR ITPLCIAQLD TGDFSTAFFN 480
SIPLSGSLAG TMLSSHSSPQ LLPLDSSTPN SFGASKPCTE PVVAASARPA GDSVNKDSMN 540
ATSTPAALSP SVLTTPSKIE PMKAFDSRFT ERSKATPGAP ALTSMTPTAV ERLKEQNLVK 600
ELRPRDLLES SSDSDEKVPL AKASSLSKRK LELEVETVEK KKKGRPRKDS RLMPVSLSVQ 660
SPAALTAEKE AMCLSAPALA LKLPIPSPQR AFTLQVSSDP SMYIEVENEV TVVGGVKLSR 720
LKCNREGKEW ETVLTSRILT AAGSCDVVCV ACEKRMLSVF STCGRRLLSP ILLPSPISTL 780
HCTGSYVMAL TAAATLSVWD VHRQVVVVKE ESLHSILAGS DMTVSQILLT QHGIPVMNLS 840
DGKAYCFNPS LSTWNLVSDK QDSLAQCADF RSSLPSQDAM LCSGPLAIIQ GRTSNSGRQA 900
ARLFSVPHVV QQETTLAYLE NQVAAALTLQ SSHEYRHWLL VYARYLVNEG FEYRLREICK 960
DLLGPVHYST GSQWESTVVG LRKRELLKEL LPVIGQNLRF QRLFTECQEQ LDILRDK 1017 
Gene Ontology
 GO:0000790; C:nuclear chromatin; IEA:Compara.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007369; P:gastrulation; IEA:Compara.
 GO:0042692; P:muscle cell differentiation; IEA:Compara.
 GO:0001649; P:osteoblast differentiation; IEA:Compara.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011494; Hira.
 IPR019015; HIRA_B_motif.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF07569; Hira
 PF09453; HIRA_B
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS