CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005775
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase 5A 
Protein Synonyms/Alias
 Histone demethylase JARID1A; Jumonji/ARID domain-containing protein 1A; Retinoblastoma-binding protein 2; RBBP-2 
Gene Name
 KDM5A 
Gene Synonyms/Alias
 JARID1A; RBBP2; RBP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45RIRPLAEKTGICKIRubiquitination[1]
106ELQGSTLKIPVVERKubiquitination[1]
113KIPVVERKILDLYALubiquitination[1]
127LSKIVASKGGFEMVTubiquitination[1]
135GGFEMVTKEKKWSKVubiquitination[1]
137FEMVTKEKKWSKVGSubiquitination[1]
152RLGYLPGKGTGSLLKubiquitination[1, 2]
159KGTGSLLKSHYERILubiquitination[1]
191PNLDLKEKVEPEVLSubiquitination[1]
222PKRTRRVKTQSESGDubiquitination[1]
238SRNTELKKLQIFGAGubiquitination[1]
247QIFGAGPKVVGLAMGubiquitination[1]
339KGDWRCPKCVAEECSubiquitination[1]
347CVAEECSKPREAFGFubiquitination[1]
425FGSGFPVKDGRRKILubiquitination[1, 3]
713LCPCPMQKKCLRYRYubiquitination[1, 2]
714CPCPMQKKCLRYRYPubiquitination[1]
733PSLLYGVKVRAQSYDubiquitination[1, 2]
758SANFNHKKDLIELRVubiquitination[1]
774LEDAEDRKYPENDLFubiquitination[1]
789RKLRDAVKEAETCASubiquitination[1]
805AQLLLSKKQKHRQSPubiquitination[1]
820DSGRTRTKLTVEELKubiquitination[1]
847ISQARQVKNLLDDVEubiquitination[1]
895LPELPRLKQELQQARubiquitination[1]
924VTLDVMKKLIDSGVGubiquitination[1]
982ESIVNEAKNIPAFLPubiquitination[1]
1029QLESLSAKGRPIPVRubiquitination[1]
1087IGVYGSGKNRRKKVKubiquitination[1]
1094KNRRKKVKELIEKEKubiquitination[1]
1151LRAANLAKMTMVDRIubiquitination[1]
1209SWQAKEVKFLCPLCMubiquitination[1]
1275ELSSALAKLSVLSQRubiquitination[1]
1294AAREKTEKIISAELQubiquitination[1]
1302IISAELQKAAANPDLubiquitination[1]
Reference
 [1] 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]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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] 
Functional Description
 Histone demethylase that specifically demethylates 'Lys- 4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. 
Sequence Annotation
 DOMAIN 19 60 JmjN.
 DOMAIN 84 174 ARID.
 DOMAIN 437 603 JmjC.
 ZN_FING 293 343 PHD-type 1.
 ZN_FING 1161 1218 PHD-type 2.
 ZN_FING 1607 1661 PHD-type 3.
 REGION 1623 1690 Interaction with LMO2.
 MOTIF 419 423 GSGFP motif.
 METAL 483 483 Iron; catalytic (By similarity).
 METAL 486 486 Iron; catalytic (By similarity).
 METAL 571 571 Iron; catalytic (By similarity).
 MOD_RES 1111 1111 Phosphoserine.
 MOD_RES 1331 1331 Phosphoserine.
 MOD_RES 1598 1598 Phosphoserine.
 MOD_RES 1603 1603 Phosphoserine.
 MOD_RES 1666 1666 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Developmental protein; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1690 AA 
Protein Sequence
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK IRPPKDWQPP 60
FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL 120
SKIVASKGGF EMVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG 180
VQMPNLDLKE KVEPEVLSTD TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ 240
IFGAGPKVVG LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 300
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE AFGFEQAVRE 360
YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS 420
GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF 480
CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM 540
NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN 600
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVLM 660
SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCPCP MQKKCLRYRY 720
PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL SANFNHKKDL IELRVMLEDA EDRKYPENDL 780
FRKLRDAVKE AETCASVAQL LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI 840
SQARQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 900
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK 960
VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGSNYAYL 1020
EQLESLSAKG RPIPVRLEAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI 1080
GVYGSGKNRR KKVKELIEKE KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA 1140
MHSLRAANLA KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 1200
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDRA 1260
RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA 1320
FNRVVSSVSS SPRQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP 1380
IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG 1440
AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD 1500
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK LAKKLAKEEE 1560
RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK 1620
DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN EDYICINCAK KQGPVSPGPA PPPSFIMSYK 1680
LPMEDLKETS 1690 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IDA:GDB.
 GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR001606; ARID/BRIGHT_DNA-bd.
 IPR003347; JmjC_dom.
 IPR013637; Lys_sp_deMease_like_dom.
 IPR003349; TF_JmjN.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR004198; Znf_C5HC2.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01388; ARID
 PF02373; JmjC
 PF02375; JmjN
 PF00628; PHD
 PF08429; PLU-1
 PF02928; zf-C5HC2 
SMART
 SM00501; BRIGHT
 SM00558; JmjC
 SM00545; JmjN
 SM00249; PHD 
PROSITE
 PS51011; ARID
 PS51184; JMJC
 PS51183; JMJN
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS