CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037431
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Lysine-specific demethylase 5D 
Protein Synonyms/Alias
  
Gene Name
 KDM5D 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
164RQSVQPSKFSSYSRRubiquitination[1]
636LRKALLEKGVTEAERubiquitination[1]
713PTMLHKLKIRAESFDubiquitination[1]
914ASSPSVDKARAELQEubiquitination[1]
932IAERWEEKAHFCLEAubiquitination[1]
969LPNIQALKEALTKAQubiquitination[1]
1240GWQDRARKALASEDVubiquitination[1, 2]
1264LRQQLQAKPRPEEASubiquitination[1]
1385RTLLELEKFEHQGSRubiquitination[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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1476 AA 
Protein Sequence
MEPGCDEFLP PPECPVFEPS WAEFQDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV 60
DNFRFTPRVQ RLNELEIVIE EGGYEAICKD RRWARVAQRL HYPPGKNIGS LLRSHYERII 120
YPYEMFQSGA NHVQCNTHPF DNEVKDKEYK PHSIPLRQSV QPSKFSSYSR RAKRLQPDPE 180
PTEEDIEKHP ELKKLQIYGP GPKMMGLGLM AKDKDKTVHK KVTCPPTVTV KDEQSGGGNV 240
SSTLLKQHLS LEPCTKTTMQ LRKNHSSAQF IDSYICQVCS RGDEDDKLLF CDGCDDNYHI 300
FCLLPPLPEI PRGIWRCPKC ILAECKQPPE AFGFEQATQE YSLQSFGEMA DSFKSDYFNM 360
PVHMVPTELV EKEFWRLVSS IEEDVTVEYG ADIHSKEFGS GFPVSNSKQN LSPEEKEYAT 420
SGWNLNVMPV LDQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY SINYLHWGEP 480
KTWYGVPSLA AEHLEEVMKM LTPELFDSQP DLLHQLVTLM NPNTLMSHGV PVVRTNQCAG 540
EFVITFPRAY HSGFNQGYNF AEAVNFCTAD WLPAGRQCIE HYRRLRRYCV FSHEELICKM 600
AAFPETLDLN LAVAVHKEMF IMVQEERRLR KALLEKGVTE AEREAFELLP DDERQCIKCK 660
TTCFLSALAC YDCPDGLVCL SHINDLCKCS SSRQYLRYRY TLDELPTMLH KLKIRAESFD 720
TWANKVRVAL EVEDGRKRSF EELRALESEA RERRFPNSEL LQRLKNCLSE VEACIAQVLG 780
LVSGQVARMD TPQLTLTELR VLLEQMGSLP CAMHQIGDVK DVLEQVEAYQ AEAREALATL 840
PSSPGLLRSL LERGQQLGVE VPEAHQLQQQ VEQAQWLDEV KQALAPSAHR GSLVIMQGLL 900
VMGAKIASSP SVDKARAELQ ELLTIAERWE EKAHFCLEAR QKHPPATLEA IIRETENIPV 960
HLPNIQALKE ALTKAQAWIA DVDEIQNGDH YPCLDDLEGL VAVGRDLPVG LEELRQLELQ 1020
VLTAHSWREK ASKTFLKKNS CYTLLEVLCP CADAGSDSTK RSRWMEKALG LYQCDTELLG 1080
LSAQDLRDPG SVIVAFKEGE QKEKEGILQL RRTNSAKPSP LAPSLMASSP TSICVCGQVP 1140
AGVGVLQCDL CQDWFHGQCV SVPHLLTSPK PSLTSSPLLA WWEWDTKFLC PLCMRSRRPR 1200
LETILALLVA LQRLPVRLPE GEALQCLTER AIGWQDRARK ALASEDVTAL LRQLAELRQQ 1260
LQAKPRPEEA SVYTSATACD PIREGSGNNI SKVQGLLENG DSVTSPENMA PGKGSDLELL 1320
SSLLPQLTGP VLELPEAIRA PLEELMMEGD LLEVTLDENH SIWQLLQAGQ PPDLDRIRTL 1380
LELEKFEHQG SRTRSRALER RRRRQKVDQG RNVENLVQQE LQSKRARSSG IMSQVGREEE 1440
HYQEKADREN MFLTPSTDHS PFLKGNQNSL QHKDSG 1476 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 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:0008270; F:zinc ion binding; IEA:InterPro. 
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
 SM00558; JmjC
 SM00545; JmjN
 SM00249; PHD 
PROSITE
 PS51011; ARID
 PS51184; JMJC
 PS51183; JMJN
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS