CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001254
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 WD repeat and HMG-box DNA-binding protein 1 
Protein Synonyms/Alias
 Acidic nucleoplasmic DNA-binding protein 1; And-1 
Gene Name
 WDHD1 
Gene Synonyms/Alias
 AND1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
63KAYSCALKSGKLVTAubiquitination[1]
108VFNGDGTKIAAGSSDubiquitination[1]
119GSSDFLVKIVDVMDSubiquitination[1]
130VMDSSQQKTFRGHDAubiquitination[1, 2, 3]
187CNDVINAKSICRLAWubiquitination[1]
197CRLAWQPKSGKLLAIubiquitination[1]
208LLAIPVEKSVKLYRRubiquitination[1]
211IPVEKSVKLYRRESWubiquitination[1]
309NVCDPSGKTSSSKVSubiquitination[1]
744NHLDYLAKNGYEYEEubiquitination[1]
754YEYEESTKNQATKEQubiquitination[1]
759STKNQATKEQQELLMubiquitination[1]
774KMLALSCKLEREFRCubiquitination[1]
805KYASRSRKLILAQKLubiquitination[1]
811RKLILAQKLSELAVEubiquitination[1, 4, 5]
840EEEDFRKKLNAGYSNubiquitination[1]
962NEKSPIIKPLIPKPKacetylation[6]
1127KLSAFAFKQE*****acetylation[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. 
Sequence Annotation
 REPEAT 11 50 WD 1.
 REPEAT 52 91 WD 2.
 REPEAT 92 131 WD 3.
 REPEAT 134 173 WD 4.
 REPEAT 184 223 WD 5.
 REPEAT 228 267 WD 6.
 REPEAT 271 310 WD 7.
 DNA_BIND 1016 1079 HMG box.
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 374 374 Phosphoserine.
 MOD_RES 383 383 Phosphoserine.
 MOD_RES 387 387 Phosphoserine.
 MOD_RES 824 824 Phosphothreonine.
 MOD_RES 868 868 Phosphoserine.
 MOD_RES 962 962 N6-acetyllysine.
 MOD_RES 984 984 Phosphoserine.
 MOD_RES 1090 1090 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1129 AA 
Protein Sequence
MPATRKPMRY GHTEGHTEVC FDDSGSFIVT CGSDGDVRIW EDLDDDDPKF INVGEKAYSC 60
ALKSGKLVTA VSNNTIQVHT FPEGVPDGIL TRFTTNANHV VFNGDGTKIA AGSSDFLVKI 120
VDVMDSSQQK TFRGHDAPVL SLSFDPKDIF LASASCDGSV RVWQISDQTC AISWPLLQKC 180
NDVINAKSIC RLAWQPKSGK LLAIPVEKSV KLYRRESWSH QFDLSDNFIS QTLNIVTWSP 240
CGQYLAAGSI NGLIIVWNVE TKDCMERVKH EKGYAICGLA WHPTCGRISY TDAEGNLGLL 300
ENVCDPSGKT SSSKVSSRVE KDYNDLFDGD DMSNAGDFLN DNAVEIPSFS KGIINDDEDD 360
EDLMMASGRP RQRSHILEDD ENSVDISMLK TGSSLLKEEE EDGQEGSIHN LPLVTSQRPF 420
YDGPMPTPRQ KPFQSGSTPL HLTHRFMVWN SIGIIRCYND EQDNAIDVEF HDTSIHHATH 480
LSNTLNYTIA DLSHEAILLA CESTDELASK LHCLHFSSWD SSKEWIIDLP QNEDIEAICL 540
GQGWAAAATS ALLLRLFTIG GVQKEVFSLA GPVVSMAGHG EQLFIVYHRG TGFDGDQCLG 600
VQLLELGKKK KQILHGDPLP LTRKSYLAWI GFSAEGTPCY VDSEGIVRML NRGLGNTWTP 660
ICNTREHCKG KSDHYWVVGI HENPQQLRCI PCKGSRFPPT LPRPAVAILS FKLPYCQIAT 720
EKGQMEEQFW RSVIFHNHLD YLAKNGYEYE ESTKNQATKE QQELLMKMLA LSCKLEREFR 780
CVELADLMTQ NAVNLAIKYA SRSRKLILAQ KLSELAVEKA AELTATQVEE EEEEEDFRKK 840
LNAGYSNTAT EWSQPRFRNQ VEEDAEDSGE ADDEEKPEIH KPGQNSFSKS TNSSDVSAKS 900
GAVTFSSQGR VNPFKVSASS KEPAMSMNSA RSTNILDNMG KSSKKSTALS RTTNNEKSPI 960
IKPLIPKPKP KQASAASYFQ KRNSQTNKTE EVKEENLKNV LSETPAICPP QNTENQRPKT 1020
GFQMWLEENR SNILSDNPDF SDEADIIKEG MIRFRVLSTE ERKVWANKAK GETASEGTEA 1080
KKRKRVVDES DETENQEEKA KENLNLSKKQ KPLDFSTNQK LSAFAFKQE 1129 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003723; F:RNA binding; IEA:Compara.
 GO:0070829; P:heterochromatin maintenance; IEA:Compara.
 GO:0033044; P:regulation of chromosome organization; IEA:Compara.
 GO:0006396; P:RNA processing; IEA:Compara. 
Interpro
 IPR022100; DUF3639.
 IPR009071; HMG_box_dom.
 IPR013979; TIF_beta_prop-like.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF12341; DUF3639
 PF08662; eIF2A
 PF00505; HMG_box
 PF00400; WD40 
SMART
 SM00398; HMG
 SM00320; WD40 
PROSITE
 PS50118; HMG_BOX_2
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS