CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016192
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein polybromo-1 
Protein Synonyms/Alias
 hPB1; BRG1-associated factor 180; BAF180; Polybromo-1D 
Gene Name
 PBRM1 
Gene Synonyms/Alias
 BAF180; PB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
569ILEPMDLKIIEHNIRubiquitination[1]
579EHNIRNDKYAGEEGMubiquitination[1]
670NEVYEAVKNYTDKRGubiquitination[1]
701PDYYLTIKKPMDMEKubiquitination[2, 3]
754KDALVLHKVLLETRRubiquitination[2, 3]
930EEKREAEKSEDSSGAubiquitination[4]
1019FLEKEVFKSDYYNKVubiquitination[1]
1025FKSDYYNKVPVSKILubiquitination[1]
1074TKSFKKIKLWTMPISubiquitination[1]
1181PRVGRIEKVWVRDGAubiquitination[1]
1293DEIYYFRKPIVPQKEsumoylation[5]
1398SEMRAVIKAQHPDYSubiquitination[1, 2, 3, 6, 7, 8]
1612LHSEAYLKYIEGLSAubiquitination[1]
1626AESNSISKWDQTLAAubiquitination[1]
1642RRDVHLSKEQESRLPubiquitination[1, 4, 6]
1654RLPSHWLKSKGAHTTubiquitination[1]
1656PSHWLKSKGAHTTMAubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [6] 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]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation. 
Sequence Annotation
 DOMAIN 64 134 Bromo 1.
 DOMAIN 200 270 Bromo 2.
 DOMAIN 400 470 Bromo 3.
 DOMAIN 538 608 Bromo 4.
 DOMAIN 676 746 Bromo 5.
 DOMAIN 792 862 Bromo 6.
 DOMAIN 956 1074 BAH 1.
 DOMAIN 1156 1272 BAH 2.
 DNA_BIND 1379 1447 HMG box.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 39 39 Phosphoserine.
 MOD_RES 131 131 Phosphoserine.
 MOD_RES 316 316 Phosphoserine.
 MOD_RES 319 319 Phosphoserine.
 MOD_RES 353 353 Phosphoserine.
 MOD_RES 355 355 Phosphoserine.
 MOD_RES 371 371 Phosphoserine.
 MOD_RES 375 375 Phosphoserine.
 MOD_RES 498 498 Phosphoserine.
 MOD_RES 636 636 Phosphoserine.
 MOD_RES 648 648 Phosphoserine.
 MOD_RES 1405 1405 Phosphoserine.
 MOD_RES 1453 1453 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Bromodomain; Chromatin regulator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1689 AA 
Protein Sequence
MGSKRRRATS PSSSVSGDFD DGHHSVSTPG PSRKRRRLSN LPTVDPIAVC HELYNTIRDY 60
KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK LKMEEYDDVN LLTADFQLLF 120
NNAKSYYKPD SPEYKAACKL WDLYLRTRNE FVQKGEADDE DDDEDGQDNQ GTVTEGSSPA 180
YLKEILEQLL EAIVVATNPS GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG 240
SYKSIHAMAK DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMAKSSLRMR 300
TPSNLAAARL TGPSHSKGSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ YGSESEEDAA 360
LAAARYEEGE SEAESITSFM DVSNPFYQLY DTVRSCRNNQ GQLIAEPFYH LPSKKKYPDY 420
YQQIKMPISL QQIRTKLKNQ EYETLDHLEC DLNLMFENAK RYNVPNSAIY KRVLKLQQVM 480
QAKKKELARR DDIEDGDSMI SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR 540
RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMIEDM KLMFRNARHY 600
NEEGSQVYND AHILEKLLKE KRKELGPLPD DDDMASPKLK LSRKSGISPK KSKYMTPMQQ 660
KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI KKPMDMEKIR SHMMANKYQD 720
IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR RDLEGDEDSH VPNVTLLIQE 780
LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNFPNKPPL TFDIIRKNVE NNRYRRLDLF 840
QEHMFEVLER ARRMNRTDSE IYEDAVELQQ FFIKIRDELC KNGEILLSPA LSYTTKHLHN 900
DVEKERKEKL PKEIEEDKLK REEEKREAEK SEDSSGAAGL SGLHRTYSQD CSFKNSMYHV 960
GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR PNETFHLATR KFLEKEVFKS 1020
DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI 1080
SSVRFVPRDV PLPVVRVASV FANADKGDDE KNTDNSEDSR AEDNFNLEKE KEDVPVEMSN 1140
GEPGCHYFEQ LHYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE 1200
ETEHEPTKMF YKKEVFLSNL EETCPMTCIL GKCAVLSFKD FLSCRPTEIP ENDILLCESR 1260
YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIVPQKE PSPLLEKKIQ LLEAKFAELE 1320
GGDDDIEEMG EEDSEVIEPP SLPQLQTPLA SELDLMPYTP PQSTPKSAKG SAKKEGSKRK 1380
INMSGYILFS SEMRAVIKAQ HPDYSFGELS RLVGTEWRNL ETAKKAEYEE RAAKVAEQQE 1440
RERAAQQQQP SASPRAGTPV GALMGVVPPP TPMGMLNQQL TPVAGMMGGY PPGLPPLQGP 1500
VDGLVSMGSM QPLHPGGPPP HHLPPGVPGL PGIPPPGVMN QGVAPMVGTP APGGSPYGQQ 1560
VGVLGPPGQQ APPPYPGPHP AGPPVIQQPT TPMFVAPPPK TQRLLHSEAY LKYIEGLSAE 1620
SNSISKWDQT LAARRRDVHL SKEQESRLPS HWLKSKGAHT TMADALWRLR DLMLRDTLNI 1680
RQAYNLENV 1689 
Gene Ontology
 GO:0000776; C:kinetochore; IEA:Compara.
 GO:0000228; C:nuclear chromosome; NAS:UniProtKB.
 GO:0003682; F:chromatin binding; NAS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006338; P:chromatin remodeling; TAS:UniProtKB.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0007067; P:mitosis; TAS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
 GO:0001890; P:placenta development; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001025; BAH_dom.
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR009071; HMG_box_dom. 
Pfam
 PF01426; BAH
 PF00439; Bromodomain
 PF00505; HMG_box 
SMART
 SM00439; BAH
 SM00297; BROMO
 SM00398; HMG 
PROSITE
 PS51038; BAH
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50118; HMG_BOX_2 
PRINTS
 PR00503; BROMODOMAIN.