CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018338
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PH-interacting protein 
Protein Synonyms/Alias
 PHIP; IRS-1 PH domain-binding protein; WD repeat-containing protein 11 
Gene Name
 PHIP 
Gene Synonyms/Alias
 WDR11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MSCERKGLSELRSubiquitination[1, 2]
42LIREVAEKELLPRRTubiquitination[3]
54RRTDWTGKEHPRTYQubiquitination[2, 3]
65RTYQNLVKYYRHLAPubiquitination[1, 2]
174TAVYQHMKMHKRILGubiquitination[1]
400QFKRREWKSILLDMAubiquitination[1]
1005LREQELMKIVGIKYEubiquitination[1, 2, 3]
1010LMKIVGIKYEVGLPTubiquitination[2]
1032FLDPDTGKLTGGSFTubiquitination[1, 2]
1062RQQFDDAKYRRWNIGubiquitination[2]
1150ECRSLIYKPLDGEWGubiquitination[1, 2]
1393RLIFSNSKAYTPSKRubiquitination[1]
1399SKAYTPSKRSRIYSMacetylation[3]
1497NAAQINGKTESSSVVacetylation[4, 5]
1528PSTSSAAKTFITKANacetylation[3]
1528PSTSSAAKTFITKANubiquitination[1]
1533AAKTFITKANASAIPacetylation[3, 4]
1542NASAIPGKTILENSVacetylation[3, 5]
1542NASAIPGKTILENSVubiquitination[1]
1553ENSVKHSKALNTLSSacetylation[3]
1736LLVPASVKVLRRSNRubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
 Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti- apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. 
Sequence Annotation
 REPEAT 181 222 WD 1.
 REPEAT 224 262 WD 2.
 REPEAT 265 310 WD 3.
 REPEAT 319 360 WD 4.
 REPEAT 363 402 WD 5.
 REPEAT 422 461 WD 6.
 REPEAT 464 504 WD 7.
 REPEAT 512 551 WD 8.
 DOMAIN 1176 1246 Bromo 1.
 DOMAIN 1333 1403 Bromo 2.
 REGION 924 1129 Mediates interaction with IRS1 (By
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 641 641 Phosphoserine.
 MOD_RES 659 659 Phosphoserine.
 MOD_RES 683 683 Phosphoserine.
 MOD_RES 692 692 Phosphoserine.
 MOD_RES 879 879 Phosphoserine.
 MOD_RES 880 880 Phosphoserine.
 MOD_RES 881 881 Phosphoserine.
 MOD_RES 911 911 Phosphoserine.
 MOD_RES 1281 1281 Phosphoserine.
 MOD_RES 1283 1283 Phosphoserine.
 MOD_RES 1296 1296 Phosphoserine.
 MOD_RES 1315 1315 Phosphoserine.
 MOD_RES 1359 1359 Phosphothreonine.
 MOD_RES 1405 1405 Phosphoserine.
 MOD_RES 1479 1479 Phosphoserine.
 MOD_RES 1497 1497 N6-acetyllysine.
 MOD_RES 1525 1525 Phosphoserine.
 MOD_RES 1533 1533 N6-acetyllysine.
 MOD_RES 1651 1651 Phosphoserine.
 MOD_RES 1762 1762 Phosphoserine.
 MOD_RES 1783 1783 Phosphoserine.
 MOD_RES 1796 1796 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Bromodomain; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1821 AA 
Protein Sequence
MSCERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD WTGKEHPRTY 60
QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL LGAGRQSLLR TNKSCKHVVW 120
KGSALAALHC GRPPESPVNY GSPPSIADTL FSRKLNGKYR LERLVPTAVY QHMKMHKRIL 180
GHLSSVYCVT FDRTGRRIFT GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI 240
AAGSCDKMIR VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW 300
DAGTLKINPR PAKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF GSGQPEKISE 360
LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK SILLDMATRP AGQNLQGIED 420
KITKMKVTMV AWDRHDNTVI TAVNNMTLKV WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR 480
VLFSAGHDGN VIVWDLARGV KIRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI 540
FGFGSSSKYD KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS 600
RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQEI SPLDSMIQRL QQEQDLRRSG 660
EAVISNTSRL SRGSISSTSE VHSPPNVGLR RSGQIEGVRQ MHSNAPRSEI ATERDLVAWS 720
RRVVVPELSA GVASRQEEWR TAKGEEEIKT YRSEEKRKHL TVPKENKIPT VSKNHAHEHF 780
LDLGESKKQQ TNQHNYRTRS ALEETPRPSE EIENGSSSSD EGEVVAVSGG TSEEEERAWH 840
SDGSSSDYSS DYSDWTADAG INLQPPKKVP KNKTKKAESS SDEEEESEKQ KQKQIKKEKK 900
KVNEEKDGPI SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSTWITDTI PRRCPFVPQM 960
GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE QELMKIVGIK YEVGLPTLCC 1020
LKLAFLDPDT GKLTGGSFTM KYHDMPDVID FLVLRQQFDD AKYRRWNIGD RFRSVIDDAW 1080
WFGTIESQEP LQLEYPDSLF QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT 1140
DGECRSLIYK PLDGEWGTNP RDEECERIVA GINQLMTLDI ASAFVAPVDL QAYPMYCTVV 1200
AYPTDLSTIK QRLENRFYRR VSSLMWEVRY IEHNTRTFNE PGSPIVKSAK FVTDLLLHFI 1260
KDQTCYNIIP LYNSMKKKVL SDSEDEEKDA DVPGTSTRKR KDHQPRRRLR NRAQSYDIQA 1320
WKKQCEELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME 1380
LCKDVRLIFS NSKAYTPSKR SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTITKR 1440
RKKRNRSSSV SSSAASSPER KKRILKPQLK SESSTSAFST PTRSIPPRHN AAQINGKTES 1500
SSVVRTRSNR VVVDPVVTEQ PSTSSAAKTF ITKANASAIP GKTILENSVK HSKALNTLSS 1560
PGQSSFSHGT RNNSAKENME KEKPVKRKMK SSVLPKASTL SKSSAVIEQG DCKNNALVPG 1620
TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTN SGEIIHKKRG RKPKKLQYAK PEDLEQNNVH 1680
PIRDEVLPSS TCNFLSETNN VKEDLLQKKN RGGRKPKRKM KTQKLDADLL VPASVKVLRR 1740
SNRKKIDDPI DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG 1800
TSSRGRVRKL TEKAKANLIG W 1821 
Gene Ontology
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; IDA:UniProtKB.
 GO:0005158; F:insulin receptor binding; NAS:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; NAS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
 GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
 GO:0045840; P:positive regulation of mitosis; ISS:UniProtKB.
 GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Compara.
 GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0006606; P:protein import into nucleus; IEA:Compara.
 GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
 GO:0040008; P:regulation of growth; IEA:Compara.
 GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR011047; Quinonprotein_ADH-like_supfam.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF00439; Bromodomain
 PF00400; WD40 
SMART
 SM00297; BROMO
 SM00320; WD40 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS
 PR00503; BROMODOMAIN.