CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014995
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nipped-B-like protein 
Protein Synonyms/Alias
 Delangin; SCC2 homolog 
Gene Name
 NIPBL 
Gene Synonyms/Alias
 IDN3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
328RKQKKQKKMKLGKDEacetylation[1]
330QKKQKKMKLGKDEKEacetylation[1]
500KEVQDKDKPLKKRKQacetylation[2]
706RPETPKQKGESRPETacetylation[3]
1029DKSRSSLKPIKNKPSacetylation[2]
1082KRSTVNEKPKYAEISacetylation[2]
1247ELGSESAKIKAMGIMacetylation[2, 4]
1547NFLSIFLKKCGSKQGubiquitination[5]
1548FLSIFLKKCGSKQGEubiquitination[5]
2337PEPAMRNKADQQLVEubiquitination[5]
2348QLVEIDKKYAGFIHMubiquitination[6]
Reference
 [1] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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] 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]
 [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] 
Functional Description
 Probably plays a structural role in chromatin. Involved in sister chromatid cohesion, possibly by interacting with the cohesin complex (By similarity). 
Sequence Annotation
 REPEAT 1767 1805 HEAT 1.
 REPEAT 1843 1881 HEAT 2.
 REPEAT 1945 1984 HEAT 3.
 REPEAT 2227 2267 HEAT 4.
 REPEAT 2313 2351 HEAT 5.
 MOTIF 996 1009 PxVxL motif.
 MOD_RES 150 150 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 256 256 Phosphoserine.
 MOD_RES 280 280 Phosphoserine (By similarity).
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 318 318 Phosphoserine.
 MOD_RES 350 350 Phosphoserine.
 MOD_RES 553 553 Phosphoserine (By similarity).
 MOD_RES 558 558 Phosphothreonine (By similarity).
 MOD_RES 713 713 Phosphothreonine.
 MOD_RES 746 746 Phosphothreonine.
 MOD_RES 912 912 Phosphoserine.
 MOD_RES 1089 1089 Phosphoserine.
 MOD_RES 1090 1090 Phosphoserine.
 MOD_RES 1096 1096 Phosphoserine.
 MOD_RES 1150 1150 Phosphoserine.
 MOD_RES 1152 1152 Phosphoserine.
 MOD_RES 1154 1154 Phosphoserine.
 MOD_RES 1160 1160 Phosphoserine.
 MOD_RES 1458 1458 Phosphothreonine (By similarity).
 MOD_RES 1459 1459 Phosphoserine (By similarity).
 MOD_RES 2509 2509 Phosphoserine.
 MOD_RES 2511 2511 Phosphoserine.
 MOD_RES 2513 2513 Phosphoserine.
 MOD_RES 2515 2515 Phosphoserine.
 MOD_RES 2658 2658 Phosphoserine.
 MOD_RES 2667 2667 Phosphothreonine.
 MOD_RES 2672 2672 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Complete proteome; Disease mutation; Mental retardation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2804 AA 
Protein Sequence
MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNARIAEEV NCLLACRDDN 60
LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL ARSPNVFREK SMQNRYVQSG 120
MMMSQYKLSQ NSMHSSPASS NYQQTTISHS PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP 180
QSPAGYMPYS HPSSYTTHPQ MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR 240
HGSSEDYLHM VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSEGTPKG SRPPLILQSQ 300
SLPCSSPRDV PPDILLDSPE RKQKKQKKMK LGKDEKEQSE KAAMYDIISS PSKDSTKLTL 360
RLSRVRSSDM DQQEDMISGV ENSNVSENDI PFNVQYPGQT SKTPITPQDI NRPLNAAQCL 420
SQQEQTAFLP ANQVPVLQQN TSVAAKQPQT SVVQNQQQIS QQGPIYDEVE LDALAEIERI 480
ERESAIERER FSKEVQDKDK PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM 540
VSIDLHQAGR VDSQASITQD SDSIKKPEEI KQCNDAPVSV LQEDIVGSLK STPENHPETP 600
KKKSDPELSK SEMKQSESRL AESKPNENRL VETKSSENKL ETKVETQTEE LKQNESRTTE 660
CKQNESTIVE PKQNENRLSD TKPNDNKQNN GRSETTKSRP ETPKQKGESR PETPKQKSDG 720
HPETPKQKGD GRPETPKQKG ESRPETPKQK NEGRPETPKH RHDNRRDSGK PSTEKKPEVS 780
KHKQDTKSDS PRLKSERAEA LKQRPDGRSV SESLRRDHDN KQKSDDRGES ERHRGDQSRV 840
RRPETLRSSS RNEHGIKSDS SKTDKLERKH RHESGDSRER PSSGEQKSRP DSPRVKQGDS 900
NKSRSDKLGF KSPTSKDDKR TEGNKSKVDT NKAHPDNKAE FPSYLLGGRS GALKNFVIPK 960
IKRDKDGNVT QETKKMEMKG EPKDKVEKIG LVEDLNKGAK PVVVLQKLSL DDVQKLIKDR 1020
EDKSRSSLKP IKNKPSKSNK GSIDQSVLKE LPPELLAEIE STMPLCERVK MNKRKRSTVN 1080
EKPKYAEISS DEDNDSDEAF ESSRKRHKKD DDKAWEYEER DRRSSGDHRR SGHSHEGRRS 1140
SGGGRYRNRS PSDSDMEDYS PPPSLSEVAR KMKKKEKQKK RKAYEPKLTP EEMMDSSTFK 1200
RFTASIENIL DNLEDMDFTA FGDDDEIPQE LLLGKHQLNE LGSESAKIKA MGIMDKLSTD 1260
KTVKVLNILE KNIQDGSKLS TLLNHNNDTE EEERLWRDLI MERVTKSADA CLTTINIMTS 1320
PNMPKAVYIE DVIERVIQYT KFHLQNTLYP QYDPVYRLDP HGGGLLSSKA KRAKCSTHKQ 1380
RVIVMLYNKV CDIVSSLSEL LEIQLLTDTT ILQVSSMGIT PFFVENVSEL QLCAIKLVTA 1440
VFSRYEKHRQ LILEEIFTSL ARLPTSKRSL RNFRLNSSDM DGEPMYIQMV TALVLQLIQC 1500
VVHLPSSEKD SNAEEDSNKK IDQDVVITNS YETAMRTAQN FLSIFLKKCG SKQGEEDYRP 1560
LFENFVQDLL STVNKPEWPA AELLLSLLGR LLVHQFSNKS TEMALRVASL DYLGTVAARL 1620
RKDAVTSKMD QGSIERILKQ VSGGEDEIQQ LQKALLDYLD ENTETDPSLV FSRKFYIAQW 1680
FRDTTLETEK AMKSQKDEES SEGTHHAKEI ETTGQIMHRA ENRKKFLRSI IKTTPSQFST 1740
LKMNSDTVDY DDACLIVRYL ASMRPFAQSF DIYLTQILRV LGENAIAVRT KAMKCLSEVV 1800
AVDPSILARL DMQRGVHGRL MDNSTSVREA AVELLGRFVL CRPQLAEQYY DMLIERILDT 1860
GISVRKRVIK ILRDICIEQP TFPKITEMCV KMIRRVNDEE GIKKLVNETF QKLWFTPTPH 1920
NDKEAMTRKI LNITDVVAAC RDTGYDWFEQ LLQNLLKSEE DSSYKPVKKA CTQLVDNLVE 1980
HILKYEESLA DSDNKGVNSG RLVACITTLF LFSKIRPQLM VKHAMTMQPY LTTKCSTQND 2040
FMVICNVAKI LELVVPLMEH PSETFLATIE EDLMKLIIKY GMTVVQHCVS CLGAVVNKVT 2100
QNFKFVWACF NRYYGAISKL KSQHQEDPNN TSLLTNKPAL LRSLFTVGAL CRHFDFDLED 2160
FKGNSKVNIK DKVLELLMYF TKHSDEEVQT KAIIGLGFAF IQHPSLMFEQ EVKNLYNNIL 2220
SDKNSSVNLK IQVLKNLQTY LQEEDTRMQQ ADRDWKKVAK QEDLKEMGDV SSGMSSSIMQ 2280
LYLKQVLEAF FHTQSSVRHF ALNVIALTLN QGLIHPVQCV PYLIAMGTDP EPAMRNKADQ 2340
QLVEIDKKYA GFIHMKAVAG MKMSYQVQQA INTCLKDPVR GFRQDESSSA LCSHLYSMIR 2400
GNRQHRRAFL ISLLNLFDDT AKTDVTMLLY IADNLACFPY QTQEEPLFIM HHIDITLSVS 2460
GSNLLQSFKE SMVKDKRKER KSSPSKENES SDSEEEVSRP RKSRKRVDSD SDSDSEDDIN 2520
SVMKCLPENS APLIEFANVS QGILLLLMLK QHLKNLCGFS DSKIQKYSPS ESAKVYDKAI 2580
NRKTGVHFHP KQTLDFLRSD MANSKITEEV KRSIVKQYLD FKLLMEHLDP DEEEEEGEVS 2640
ASTNARNKAI TSLLGGGSPK NNTAAETEDD ESDGEDRGGG TSGSLRRSKR NSDSTELAAQ 2700
MNESVDVMDV IAICCPKYKD RPQIARVVQK TSSGFSVQWM AGSYSGSWTE AKRRDGRKLV 2760
PWVDTIKESD IIYKKIALTS ANKLTNKVVQ TLRSLYAAKD GTSS 2804 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0032116; C:SMC loading complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0007420; P:brain development; IMP:BHF-UCL.
 GO:0034613; P:cellular protein localization; IMP:UniProtKB.
 GO:0071481; P:cellular response to X-ray; IMP:UniProtKB.
 GO:0050890; P:cognition; IMP:BHF-UCL.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0048589; P:developmental growth; IMP:BHF-UCL.
 GO:0042471; P:ear morphogenesis; IMP:BHF-UCL.
 GO:0048557; P:embryonic digestive tract morphogenesis; IMP:BHF-UCL.
 GO:0035115; P:embryonic forelimb morphogenesis; IMP:BHF-UCL.
 GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Compara.
 GO:0035261; P:external genitalia morphogenesis; IMP:BHF-UCL.
 GO:0048592; P:eye morphogenesis; IMP:BHF-UCL.
 GO:0060325; P:face morphogenesis; IMP:BHF-UCL.
 GO:0045444; P:fat cell differentiation; IEA:Compara.
 GO:0061010; P:gall bladder development; IMP:BHF-UCL.
 GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
 GO:0001656; P:metanephros development; NAS:BHF-UCL.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
 GO:0031065; P:positive regulation of histone deacetylation; IDA:BHF-UCL.
 GO:0040018; P:positive regulation of multicellular organism growth; IEA:Compara.
 GO:0045778; P:positive regulation of ossification; IEA:Compara.
 GO:0048638; P:regulation of developmental growth; IMP:BHF-UCL.
 GO:0045995; P:regulation of embryonic development; IMP:BHF-UCL.
 GO:0042634; P:regulation of hair cycle; IMP:BHF-UCL.
 GO:0006974; P:response to DNA damage stimulus; IMP:UniProtKB.
 GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
 GO:0019827; P:stem cell maintenance; IEA:Compara.
 GO:0061038; P:uterus morphogenesis; IMP:BHF-UCL. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR026003; Cohesin_HEAT.
 IPR024986; Nipped-B_C. 
Pfam
 PF12765; Cohesin_HEAT
 PF12830; Nipped-B_C 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS