CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001227
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable E3 ubiquitin-protein ligase MYCBP2 
Protein Synonyms/Alias
 Myc-binding protein 2; Pam/highwire/rpm-1 protein; Protein associated with Myc 
Gene Name
 MYCBP2 
Gene Synonyms/Alias
 KIAA0916; PAM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88SKVKTRSKSENLENTubiquitination[1]
540WVELPITKSPKIVHFubiquitination[1]
687GAMNQGGKGFGVENMubiquitination[2]
724PPGMHKWKLEQCMVCubiquitination[1]
1008PMPNIGSKYGRKATWubiquitination[3]
1762WTSLELVKGTYTTDDubiquitination[2]
1790VPLKENVKYAVRLRNacetylation[4]
2094SDYVKDDKASFYGFKubiquitination[3]
2422GTQLVKPKSEPQPNKacetylation[4]
3496SAHSSLSKGERNFQWubiquitination[1]
3750NITINCVKGINARYVubiquitination[1, 5]
3835QVKVLGWKDGESTKIubiquitination[1]
3889PTPEQEEKALLSSPEubiquitination[2]
4560GTDFLEYKCRYCCSVubiquitination[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] 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] 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]
 [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] 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
 Probable E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. May function as a facilitator or regulator of transcriptional activation by MYC. May have a role during synaptogenesis. 
Sequence Annotation
 REPEAT 562 617 RCC1 1.
 REPEAT 661 717 RCC1 2.
 REPEAT 869 919 RCC1 3.
 REPEAT 920 970 RCC1 4.
 REPEAT 972 1028 RCC1 5.
 REPEAT 2303 2405 Filamin.
 DOMAIN 3681 3859 DOC.
 ZN_FING 4390 4441 RING-type; atypical.
 ZN_FING 4544 4594 B box-type.
 REGION 1197 1348 PHR domain 1 (By similarity).
 REGION 1688 1846 PHR domain 2 (By similarity).
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 143 143 Phosphoserine.
 MOD_RES 145 145 Phosphoserine.
 MOD_RES 1586 1586 Phosphoserine (By similarity).
 MOD_RES 2645 2645 Phosphothreonine.
 MOD_RES 2751 2751 Phosphoserine.
 MOD_RES 2882 2882 Phosphoserine.
 MOD_RES 3052 3052 Phosphoserine.
 MOD_RES 3440 3440 Phosphoserine.
 MOD_RES 3467 3467 Phosphoserine.
 MOD_RES 3883 3883 Phosphothreonine (By similarity).
 DISULFID 1710 1825 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Disulfide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4640 AA 
Protein Sequence
MPVPDGSVAA AGLGLGLPAA DSRGHYQLLL SGRALADRYR RIYTAALNDR DQGGGSAGHP 60
ASRNKKILNK KKLKRKQKSK SKVKTRSKSE NLENTVIIPD IKLHSNPSAF NIYCNVRHCV 120
LEWQKKEISL AAASKNSVQS GESDSDEEEE SKEPPIKLPK IIEVGLCEVF ELIKETRFSH 180
PSLCLRSLQA LLNVLQGQQP EGLQSEPPEV LESLFQLLLE ITVRSTGMND STGQSLTALS 240
CACLFSLVAS WGETGRTLQA ISAILTNNGS HACQTIQVPT ILNSLQRSVQ AVLVGKIQIQ 300
DWFSNGIKKA ALMHKWPLKE ISVDEDDQCL LQNDGFFLYL LCKDGLYKIG SGYSGTVRGH 360
IYNSTSRIRN RKEKKSWLGY AQGYLLYRDV NNHSMTAIRI SPETLEQDGT VMLPDCHTEG 420
QNILFTDGEY INQIAASRDD GFVVRIFATS TEPVLQQELQ LKLARKCLHA CGISLFDLEK 480
DLHIISTGFD EESAILGAGR EFALMKTANG KIYYTGKYQS LGIKQGGPSA GKWVELPITK 540
SPKIVHFSVG HDGSHALLVA EDGSIFFTGS ASKGEDGEST KSRRQSKPYK PKKIIKMEGK 600
IVVYTACNNG SSSVISKDGE LYMFGKDAIY SDSSSLVTDL KGHFVTQVAM GKAHTCVLMK 660
NGEVWTFGVN NKGQCGRDTG AMNQGGKGFG VENMATAMDE DLEEELDEKD EKSMMCPPGM 720
HKWKLEQCMV CTVCGDCTGY GASCVSSGRP DRVPGGICGC GSGESGCAVC GCCKACAREL 780
DGQEARQRGI LDAVKEMIPL DLLLAVPVPG VNIEEHLQLR QEEKRQRVIR RHRLEEGRGP 840
LVFAGPIFMN HREQALARLR SHPAQLKHKR DKHKDGSGER GEKDASKITT YPPGSVRFDC 900
ELRAVQVSCG FHHSVVLMEN GDVYTFGYGQ HGQLGHGDVN SRGCPTLVQA LPGPSTQVTA 960
GSNHTAVLLM DGQVFTFGSF SKGQLGRPIL DVPYWNAKPA PMPNIGSKYG RKATWIGASG 1020
DQTFLRIDEA LINSHVLATS EIFASKHIIG LVPASISEPP PFKCLLINKV DGSCKTFNDS 1080
EQEDLQGFGV CLDPVYDVIW RFRPNTRELW CYNAVVADAR LPSAADMQSR CSILSPELAL 1140
PTGSRALTTR SHAALHILGC LDTLAAMQDL KMGVASTEEE TQAVMKVYSK EDYSVVNRFE 1200
SHGGGWGYSA HSVEAIRFSA DTDILLGGLG LFGGRGEYTA KIKLFELGPD GGDHETDGDL 1260
LAETDVLAYD CAAREKYAMM FDEPVLLQAG WWYVAWARVS GPSSDCGSHG QASITTDDGV 1320
VFQFKSSKKS NNGTDVNAGQ IPQLLYRLPT SDGSASKGKQ QTSEPVHILK RSFARTVSVE 1380
CFESLLSILH WSWTTLVLGV EELRGLKGFQ FTATLLDLER LRFVGTCCLR LLRVYTCEIY 1440
PVSATGKAVV EETSKLAECI GKTRTLLRKI LSEGVDHCMV KLDNDPQGYL SQPLSLLEAV 1500
LQECHNTFTA CFHSFYPTPA LQWACLCDLL NCLDQDIQEA NFKTSSSRLL AAVMSALCHT 1560
SVKLTSIFPI AYDGEVLLRS IVKQVSTEND STLVHRFPLL VAHMEKLSQS EENISGMTSF 1620
REVLEKMLVI VVLPVRNSLR RENELFSSHL VSNTCGLLAS IVSELTASAL GSEVDGLNSL 1680
HSVKASANRF TKTSQGRSWN TGNGSPDAIC FSVDKPGIVV VGFSVYGGGG IHEYELEVLV 1740
DDSEHAGDST HSHRWTSLEL VKGTYTTDDS PSDIAEIRLD KVVPLKENVK YAVRLRNYGS 1800
RTANGDGGMT TVQCPDGVTF TFSTCSLSSN GTNQTRGQIP QILYYRSEFD GDLQSQLLSK 1860
ANEEDKNCSR ALSVVSTVVR ASKDLLHRAL AVDADDIPEL LSSSSLFSML LPLIIAYIGP 1920
VAAAIPKVAV EVFGLVQQLL PSVAILNQKY APPAFNPNQS TDSTTGNQPE QGLSACTTSS 1980
HYAVIESEHP YKPACVMHYK VTFPECVRWM TIEFDPQCGT AQSEDVLRLL IPVRTVQNSG 2040
YGPKLTSVHE NLNSWIELKK FSGSSGWPTM VLVLPGNEAL FSLETASDYV KDDKASFYGF 2100
KCFAIGYEFS PGPDEGVIQL EKELANLGGV CAAALMKKDL ALPIGNELEE DLEILEEAAL 2160
QVCKTHSGIL GKGLALSHSP TILEALEGNL PLQIQSNEQS FLDDFIACVP GSSGGRLARW 2220
LQPDSYADPQ KTSLILNKDD IRCGWPTTIT VQTKDQYGDV VHVPNMKVEV KAVPVSQKKM 2280
SLQQDQAKKP QRIPGSPAVT AASSNTDMTY GGLASPKLDV SYEPMIVKEA RYIAITMMKV 2340
YENYSFEELR FASPTPKRPS ENMLIRVNND GTYCANWTPG AIGLYTLHVT IDGIEIDAGL 2400
EVKVKDPPKG MIPPGTQLVK PKSEPQPNKV RKFVAKDSAG LRIRSHPSLQ SEQIGIVKVN 2460
GTITFIDEIH NDDGVWLRLN DETIKKYVPN MNGYTEAWCL SFNQHLGKSL LVPVDESKTN 2520
TDDFFKDINS CCPQEATMQE QDMPFLRGGP GMYKVVKTGP SGHNIRSCPN LRGIPIGMLV 2580
LGNKVKAVGE VTNSEGTWVQ LDQNSMVEFC ESDEGEAWSL ARDRGGNQYL RHEDEQALLD 2640
QNSQTPPPSP FSVQAFNKGA SCSAQGFDYG LGNSKGDRGN ISTSSKPAST SGKSELSSKH 2700
SRSLKPDGRM SRTTADQKKP RGTESLSASE SLILKSDAAK LRSDSHSRSL SPNHNTLQTL 2760
KSDGRMPSSS RAESPGPGSR LSSPKPKTLP ANRSSPSGAS SPRSSSPHDK NLPQKSTAPV 2820
KTKLDPPRER SKSDSYTLDP DTLRKKKMPL TEPLRGRSTS PKPKSVPKDS TDSPGSENRA 2880
PSPHVVQENL HSEVVEVCTS STLKTNSLTD STCDDSSEFK SVDEGSNKVH FSIGKAPLKD 2940
EQEMRASPKI SRKCANRHTR PKKEKSSFLF KGDGSKPLEP AKQAMSPSVA ECARAVFASF 3000
LWHEGIVHDA MACSSFLKFH PELSKEHAPI RSSLNSQQPT EEKETKLKNR HSLEISSALN 3060
MFNIAPHGPD ISKMGSINKN KVLSMLKEPP LHEKCEDGKT ETTFEMSMHN TMKSKSPLPL 3120
TLQHLVAFWE DISLATIKAA SQNMIFPSPG SCAVLKKKEC EKENKKSKKE KKKKEKAEVR 3180
PRGNLFGEMA QLAVGGPEKD TICELCGESH PYPVTYHMRQ AHPGCGRYAG GQGYNSIGHF 3240
CGGWAGNCGD GGIGGSTWYL VCDRCREKYL REKQAAAREK VKQSRRKPMQ VKTPRALPTM 3300
EAHQVIKANA LFLLSLSSAA EPSILCYHPA KPFQSQLPSV KEGISEDLPV KMPCLYLQTL 3360
ARHHHENFVG YQDDNLFQDE MRYLRSTSVP APYISVTPDA SPNVFEEPES NMKSMPPSLE 3420
TSPITDTDLA KRTVFQRSYS VVASEYDKQH SILPARVKAI PRRRVNSGDT EVGSSLLRHP 3480
SPELSRLISA HSSLSKGERN FQWPVLAFVI QHHDLEGLEI AMKQALRKSA CRVFAMEAFN 3540
WLLCNVIQTT SLHDILWHFV ASLTPAPVEP EEEEDEENKT SKENSEQEKD TRVCEHPLSD 3600
IVIAGEAAHP LPHTFHRLLQ TISDLMMSLP SGSSLQQMAL RCWSLKFKQS DHQFLHQSNV 3660
FHHINNILSK SDDGDSEESF SISIQSGFEA MSQELCIVMC LKDLTSIVDI KTSSRPAMIG 3720
SLTDGSTETF WESGDEDKNK TKNITINCVK GINARYVSVH VDNSRDLGNK VTSMTFLTGK 3780
AVEDLCRIKQ VDLDSRHIGW VTSELPGGDN HIIKIELKGP ENTLRVRQVK VLGWKDGEST 3840
KIAGQISASV AQQRNCEAET LRVFRLITSQ VFGKLISGDA EPTPEQEEKA LLSSPEGEEK 3900
VYNATSDADL KEHMVGIIFS RSKLTNLQKQ VCAHIVQAIR MEATRVREEW EHAISSKENA 3960
NSQPNDEDAS SDAYCFELLS MVLALSGSNV GRQYLAQQLT LLQDLFSLLH TASPRVQRQV 4020
TSLLRRVLPE VTPSRLASII GVKSLPPADI SDIIHSTEKG DWNKLGILDM FLGCIAKALT 4080
VQLKAKGTTI TGTAGTTVGK GVTTVTLPMI FNSSYLRRGE SHWWMKGSTP TQISEIIIKL 4140
IKDMAAGHLS EAWSRVTKNA IAETIIALTK MEEEFRSPVR CIATTRLWLA LASLCVLDQD 4200
HVDRLSSGRW MGKDGQQKQM PMCDNHDDGE TAAIILCNVC GNLCTDCDRF LHLHRRTKTH 4260
QRQVFKEEEE AIKVDLHEGC GRTKLFWLMA LADSKTMKAM VEFREHTGKP TTSSSEACRF 4320
CGSRSGTELS AVGSVCSDAD CQEYAKIACS KTHPCGHPCG GVKNEEHCLP CLHGCDKSAT 4380
SLKQDADDMC MICFTEALSA APAIQLDCSH IFHLQCCRRV LENRWLGPRI TFGFISCPIC 4440
KNKINHIVLK DLLDPIKELY EDVRRKALMR LEYEGLHKSE AITTPGVRFY NDPAGYAMNR 4500
YAYYVCYKCR KAYFGGEARC DAEAGRGDDY DPRELICGAC SDVSRAQMCP KHGTDFLEYK 4560
CRYCCSVAVF FCFGTTHFCN ACHDDFQRMT SIPKEELPHC PAGPKGKQLE GTECPLHVVH 4620
PPTGEEFALG CGVCRNAHTF 4640 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0015630; C:microtubule cytoskeleton; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0021785; P:branchiomotor neuron axon guidance; IEA:Compara.
 GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Compara.
 GO:0051493; P:regulation of cytoskeleton organization; IEA:Compara.
 GO:0032880; P:regulation of protein localization; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR004939; APC_su10/DOC_dom.
 IPR017868; Filamin/ABP280_repeat-like.
 IPR008979; Galactose-bd-like.
 IPR027047; Highwire/Pam/Rpm-1.
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set.
 IPR012983; PHR.
 IPR009091; RCC1/BLIP-II.
 IPR000408; Reg_chr_condens.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF08005; PHR
 PF00415; RCC1
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS51284; DOC
 PS50194; FILAMIN_REPEAT
 PS00625; RCC1_1
 PS00626; RCC1_2
 PS50012; RCC1_3
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR00633; RCCNDNSATION.