CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035394
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein LOC100911178 
Protein Synonyms/Alias
  
Gene Name
 Ranbp2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
614RKVLPLLKMIRKKNSacetylation[1]
1133FTFHGPGKSIFTTPTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Isomerase; Reference proteome; Rotamase; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3055 AA 
Protein Sequence
MRRSKAEVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP 60
KAHRFLGLLY EIEENTDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER 120
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDVHVNIR LVELYRSNKR 180
LKDAVAHCHE ADRNMALRSS LEWNSCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYS 240
NLMLLTLSTR DVQESRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK 300
MGQQSDIQWR ALSELAALCY LIAFQVPRPK VKLIKGETGQ NLLEMMAHDR LSQSGHMLLN 360
LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKDRSF LGNDDIGNLD GQVPDLDDLA 420
RYDTGAVRAH SGSLQHLTWL GLQWNSLPTL PAIRKWLKQL FHHLPQETSR LETNAPESIC 480
ILDLEVFLLG VIYTSHLQLR EKSNSHHTSY QPLCLPLPVC RQLCTERQKS WWDAVCTLIH 540
RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG 600
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQV SEIGEYEEDA HITFAILDAV 660
NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK 720
ILDDSDSNIS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCFRS ADSELKHSTP 780
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR 840
WPAEHYRQDP VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 900
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS SCMFSQEMYG PPLRFESPAT GILSPRGDDY 960
FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSGESKVIEF GKSNFVQPMQ GEVIRPPLAT 1020
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VTQSPSTAYS NSESLLGLLT SDKPLQGDGY 1080
SGLKPISAQT GGSRNTFSFG SKSTLTENMG PNQQKNFGFR RSDDMFTFHG PGKSIFTTPT 1140
SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG 1200
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW 1260
HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNASTAA NHTLRIVKEP 1320
ATQDNKDICK SDGGNLNFEF QIVKKEGPFW NCNSCSFKNA ATATKCVSCQ NTKPTNGKEL 1380
LGSPLVENGF ASKTGPENVQ DRFALMTPNK EGHWDCSVCL VRNEPTVSRC IACQNTKNGS 1440
SFAQTSFKFG QGDLSKSADS DFRSVFSKKE GQWDCSICLV RNEASSTKCV ACQNPAKQAK 1500
EGQWDCSLCS VRNEANAVKC VACQNPVKPS SSTTVTVLPS FKFGTSEMTK PPRSGFEGMF 1560
AKKEGQWDCS LCFVRNEASA SQCIACQNPN KQNQPTSAVS APASSETSKS PKCGFEGLFT 1620
RKEGEWECTV CSVQNESSSL KCVSCDASKP THKPIAEAPS AFTVGSKSQL NESAGSQVGT 1680
EFKSNFPEKN FKVGISEQKF KFGHVDQEKT PSFTFQGSSN TEFKSIKDGF SFCIPVSADG 1740
FKFGIQEKGN QEKKSEKHLE NDPGFQAHDT SGQKNGSGVV FGQTSSTFTF ADLAKSTSRE 1800
GFQFGKKDPN FKGFSGAGEK LFSSQSGKVA EKANTSDLEK DDDAYKTEDS DDIHFEPVVQ 1860
MPEKVELVTG EEDEKVLYSQ RVKLFRFDAE ISQWKERGLG NLKILKNEVN GKLRMLMRRE 1920
QVLKVCANHW ITTTMNLKPL SGSDRAWMWL ASDFSDGDAK LEQLAAKFKT PELAEEFKQK 1980
FEECQRLLLD IPLQTPHKLV DTGRAAKLIQ RAEEMKSGLK DFKTFLTNDQ AKVTEEENTS 2040
SGADASSASD TTVKQNPDNT GPALEWDNYD LREDALDDSV SSSSVHASPL ASSPVRKNLF 2100
RFGESTTGFN FSFKSALSPS KSPAKLNQSG TSVGTDEESD VTQEEERDGQ YFEPVVPLPD 2160
LIEVSSGEEN EQVVFSHRAK LYRYDKDVGQ WKERGIGDIK ILQNYDNKQV RIVMRRDQVL 2220
KLCANHRITP DMTLQTMKGT ERVWVWTACD FADGERKIEH LAVRFKLQDV ADSFKKIFDE 2280
AKTAQEKDCL ITPHVSHLST PRESPCGKIA IAVLEETTRE RTDLTQGDEV VDTTSEAGET 2340
SSTSETTPKA VVSPPKFVFG SESVKSIFSS EKSKPFAFGN SSATGSLFGF SFNAPLKNSN 2400
SEISSIVQSG SEGKVDPDKG ELPPNSDIKQ SSDGKVKNLI AFSKETSSTF KTPEKAREKN 2460
KPEDPPSDTD ILIVYELTPT PEQKALAEKL LLPSTFFCYK NRPGYVSEEE EDDEDFEMAV 2520
KKLNGKLYVD DSEKPLEENL ADNDKECVIV WEKKPTVEER AKADTLKLPP TFFCGVCSDT 2580
DEDNGNGEDF QSELRKVQEA QKSQSEKVTN TVGIEQTGET EATNPDGSKS EEPDSDTKHS 2640
SSSPVPGTMD KPVDLSTKKE TDMEFPSQGE SKTVLFGFGS GTGLSFADLA SSNSGDFAFG 2700
PKDKNFQWAN TGAAVFGTQS TSKDGDDEDG SDEDVVHNED IHFEPIVSLP EVEVKSGEED 2760
EEVLFKERAK LYRWDRDVSQ WKERGIGDIK ILWHSVKNYY RILMRRDQVF KVCANHVITK 2820
AMELKPLNFS NNALVWTASD YADGEAKIEQ LAVRFKTKEI TECFKKKIEE CQQNIMKLQN 2880
GQVSLAAELS KETNPVVFFD VCVDGEPLGR IIMELFSNIV PQTAENFRAL CTGEKGFGFK 2940
NSIFHRVVPD FICQGGDITK YNGTGGQSIY GDKFDDENFD LKHTGPGLLS MANCGQNTNS 3000
SQFFITLKKA EHLDFKHVVF GFVKDGMDTV RKIESFGSPK GSVSRRICIT ECGQL 3055 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0046907; P:intracellular transport; IEA:InterPro.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC. 
Interpro
 IPR002130; Cyclophilin-like_PPIase_dom.
 IPR020892; Cyclophilin-type_PPIase_CS.
 IPR022011; IR1-M.
 IPR011993; PH_like_dom.
 IPR000156; Ran_bind_dom.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat.
 IPR001876; Znf_RanBP2. 
Pfam
 PF12185; IR1-M
 PF00160; Pro_isomerase
 PF00638; Ran_BP1
 PF00515; TPR_1
 PF00641; zf-RanBP 
SMART
 SM00160; RanBD
 SM00547; ZnF_RBZ 
PROSITE
 PS00170; CSA_PPIASE_1
 PS50072; CSA_PPIASE_2
 PS50196; RANBD1
 PS50005; TPR
 PS50293; TPR_REGION
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS
 PR00153; CSAPPISMRASE.