CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021116
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase RanBP2 
Protein Synonyms/Alias
 Ran-binding protein 2; RanBP2; Putative peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase 
Gene Name
 Ranbp2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
225LQCLDSDKSTWRATNubiquitination[1]
335RPKVKLIKGEAGQNLubiquitination[1]
379VVESFANKSGQSALCubiquitination[1]
396LFSSQSSKERSFLGNubiquitination[1]
996ASRSAESKVIEFGKSacetylation[2, 3]
1814GFSGAGEKLFSSQSGacetylation[2, 3]
1898ERGLGNLKILKNEVNubiquitination[1]
1962KLEQLAAKFKTPELAubiquitination[1]
2788ERGIGDIKILWHTMKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1 (By similarity). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (By similarity). 
Sequence Annotation
 REPEAT 26 59 TPR 1.
 REPEAT 60 93 TPR 2.
 REPEAT 583 616 TPR 3.
 DOMAIN 1165 1301 RanBD1 1.
 DOMAIN 1849 1985 RanBD1 2.
 DOMAIN 2146 2282 RanBD1 3.
 REPEAT 2470 2522 1.
 REPEAT 2546 2596 2.
 DOMAIN 2740 2875 RanBD1 4.
 DOMAIN 2896 3052 PPIase cyclophilin-type.
 ZN_FING 1345 1375 RanBP2-type 1.
 ZN_FING 1410 1439 RanBP2-type 2.
 ZN_FING 1469 1498 RanBP2-type 3.
 ZN_FING 1494 1527 RanBP2-type 4.
 ZN_FING 1558 1587 RanBP2-type 5.
 ZN_FING 1617 1646 RanBP2-type 6.
 REGION 2468 2472 Interaction with sumoylated RANGAP1 (By
 REGION 2470 2596 2 X 50 AA approximate repeats.
 REGION 2470 2545 Required for E3 SUMO-ligase activity (By
 REGION 2470 2522 Interaction with UBE2I (By similarity).
 REGION 2523 2596 Interaction with SUMO1 (By similarity).
 MOD_RES 21 21 Phosphoserine (By similarity).
 MOD_RES 781 781 Phosphoserine.
 MOD_RES 788 788 Phosphoserine.
 MOD_RES 837 837 Phosphoserine (By similarity).
 MOD_RES 947 947 Phosphoserine (By similarity).
 MOD_RES 954 954 Phosphoserine.
 MOD_RES 1098 1098 Phosphoserine.
 MOD_RES 1138 1138 Phosphothreonine (By similarity).
 MOD_RES 1154 1154 Phosphoserine (By similarity).
 MOD_RES 1407 1407 Phosphothreonine (By similarity).
 MOD_RES 1438 1438 Phosphoserine (By similarity).
 MOD_RES 1446 1446 Phosphoserine (By similarity).
 MOD_RES 1528 1528 Phosphoserine (By similarity).
 MOD_RES 1670 1670 Phosphoserine (By similarity).
 MOD_RES 1706 1706 Phosphoserine (By similarity).
 MOD_RES 2083 2083 Phosphoserine.
 MOD_RES 2088 2088 Phosphoserine.
 MOD_RES 2107 2107 Phosphoserine (By similarity).
 MOD_RES 2113 2113 Phosphoserine.
 MOD_RES 2117 2117 Phosphoserine.
 MOD_RES 2130 2130 Phosphothreonine.
 MOD_RES 2134 2134 Phosphoserine.
 MOD_RES 2450 2450 Phosphothreonine (By similarity).
 MOD_RES 2505 2505 Phosphoserine.
 MOD_RES 2576 2576 Phosphoserine.
 MOD_RES 2578 2578 Phosphothreonine.
 MOD_RES 2729 2729 Phosphoserine.
 MOD_RES 3036 3036 Phosphoserine (By similarity).
 CROSSLNK 2430 2430 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Isomerase; Isopeptide bond; Ligase; Membrane; Metal-binding; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Rotamase; TPR repeat; Translocation; Transport; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3053 AA 
Protein Sequence
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP 60
KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER 120
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDIHVNIR LVELYRSNKR 180
LKDAVAHCHE ADRNTALRSS LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA 240
NLMLLTLSTR DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK 300
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR LSQSGHMLLN 360
LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF LGNDDIGNLD GQVPDPDDLA 420
RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL PAIRKWLKQL FHHLPQETSR LETNAPESIC 480
ILDLEVFLLG VIYTSHLQLK EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH 540
RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG 600
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA HITFAILDAV 660
NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIR 720
ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCWRS ADSELKHSTP 780
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR 840
WPAEPYGQDP APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 900
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT GILSPRGDDY 960
FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF GKSNFVQPMQ GEVIRPPLTT 1020
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPSTAYS NSESLLGLLT SDKPLQGDGY 1080
SGLKPISGQA SGSRNTFSFG SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA 1140
SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG 1200
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW 1260
HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNTSTAP NHTLRIVKES 1320
ATQDNKDICK ADGGNLNFEF QIVKKEGPYW NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL 1380
LGPPLVENGF APKTGLENAQ DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS 1440
SFVQTSFKFG QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK 1500
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG FEGMFAKKEG 1560
QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS ETSRSPKSGF EGLFPKKEGE 1620
WECAVCSVQN ESSSLKCVAC EASKPTHKPH EAPSAFTVGS KSQSNESAGS QVGTEFKSNF 1680
PEKNFKVGIS EQKFKFGHVD QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ 1740
EKGNQEKKSE KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK 1800
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF EPVVQMPEKV 1860
ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL KNEVNGKLRM LMRREQVLKV 1920
CANHWITTTM NLKPLSGSDR AWMWLASDFS DGDAKLEQLA AKFKTPELAE EFKQKFEECQ 1980
RLLLDIPLQT PHKLVDTGRA AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA 2040
PSASDTTAKQ NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES 2100
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV VPLPDLVEVS 2160
SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY DNKQVRIVMR RDQVLKLCAN 2220
HRITPDMTLQ TMKGTERVWV WTACDFADGE RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ 2280
EKDSLITPHV SHLSTPRESP CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE 2340
TTPKAVVSPP KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS 2400
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT PEKAQEKSKP 2460
EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR PGYVSEEEED DEDYEMAVKK 2520
LNGKLYLDDS EKPLEENLAD NDKECVIVWE KKPTVEERAK ADTLKLPPTF FCGVCSDTDE 2580
DNGNGEDFQS ELRKVCEAQK SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS 2640
SPVSGTMDKP VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK 2700
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV EVKSGEEDEE 2760
VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI LMRRDQVFKV CANHVITKAM 2820
ELKPLNVSNN ALVWTASDYA DGEAKVEQLA VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH 2880
TSLAAELSKD TNPVVFFDVC ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS 2940
IFHRVVPDFI CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ 3000
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC GQL 3053 
Gene Ontology
 GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
 GO:0031965; C:nuclear membrane; ISS:UniProtKB.
 GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
 GO:0016925; P:protein sumoylation; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
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.