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P49792 (RBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 SUMO-protein ligase RanBP2

EC=6.3.2.-
Alternative name(s):
358 kDa nucleoporin
Nuclear pore complex protein Nup358
Nucleoporin Nup358
Ran-binding protein 2
Short name=RanBP2
p270
Gene names
Name:RANBP2
Synonyms:NUP358
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Ref.6 Ref.7 Ref.10 Ref.29 Ref.30

Pathway

Protein modification; protein sumoylation.

Subunit structure

Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with PARK2. Interacts with sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform PML-4) Ref.10 Ref.11 Ref.12 Ref.15 Ref.22 Ref.29 Ref.30

Subcellular location

Nucleus. Nucleus membrane. Nucleusnuclear pore complex. Note: Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. Ref.8 Ref.32

Domain

Contains a dozen F-X-F-G repeats in the C-terminal half. Ref.32

The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (Ref.32). Only about half of the residues that surround the PPIA active site cleft are conserved. Ref.32

Post-translational modification

Polyubiquitinated by PARK2, which leads to proteasomal degradation.

The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC By similarity.

Involvement in disease

Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem.
Note: The disease is caused by mutations affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (Ref.33). Ref.33

Sequence similarities

Contains 1 PPIase cyclophilin-type domain.

Contains 4 RanBD1 domains.

Contains 8 RanBP2-type zinc fingers.

Contains 7 TPR repeats.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
Ubl conjugation pathway
   Cellular componentMembrane
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
TPR repeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Disulfide bond
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

glucose transport

Traceable author statement. Source: Reactome

hexose transport

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

negative regulation of glucokinase activity

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: InterPro

protein import into nucleus

Traceable author statement Ref.2. Source: ProtInc

protein sumoylation

Inferred from direct assay PubMed 17264123PubMed 22155184. Source: UniProtKB

regulation of gluconeogenesis involved in cellular glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

regulation of glucose transport

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nuclear inclusion body

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear pore

Inferred from direct assay PubMed 17098863. Source: UniProtKB

nuclear pore nuclear basket

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Ran GTPase binding

Traceable author statement Ref.2. Source: ProtInc

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 32243224E3 SUMO-protein ligase RanBP2
PRO_0000204913

Regions

Repeat26 – 5934TPR 1
Repeat60 – 9334TPR 2
Repeat94 – 12835TPR 3
Repeat165 – 20137TPR 4
Repeat287 – 31933TPR 5
Repeat583 – 61634TPR 6
Repeat648 – 68134TPR 7
Domain1171 – 1307137RanBD1 1
Domain2012 – 2148137RanBD1 2
Domain2309 – 2445137RanBD1 3
Repeat2633 – 2685531
Repeat2711 – 2761512
Domain2911 – 3046136RanBD1 4
Domain3067 – 3223157PPIase cyclophilin-type
Zinc finger1351 – 138131RanBP2-type 1
Zinc finger1415 – 144430RanBP2-type 2
Zinc finger1479 – 150830RanBP2-type 3
Zinc finger1543 – 157230RanBP2-type 4
Zinc finger1606 – 163530RanBP2-type 5
Zinc finger1665 – 169430RanBP2-type 6
Zinc finger1724 – 175330RanBP2-type 7
Zinc finger1781 – 181030RanBP2-type 8
Region2631 – 26355Interaction with sumoylated RANGAP1
Region2633 – 27611292 X 50 AA approximate repeats
Region2633 – 271078Required for E3 SUMO-ligase activity
Region2633 – 268553Interaction with UBE2I
Region2686 – 276176Interaction with SUMO1

Amino acid modifications

Modified residue191Phosphothreonine Ref.19 Ref.23 Ref.24
Modified residue211Phosphoserine Ref.16 Ref.19 Ref.23 Ref.24
Modified residue7811Phosphoserine Ref.19 Ref.24
Modified residue7881Phosphoserine By similarity
Modified residue8371Phosphoserine Ref.24
Modified residue9481Phosphoserine Ref.19 Ref.24
Modified residue9551Phosphoserine Ref.19 Ref.23 Ref.24
Modified residue11071Phosphoserine Ref.23
Modified residue11101Phosphoserine Ref.19 Ref.24
Modified residue11441Phosphothreonine Ref.16 Ref.19
Modified residue11601Phosphoserine Ref.19 Ref.24 Ref.26
Modified residue13961Phosphothreonine Ref.19 Ref.23
Modified residue14121Phosphothreonine Ref.24
Modified residue14431Phosphoserine Ref.19
Modified residue14561Phosphoserine Ref.19 Ref.26
Modified residue15091Phosphoserine Ref.19 Ref.24
Modified residue15731Phosphoserine Ref.19
Modified residue18351Phosphoserine Ref.24
Modified residue18691Phosphoserine Ref.19
Modified residue18711Phosphoserine Ref.23
Modified residue19771N6-acetyllysine By similarity
Modified residue22461Phosphoserine By similarity
Modified residue22701Phosphoserine Ref.19 Ref.23
Modified residue22931Phosphothreonine By similarity
Modified residue22971Phosphoserine By similarity
Modified residue25101Phosphoserine By similarity
Modified residue26131Phosphothreonine Ref.19
Modified residue26681Phosphoserine Ref.19 Ref.23 Ref.26
Modified residue27411Phosphoserine Ref.19
Modified residue27431Phosphothreonine Ref.19
Modified residue29001Phosphoserine Ref.19 Ref.23 Ref.24 Ref.26
Modified residue32071Phosphoserine Ref.24 Ref.26
Cross-link2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.10

Natural variations

Natural variant5481V → L.
Corresponds to variant rs1057954 [ dbSNP | Ensembl ].
VAR_029765
Natural variant5801E → K.
Corresponds to variant rs4012065 [ dbSNP | Ensembl ].
VAR_029766
Natural variant5811C → Y.
Corresponds to variant rs1057957 [ dbSNP | Ensembl ].
VAR_029767
Natural variant5851T → M in IIAE3. Ref.33
VAR_054997
Natural variant6531T → I in IIAE3. Ref.33
VAR_054998
Natural variant6561I → V in IIAE3. Ref.33
VAR_054999
Natural variant7251S → G.
Corresponds to variant rs17414315 [ dbSNP | Ensembl ].
VAR_050575
Natural variant7841R → K. Ref.2
Corresponds to variant rs2912838 [ dbSNP | Ensembl ].
VAR_023939
Natural variant18701P → L.
Corresponds to variant rs2889846 [ dbSNP | Ensembl ].
VAR_029768
Natural variant18921P → A.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].
VAR_014886
Natural variant18921P → R.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].
VAR_050576

Experimental info

Mutagenesis26321V → K: Abolishes interaction with sumoylated RANGAP1. Ref.11
Mutagenesis26341I → K: Abolishes interaction with sumoylated RANGAP1. Ref.11
Mutagenesis26351V → K: Abolishes interaction with sumoylated RANGAP1. Ref.11
Mutagenesis26401P → A: No effect on SUMO E3 ligase activity. Ref.10
Mutagenesis26451K → A: No effect on SUMO E3 ligase activity. Ref.10
Mutagenesis26511L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10
Mutagenesis26521K → A: No effect on SUMO E3 ligase activity. Ref.10
Mutagenesis26531L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10
Mutagenesis26541P → A: Impairs SUMO E3 ligase activity. Ref.10
Mutagenesis26551P → A: No effect on SUMO E3 ligase activity. Ref.10
Mutagenesis26561T → A: Impairs SUMO E3 ligase activity. Ref.10
Mutagenesis26571F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10
Mutagenesis26581F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10
Mutagenesis26591C → S or A: Impairs SUMO E3 ligase activity. Ref.10
Mutagenesis26761D → A: Impairs SUMO E3 ligase activity. Ref.10
Mutagenesis26771F → A: Impairs SUMO E3 ligase activity. Ref.10
Mutagenesis26891Y → A: Impairs SUMO E3 ligase activity. Ref.10
Sequence conflict7771H → R in AAC41758. Ref.1
Sequence conflict22071S → A in AAA85838. Ref.5
Sequence conflict22101T → P in AAA85838. Ref.5
Sequence conflict22161E → V in AAA85838. Ref.5
Sequence conflict24361F → C in AAA85838. Ref.5
Sequence conflict24751T → P in AAA85838. Ref.5
Sequence conflict25311K → N in AAA85838. Ref.5
Sequence conflict25451F → C Ref.5

Secondary structure

...................................................................................................................... 3224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49792 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 4CD9A3D5E77183FB

FASTA3,224358,199
        10         20         30         40         50         60 
MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP 

        70         80         90        100        110        120 
KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWLER 

       130        140        150        160        170        180 
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR 

       190        200        210        220        230        240 
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA 

       250        260        270        280        290        300 
NLMLLTLSTR DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM 

       310        320        330        340        350        360 
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN 

       370        380        390        400        410        420 
LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLT 

       430        440        450        460        470        480 
RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPHETSR LETNAPESIC 

       490        500        510        520        530        540 
ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH 

       550        560        570        580        590        600 
RKAVPGNVAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG 

       610        620        630        640        650        660 
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV 

       670        680        690        700        710        720 
NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK 

       730        740        750        760        770        780 
IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP 

       790        800        810        820        830        840 
SPTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR 

       850        860        870        880        890        900 
WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 

       910        920        930        940        950        960 
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD 

       970        980        990       1000       1010       1020 
YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP 

      1030       1040       1050       1060       1070       1080 
TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG 

      1090       1100       1110       1120       1130       1140 
YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS 

      1150       1160       1170       1180       1190       1200 
VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK 

      1210       1220       1230       1240       1250       1260 
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS 

      1270       1280       1290       1300       1310       1320 
DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVAMASNQAV 

      1330       1340       1350       1360       1370       1380 
RIVKEPTSHD NKDICKSDAG NLNFEFQVAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP 

      1390       1400       1410       1420       1430       1440 
SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN 

      1450       1460       1470       1480       1490       1500 
TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA 

      1510       1520       1530       1540       1550       1560 
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA 

      1570       1580       1590       1600       1610       1620 
TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE 

      1630       1640       1650       1660       1670       1680 
ASATKCIACQ NPGKQNQTTS AVSTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA 

      1690       1700       1710       1720       1730       1740 
SATKCIACQN PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS 

      1750       1760       1770       1780       1790       1800 
ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK 

      1810       1820       1830       1840       1850       1860 
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS KFGNTEQGFK 

      1870       1880       1890       1900       1910       1920 
FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENGT 

      1930       1940       1950       1960       1970       1980 
GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS 

      1990       2000       2010       2020       2030       2040 
SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV 

      2050       2060       2070       2080       2090       2100 
KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG 

      2110       2120       2130       2140       2150       2160 
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT 

      2170       2180       2190       2200       2210       2220 
GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP 

      2230       2240       2250       2260       2270       2280 
TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS 

      2290       2300       2310       2320       2330       2340 
PAKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY 

      2350       2360       2370       2380       2390       2400 
RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER 

      2410       2420       2430       2440       2450       2460 
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR 

      2470       2480       2490       2500       2510       2520 
ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST SETTPKAVVS PPKFVFGSES 

      2530       2540       2550       2560       2570       2580 
VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPKKCELS 

      2590       2600       2610       2620       2630       2640 
KNSDIEQSSD SKVKNLFASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP 

      2650       2660       2670       2680       2690       2700 
TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE 

      2710       2720       2730       2740       2750       2760 
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV 

      2770       2780       2790       2800       2810       2820 
QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS 

      2830       2840       2850       2860       2870       2880 
TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF 

      2890       2900       2910       2920       2930       2940 
GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL 

      2950       2960       2970       2980       2990       3000 
YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN 

      3010       3020       3030       3040       3050       3060 
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK 

      3070       3080       3090       3100       3110       3120 
ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF 

      3130       3140       3150       3160       3170       3180 
VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFVITLKKAE 

      3190       3200       3210       3220 
HLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQI 

« Hide

References

« Hide 'large scale' references
[1]"Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region."
Wu J., Matunis M.J., Kraemer D., Blobel G., Coutavas E.
J. Biol. Chem. 270:14209-14213(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A giant nucleopore protein that binds Ran/TC4."
Yokoyama N., Hayashi N., Seki T., Nishii K., Hayashida T., Kuma K., Miyata T., Fukui M., Nishimoto T., Pante N., Aebi U.
Nature 376:184-188(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-784.
Tissue: Blood.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-3224.
Tissue: Brain.
[5]"The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif."
Beddow A.L., Richards S.A., Orem N.R., Macara I.G.
Proc. Natl. Acad. Sci. U.S.A. 92:3328-3332(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2205-2546.
Tissue: Hippocampus.
[6]"The nucleoporin RanBP2 has SUMO1 E3 ligase activity."
Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F.
Cell 108:109-120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUMOYLATION.
[7]"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase."
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.
EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type."
Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.
Nat. Struct. Mol. Biol. 11:984-991(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2I, SUMOYLATION AT LYS-2592, MUTAGENESIS OF PRO-2640; LYS-2645; LEU-2651; LYS-2652; LEU-2653; PRO-2654; PRO-2655; THR-2656; PHE-2657; PHE-2658; CYS-2659; ASP-2676; PHE-2677 AND TYR-2689.
[11]"Identification of a SUMO-binding motif that recognizes SUMO-modified proteins."
Song J., Durrin L.K., Wilkinson T.A., Krontiris T.G., Chen Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14373-14378(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMOYLATED RANGAP1, MUTAGENESIS OF VAL-2632; ILE-2634 AND VAL-2635.
[12]"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMO1 AND UBE2I.
[13]"A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Parkin ubiquitinates and promotes the degradation of RanBP2."
Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.
J. Biol. Chem. 281:3595-3603(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARK2, UBIQUITINATION.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781; SER-948; SER-955; SER-1110; THR-1144; SER-1160; THR-1396; SER-1443; SER-1456; SER-1509; SER-1573; SER-1869; SER-2270; THR-2613; SER-2668; SER-2741; THR-2743 AND SER-2900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin."
Klein U.R., Haindl M., Nigg E.A., Muller S.
Mol. Biol. Cell 20:410-418(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCA8.
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-955; SER-1107; THR-1396; SER-1871; SER-2270; SER-2668 AND SER-2900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781; SER-837; SER-948; SER-955; SER-1110; SER-1160; THR-1412; SER-1509; SER-1835; SER-2900 AND SER-3207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1456; SER-2668; SER-2900 AND SER-3207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport."
Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.
Nature 398:39-46(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1171-1304.
[28]"Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran."
Geyer J.P., Doker R., Kremer W., Zhao X., Kuhlmann J., Kalbitzer H.R.
J. Mol. Biol. 348:711-725(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2028-2154.
[29]"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 2631-2711 IN COMPLEX WITH SUMO1; RANGAP1 AND UBE2I, SUBUNIT, FUNCTION.
[30]"Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2."
Gareau J.R., Reverter D., Lima C.D.
J. Biol. Chem. 287:4740-4751(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2631-2695 IN COMPLEX WITH SUMO1; RANGAP1 AND UBE2I, SUBUNIT, FUNCTION.
[31]"Crystal structure of the N-terminal domain of Nup358/RanBP2."
Kassube S.A., Stuwe T., Lin D.H., Antonuk C.D., Napetschnig J., Blobel G., Hoelz A.
J. Mol. Biol. 423:752-765(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 1-145, TPR REPEATS.
[32]"Structural and functional analysis of the C-terminal domain of Nup358/RanBP2."
Lin D.H., Zimmermann S., Stuwe T., Stuwe E., Hoelz A.
J. Mol. Biol. 425:1318-1329(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3062-3224, DOMAIN, ABSENCE OF ROTAMASE ACTIVITY, SUBCELLULAR LOCATION.
[33]"Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2."
Neilson D.E., Adams M.D., Orr C.M.D., Schelling D.K., Eiben R.M., Kerr D.S., Anderson J., Bassuk A.G., Bye A.M., Childs A.-M., Clarke A., Crow Y.J., Di Rocco M., Dohna-Schwake C., Dueckers G., Fasano A.E., Gika A.D., Gionnis D. expand/collapse author list , Gorman M.P., Grattan-Smith P.J., Hackenberg A., Kuster A., Lentschig M.G., Lopez-Laso E., Marco E.J., Mastroyianni S., Perrier J., Schmitt-Mechelke T., Servidei S., Skardoutsou A., Uldall P., van der Knaap M.S., Goglin K.C., Tefft D.L., Aubin C., de Jager P., Hafler D., Warman M.L.
Am. J. Hum. Genet. 84:44-51(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IIAE3 MET-585; ILE-653 AND VAL-656.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41840 Genomic DNA. Translation: AAC41758.1.
D42063 mRNA. Translation: BAA07662.1.
AC010095 Genomic DNA. Translation: AAY14984.1.
AB209483 mRNA. Translation: BAD92720.1.
U19248 mRNA. Translation: AAA85838.1.
PIRS58884.
RefSeqNP_006258.3. NM_006267.4.
UniGeneHs.199561.
Hs.715056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRPX-ray2.96B/D1171-1304[»]
1XKENMR-A2028-2154[»]
1Z5SX-ray3.01D2631-2711[»]
3UINX-ray2.60D2629-2695[»]
3UIOX-ray2.60D2631-2695[»]
3UIPX-ray2.29D2631-2695[»]
4GA0X-ray1.15A1-145[»]
4I9YX-ray1.75A/B/C/D/E/F3062-3224[»]
4L6EX-ray2.50A2907-3050[»]
4LQWX-ray1.95A/B3057-3224[»]
ProteinModelPortalP49792.
SMRP49792. Positions 3-145, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2709-2761, 2925-3048, 3062-3224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111839. 90 interactions.
DIPDIP-37654N.
IntActP49792. 40 interactions.
MINTMINT-191403.
STRING9606.ENSP00000283195.

PTM databases

PhosphoSiteP49792.

Polymorphism databases

DMDM83305554.

2D gel databases

OGPP49792.

Proteomic databases

PaxDbP49792.
PeptideAtlasP49792.
PRIDEP49792.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283195; ENSP00000283195; ENSG00000153201.
GeneID5903.
KEGGhsa:5903.
UCSCuc002tem.4. human.

Organism-specific databases

CTD5903.
GeneCardsGC02P109335.
H-InvDBHIX0002358.
HGNCHGNC:9848. RANBP2.
HPAHPA018437.
HPA023960.
MIM601181. gene.
608033. phenotype.
neXtProtNX_P49792.
Orphanet263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBPA34209.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5171.
HOGENOMHOG000089994.
HOVERGENHBG092361.
InParanoidP49792.
KOK12172.
OMASATKCIA.
OrthoDBEOG7X0VG5.
PhylomeDBP49792.
TreeFamTF314797.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressP49792.
BgeeP49792.
CleanExHS_RANBP2.
GenevestigatorP49792.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
2.30.29.30. 4 hits.
InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR022011. IR1-M.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00515. TPR_1. 1 hit.
PF00641. zf-RanBP. 8 hits.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SMARTSM00160. RanBD. 4 hits.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view]
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50196. RANBD1. 4 hits.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
PS01358. ZF_RANBP2_1. 8 hits.
PS50199. ZF_RANBP2_2. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRANBP2. human.
EvolutionaryTraceP49792.
GeneWikiRANBP2.
GenomeRNAi5903.
NextBio22964.
PROP49792.
SOURCESearch...

Entry information

Entry nameRBP2_HUMAN
AccessionPrimary (citable) accession number: P49792
Secondary accession number(s): Q13074 expand/collapse secondary AC list , Q15280, Q53TE2, Q59FH7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM