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Protein

E3 SUMO-protein ligase RanBP2

Gene

Ranbp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (By similarity).By similarity

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1345 – 137531RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1410 – 143930RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1469 – 149830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1494 – 152734RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1558 – 158730RanBP2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1617 – 164630RanBP2-type 6PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase RanBP2 (EC:6.3.2.-)
Alternative name(s):
Ran-binding protein 2
Short name:
RanBP2
Gene namesi
Name:Ranbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:894323. Ranbp2.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus membrane By similarity
  • Nucleusnuclear pore complex By similarity

  • Note: Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30533053E3 SUMO-protein ligase RanBP2PRO_0000204914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei779 – 7791PhosphothreonineBy similarity
Modified residuei781 – 7811PhosphoserineCombined sources
Modified residuei788 – 7881PhosphoserineCombined sources
Modified residuei837 – 8371PhosphoserineBy similarity
Modified residuei947 – 9471PhosphoserineBy similarity
Modified residuei954 – 9541PhosphoserineCombined sources
Modified residuei1096 – 10961PhosphothreonineBy similarity
Modified residuei1101 – 11011PhosphoserineCombined sources
Modified residuei1138 – 11381PhosphothreonineBy similarity
Modified residuei1154 – 11541PhosphoserineCombined sources
Modified residuei1243 – 12431PhosphoserineBy similarity
Modified residuei1407 – 14071PhosphothreonineBy similarity
Modified residuei1438 – 14381PhosphoserineBy similarity
Modified residuei1441 – 14411PhosphoserineBy similarity
Modified residuei1446 – 14461PhosphoserineBy similarity
Modified residuei1528 – 15281PhosphoserineBy similarity
Cross-linki1557 – 1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1557 – 1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1616 – 1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1616 – 1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1670 – 16701PhosphoserineBy similarity
Modified residuei1706 – 17061PhosphoserineBy similarity
Modified residuei1814 – 18141N6-acetyllysineCombined sources
Modified residuei1842 – 18421PhosphothreonineCombined sources
Modified residuei1845 – 18451PhosphoserineCombined sources
Modified residuei1990 – 19901PhosphothreonineCombined sources
Modified residuei2083 – 20831PhosphoserineCombined sources
Modified residuei2088 – 20881PhosphoserineCombined sources
Modified residuei2107 – 21071PhosphoserineCombined sources
Modified residuei2117 – 21171PhosphoserineCombined sources
Modified residuei2127 – 21271PhosphoserineCombined sources
Modified residuei2130 – 21301PhosphothreonineCombined sources
Modified residuei2134 – 21341PhosphoserineCombined sources
Modified residuei2299 – 22991PhosphoserineCombined sources
Modified residuei2330 – 23301PhosphoserineCombined sources
Modified residuei2348 – 23481PhosphoserineCombined sources
Modified residuei2364 – 23641PhosphoserineBy similarity
Cross-linki2430 – 2430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki2432 – 2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei2450 – 24501PhosphothreonineBy similarity
Modified residuei2503 – 25031PhosphotyrosineBy similarity
Modified residuei2505 – 25051PhosphoserineCombined sources
Modified residuei2576 – 25761PhosphoserineCombined sources
Modified residuei2578 – 25781PhosphothreonineCombined sources
Cross-linki2627 – 2627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2640 – 26401PhosphoserineBy similarity
Modified residuei2729 – 27291PhosphoserineCombined sources
Modified residuei3036 – 30361PhosphoserineBy similarity

Post-translational modificationi

Polyubiquitinated by PARK2, which leads to proteasomal degradation.By similarity
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.

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9ERU9.
MaxQBiQ9ERU9.
PaxDbiQ9ERU9.
PeptideAtlasiQ9ERU9.
PRIDEiQ9ERU9.

PTM databases

iPTMnetiQ9ERU9.
PhosphoSiteiQ9ERU9.

Expressioni

Gene expression databases

BgeeiQ9ERU9.
CleanExiMM_RANBP2.
GenevisibleiQ9ERU9. MM.

Interactioni

Subunit structurei

Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with sumoylated RANGAP1. Interacts with CDCA8 (By similarity). Interacts with PARK2. Interacts with PML (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Park2Q9WVS62EBI-643756,EBI-973635

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202582. 82 interactions.
IntActiQ9ERU9. 87 interactions.
MINTiMINT-1659128.
STRINGi10090.ENSMUSP00000003310.

Structurei

3D structure databases

ProteinModelPortaliQ9ERU9.
SMRiQ9ERU9. Positions 3-145, 1163-1301, 1864-1991, 2468-2530, 2754-2877, 2891-3053.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati26 – 5934TPR 1Add
BLAST
Repeati60 – 9334TPR 2Add
BLAST
Repeati94 – 12835TPR 3Add
BLAST
Repeati165 – 20137TPR 4Add
BLAST
Repeati288 – 31932TPR 5Add
BLAST
Repeati583 – 61634TPR 6Add
BLAST
Repeati648 – 68134TPR 7Add
BLAST
Domaini1165 – 1301137RanBD1 1PROSITE-ProRule annotationAdd
BLAST
Domaini1849 – 1985137RanBD1 2PROSITE-ProRule annotationAdd
BLAST
Domaini2146 – 2282137RanBD1 3PROSITE-ProRule annotationAdd
BLAST
Repeati2470 – 2522531Add
BLAST
Repeati2546 – 2596512Add
BLAST
Domaini2740 – 2875136RanBD1 4PROSITE-ProRule annotationAdd
BLAST
Domaini2896 – 3052157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2468 – 24725Interaction with sumoylated RANGAP1By similarity
Regioni2470 – 25961272 X 50 AA approximate repeatsAdd
BLAST
Regioni2470 – 254576Required for E3 SUMO-ligase activityBy similarityAdd
BLAST
Regioni2470 – 252253Interaction with UBE2IBy similarityAdd
BLAST
Regioni2523 – 259674Interaction with SUMO1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2074 – 20796Poly-Ser
Compositional biasi2506 – 25094Poly-Glu
Compositional biasi2638 – 26414Poly-Ser

Domaini

Contains a dozen F-X-F-G repeats in the C-terminal half.
The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (By similarity). Only about half of the residues that surround the PPIA active site cleft are conserved.By similarity

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 4 RanBD1 domains.PROSITE-ProRule annotation
Contains 6 RanBP2-type zinc fingers.PROSITE-ProRule annotation
Contains 7 TPR repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1345 – 137531RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1410 – 143930RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1469 – 149830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1494 – 152734RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1558 – 158730RanBP2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1617 – 164630RanBP2-type 6PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0864. Eukaryota.
KOG0865. Eukaryota.
COG0652. LUCA.
COG5171. LUCA.
GeneTreeiENSGT00840000129823.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiQ9ERU9.
KOiK12172.
OMAiQWDCNVC.
OrthoDBiEOG7X0VG5.
TreeFamiTF314797.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
2.30.29.30. 4 hits.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR022011. IR1-M.
IPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00641. zf-RanBP. 6 hits.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00160. RanBD. 4 hits.
SM00028. TPR. 1 hit.
SM00547. ZnF_RBZ. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50729. SSF50729. 4 hits.
SSF50891. SSF50891. 1 hit.
SSF90209. SSF90209. 4 hits.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50196. RANBD1. 4 hits.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
PS01358. ZF_RANBP2_1. 6 hits.
PS50199. ZF_RANBP2_2. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ERU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS
60 70 80 90 100
TYINVQERDP KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI
110 120 130 140 150
AELLCKNDVT DGRAKYWVER AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL
160 170 180 190 200
FDLIQSELYA RPDDIHVNIR LVELYRSNKR LKDAVAHCHE ADRNTALRSS
210 220 230 240 250
LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA NLMLLTLSTR
260 270 280 290 300
DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK
310 320 330 340 350
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR
360 370 380 390 400
LSQSGHMLLN LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF
410 420 430 440 450
LGNDDIGNLD GQVPDPDDLA RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL
460 470 480 490 500
PAIRKWLKQL FHHLPQETSR LETNAPESIC ILDLEVFLLG VIYTSHLQLK
510 520 530 540 550
EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH RKALPGTSAK
560 570 580 590 600
LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG
610 620 630 640 650
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA
660 670 680 690 700
HITFAILDAV NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS
710 720 730 740 750
PEEQEECKNY LRKTRDYLIR ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM
760 770 780 790 800
QELEDYSEGG TLYKNGCWRS ADSELKHSTP SPTKYSLSPS KSYKYSPKTP
810 820 830 840 850
PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR WPAEPYGQDP
860 870 880 890 900
APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
910 920 930 940 950
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT
960 970 980 990 1000
GILSPRGDDY FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF
1010 1020 1030 1040 1050
GKSNFVQPMQ GEVIRPPLTT PAHTTQPTPF KFNSNFKSND GDFTFSSPQV
1060 1070 1080 1090 1100
VAQPPSTAYS NSESLLGLLT SDKPLQGDGY SGLKPISGQA SGSRNTFSFG
1110 1120 1130 1140 1150
SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA SELANKSHET
1160 1170 1180 1190 1200
DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG
1210 1220 1230 1240 1250
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP
1260 1270 1280 1290 1300
NAGSDRSFVW HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK
1310 1320 1330 1340 1350
ALGTNTSTAP NHTLRIVKES ATQDNKDICK ADGGNLNFEF QIVKKEGPYW
1360 1370 1380 1390 1400
NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL LGPPLVENGF APKTGLENAQ
1410 1420 1430 1440 1450
DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS SFVQTSFKFG
1460 1470 1480 1490 1500
QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK
1510 1520 1530 1540 1550
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG
1560 1570 1580 1590 1600
FEGMFAKKEG QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS
1610 1620 1630 1640 1650
ETSRSPKSGF EGLFPKKEGE WECAVCSVQN ESSSLKCVAC EASKPTHKPH
1660 1670 1680 1690 1700
EAPSAFTVGS KSQSNESAGS QVGTEFKSNF PEKNFKVGIS EQKFKFGHVD
1710 1720 1730 1740 1750
QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ EKGNQEKKSE
1760 1770 1780 1790 1800
KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK
1810 1820 1830 1840 1850
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF
1860 1870 1880 1890 1900
EPVVQMPEKV ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL
1910 1920 1930 1940 1950
KNEVNGKLRM LMRREQVLKV CANHWITTTM NLKPLSGSDR AWMWLASDFS
1960 1970 1980 1990 2000
DGDAKLEQLA AKFKTPELAE EFKQKFEECQ RLLLDIPLQT PHKLVDTGRA
2010 2020 2030 2040 2050
AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA PSASDTTAKQ
2060 2070 2080 2090 2100
NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES
2110 2120 2130 2140 2150
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV
2160 2170 2180 2190 2200
VPLPDLVEVS SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY
2210 2220 2230 2240 2250
DNKQVRIVMR RDQVLKLCAN HRITPDMTLQ TMKGTERVWV WTACDFADGE
2260 2270 2280 2290 2300
RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ EKDSLITPHV SHLSTPRESP
2310 2320 2330 2340 2350
CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE TTPKAVVSPP
2360 2370 2380 2390 2400
KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS
2410 2420 2430 2440 2450
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT
2460 2470 2480 2490 2500
PEKAQEKSKP EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR
2510 2520 2530 2540 2550
PGYVSEEEED DEDYEMAVKK LNGKLYLDDS EKPLEENLAD NDKECVIVWE
2560 2570 2580 2590 2600
KKPTVEERAK ADTLKLPPTF FCGVCSDTDE DNGNGEDFQS ELRKVCEAQK
2610 2620 2630 2640 2650
SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS SPVSGTMDKP
2660 2670 2680 2690 2700
VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK
2710 2720 2730 2740 2750
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV
2760 2770 2780 2790 2800
EVKSGEEDEE VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI
2810 2820 2830 2840 2850
LMRRDQVFKV CANHVITKAM ELKPLNVSNN ALVWTASDYA DGEAKVEQLA
2860 2870 2880 2890 2900
VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH TSLAAELSKD TNPVVFFDVC
2910 2920 2930 2940 2950
ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS IFHRVVPDFI
2960 2970 2980 2990 3000
CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ
3010 3020 3030 3040 3050
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC

GQL
Length:3,053
Mass (Da):341,121
Last modified:July 27, 2011 - v2
Checksum:i62FD4249DEE466AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 22210EYLESLQCLD → VGETYFSTVF in BAC31101 (PubMed:16141072).Curated
Sequence conflicti985 – 100117LVAHA…VIEFG → IPGSRFKVSRIKGYRIWL in CAA60778 (PubMed:8603673).CuratedAdd
BLAST
Sequence conflicti1086 – 10894ISGQ → YLA in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1269 – 12691L → F in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1273 – 12731E → G in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1276 – 12761A → S in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1280 – 12801K → Q in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1293 – 12931E → G in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1297 – 12971N → D in CAA60778 (PubMed:8603673).Curated
Sequence conflicti1861 – 18611E → D in CAA60778 (PubMed:8603673).Curated
Sequence conflicti2868 – 28692EC → DS in AAG17403 (PubMed:11353387).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279458 Genomic DNA. Translation: AAG17403.1.
AC158593 Genomic DNA. No translation available.
AK041932 mRNA. Translation: BAC31101.1.
X87337 mRNA. Translation: CAA60778.1.
CCDSiCCDS23861.1.
PIRiS57968.
RefSeqiNP_035370.2. NM_011240.3.
UniGeneiMm.431695.

Genome annotation databases

EnsembliENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226.
GeneIDi19386.
KEGGimmu:19386.
UCSCiuc007fdd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279458 Genomic DNA. Translation: AAG17403.1.
AC158593 Genomic DNA. No translation available.
AK041932 mRNA. Translation: BAC31101.1.
X87337 mRNA. Translation: CAA60778.1.
CCDSiCCDS23861.1.
PIRiS57968.
RefSeqiNP_035370.2. NM_011240.3.
UniGeneiMm.431695.

3D structure databases

ProteinModelPortaliQ9ERU9.
SMRiQ9ERU9. Positions 3-145, 1163-1301, 1864-1991, 2468-2530, 2754-2877, 2891-3053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202582. 82 interactions.
IntActiQ9ERU9. 87 interactions.
MINTiMINT-1659128.
STRINGi10090.ENSMUSP00000003310.

PTM databases

iPTMnetiQ9ERU9.
PhosphoSiteiQ9ERU9.

Proteomic databases

EPDiQ9ERU9.
MaxQBiQ9ERU9.
PaxDbiQ9ERU9.
PeptideAtlasiQ9ERU9.
PRIDEiQ9ERU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226.
GeneIDi19386.
KEGGimmu:19386.
UCSCiuc007fdd.1. mouse.

Organism-specific databases

CTDi5903.
MGIiMGI:894323. Ranbp2.

Phylogenomic databases

eggNOGiKOG0864. Eukaryota.
KOG0865. Eukaryota.
COG0652. LUCA.
COG5171. LUCA.
GeneTreeiENSGT00840000129823.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiQ9ERU9.
KOiK12172.
OMAiQWDCNVC.
OrthoDBiEOG7X0VG5.
TreeFamiTF314797.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiRanbp2. mouse.
PROiQ9ERU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERU9.
CleanExiMM_RANBP2.
GenevisibleiQ9ERU9. MM.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
2.30.29.30. 4 hits.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR022011. IR1-M.
IPR011993. PH_dom-like.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00641. zf-RanBP. 6 hits.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00160. RanBD. 4 hits.
SM00028. TPR. 1 hit.
SM00547. ZnF_RBZ. 6 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50729. SSF50729. 4 hits.
SSF50891. SSF50891. 1 hit.
SSF90209. SSF90209. 4 hits.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50196. RANBD1. 4 hits.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
PS01358. ZF_RANBP2_1. 6 hits.
PS50199. ZF_RANBP2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization, expression, and localization of murine Ran-binding protein 2 (RanBP2) gene."
    Fauser S., Aslanukov A., Roepman R., Ferreira P.A.
    Mamm. Genome 12:406-415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Ola.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-222.
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. "Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex."
    Wilken N., Senecal J.L., Scheer U., Dabauvalle M.C.
    Eur. J. Cell Biol. 68:211-219(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 985-2249.
  5. "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.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-954; SER-2083; THR-2130; SER-2134; SER-2348; SER-2505; SER-2576; THR-2578 AND SER-2729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954; SER-1154 AND SER-2729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-788 AND SER-2505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-781; SER-788; SER-954; SER-1101; SER-1154; THR-1842; SER-1845; THR-1990; SER-2083; SER-2088; SER-2107; SER-2117; SER-2127; THR-2130; SER-2134; SER-2299; SER-2330; SER-2505; SER-2576; THR-2578 AND SER-2729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport."
    Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.
    J. Cell Sci. 126:3141-3150(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRBP2_MOUSE
AccessioniPrimary (citable) accession number: Q9ERU9
Secondary accession number(s): E9QM01, Q61992, Q8C9K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.