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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)DescriptionActionsGraphical viewLength
Zinc fingeri1345 – 1375RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1410 – 1439RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1469 – 1498RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1494 – 1527RanBP2-type 4PROSITE-ProRule annotationAdd BLAST34
Zinc fingeri1558 – 1587RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1617 – 1646RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30

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-191859. snRNP Assembly.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00002049141 – 3053E3 SUMO-protein ligase RanBP2Add BLAST3053

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21PhosphoserineCombined sources1
Modified residuei779PhosphothreonineBy similarity1
Modified residuei781PhosphoserineCombined sources1
Modified residuei788PhosphoserineCombined sources1
Modified residuei837PhosphoserineBy similarity1
Modified residuei944Asymmetric dimethylarginineBy similarity1
Modified residuei947PhosphoserineBy similarity1
Modified residuei954PhosphoserineCombined sources1
Modified residuei1015Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei1015Omega-N-methylarginine; alternateBy similarity1
Modified residuei1096PhosphothreonineBy similarity1
Modified residuei1101PhosphoserineCombined sources1
Modified residuei1138PhosphothreonineBy similarity1
Modified residuei1154PhosphoserineCombined sources1
Modified residuei1243PhosphoserineBy similarity1
Modified residuei1407PhosphothreonineBy similarity1
Modified residuei1438PhosphoserineBy similarity1
Modified residuei1441PhosphoserineBy similarity1
Modified residuei1446PhosphoserineBy similarity1
Modified residuei1528PhosphoserineBy similarity1
Cross-linki1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1670PhosphoserineBy similarity1
Modified residuei1706PhosphoserineBy similarity1
Modified residuei1814N6-acetyllysineCombined sources1
Modified residuei1842PhosphothreonineCombined sources1
Modified residuei1845PhosphoserineCombined sources1
Modified residuei1990PhosphothreonineCombined sources1
Modified residuei2083PhosphoserineCombined sources1
Modified residuei2088PhosphoserineCombined sources1
Modified residuei2107PhosphoserineCombined sources1
Modified residuei2117PhosphoserineCombined sources1
Modified residuei2127PhosphoserineCombined sources1
Modified residuei2130PhosphothreonineCombined sources1
Modified residuei2134PhosphoserineCombined sources1
Modified residuei2299PhosphoserineCombined sources1
Modified residuei2330PhosphoserineCombined sources1
Modified residuei2348PhosphoserineCombined sources1
Modified residuei2364PhosphoserineBy similarity1
Cross-linki2430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei2450PhosphothreonineBy similarity1
Modified residuei2503PhosphotyrosineBy similarity1
Modified residuei2505PhosphoserineCombined sources1
Modified residuei2576PhosphoserineCombined sources1
Modified residuei2578PhosphothreonineCombined sources1
Cross-linki2627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2640PhosphoserineBy similarity1
Modified residuei2729PhosphoserineCombined sources1
Modified residuei3036PhosphoserineBy similarity1

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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9ERU9.
MaxQBiQ9ERU9.
PaxDbiQ9ERU9.
PeptideAtlasiQ9ERU9.
PRIDEiQ9ERU9.

PTM databases

iPTMnetiQ9ERU9.
PhosphoSitePlusiQ9ERU9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000003226.
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 interactors.
IntActiQ9ERU9. 88 interactors.
MINTiMINT-1659128.
STRINGi10090.ENSMUSP00000003310.

Structurei

3D structure databases

ProteinModelPortaliQ9ERU9.
SMRiQ9ERU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati26 – 59TPR 1Add BLAST34
Repeati60 – 93TPR 2Add BLAST34
Repeati94 – 128TPR 3Add BLAST35
Repeati165 – 201TPR 4Add BLAST37
Repeati288 – 319TPR 5Add BLAST32
Repeati583 – 616TPR 6Add BLAST34
Repeati648 – 681TPR 7Add BLAST34
Domaini1165 – 1301RanBD1 1PROSITE-ProRule annotationAdd BLAST137
Domaini1849 – 1985RanBD1 2PROSITE-ProRule annotationAdd BLAST137
Domaini2146 – 2282RanBD1 3PROSITE-ProRule annotationAdd BLAST137
Repeati2470 – 25221Add BLAST53
Repeati2546 – 25962Add BLAST51
Domaini2740 – 2875RanBD1 4PROSITE-ProRule annotationAdd BLAST136
Domaini2896 – 3052PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2468 – 2472Interaction with sumoylated RANGAP1By similarity5
Regioni2470 – 25962 X 50 AA approximate repeatsAdd BLAST127
Regioni2470 – 2545Required for E3 SUMO-ligase activityBy similarityAdd BLAST76
Regioni2470 – 2522Interaction with UBE2IBy similarityAdd BLAST53
Regioni2523 – 2596Interaction with SUMO1By similarityAdd BLAST74

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2074 – 2079Poly-Ser6
Compositional biasi2506 – 2509Poly-Glu4
Compositional biasi2638 – 2641Poly-Ser4

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)DescriptionActionsGraphical viewLength
Zinc fingeri1345 – 1375RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1410 – 1439RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1469 – 1498RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1494 – 1527RanBP2-type 4PROSITE-ProRule annotationAdd BLAST34
Zinc fingeri1558 – 1587RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1617 – 1646RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0864. Eukaryota.
KOG0865. Eukaryota.
COG0652. LUCA.
COG5171. LUCA.
GeneTreeiENSGT00840000129823.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiQ9ERU9.
KOiK12172.
OMAiKEGEWDC.
OrthoDBiEOG091G0BGL.
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)DescriptionActionsGraphical viewLength
Sequence conflicti213 – 222EYLESLQCLD → VGETYFSTVF in BAC31101 (PubMed:16141072).Curated10
Sequence conflicti985 – 1001LVAHA…VIEFG → IPGSRFKVSRIKGYRIWL in CAA60778 (PubMed:8603673).CuratedAdd BLAST17
Sequence conflicti1086 – 1089ISGQ → YLA in CAA60778 (PubMed:8603673).Curated4
Sequence conflicti1269L → F in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1273E → G in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1276A → S in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1280K → Q in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1293E → G in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1297N → D in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1861E → D in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti2868 – 2869EC → DS in AAG17403 (PubMed:11353387).Curated2

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202582. 82 interactors.
IntActiQ9ERU9. 88 interactors.
MINTiMINT-1659128.
STRINGi10090.ENSMUSP00000003310.

PTM databases

iPTMnetiQ9ERU9.
PhosphoSitePlusiQ9ERU9.

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.
OMAiKEGEWDC.
OrthoDBiEOG091G0BGL.
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-191859. snRNP Assembly.
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

BgeeiENSMUSG00000003226.
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...

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: November 30, 2016
This is version 136 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.