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P49792

- RBP2_HUMAN

UniProt

P49792 - RBP2_HUMAN

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Protein

E3 SUMO-protein ligase RanBP2

Gene

RANBP2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB.5 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1351 – 138131RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1415 – 144430RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1479 – 150830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1543 – 157230RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1606 – 163530RanBP2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1665 – 169430RanBP2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1724 – 175330RanBP2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1781 – 181030RanBP2-type 8PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: InterPro
  3. Ran GTPase binding Source: ProtInc
  4. RNA binding Source: UniProtKB-KW
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. glucose transport Source: Reactome
  4. hexose transport Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear envelope disassembly Source: Reactome
  7. mRNA transport Source: UniProtKB-KW
  8. negative regulation of glucokinase activity Source: Ensembl
  9. protein folding Source: InterPro
  10. protein import into nucleus Source: ProtInc
  11. protein sumoylation Source: UniProtKB
  12. regulation of gluconeogenesis involved in cellular glucose homeostasis Source: Ensembl
  13. regulation of glucose transport Source: Reactome
  14. small molecule metabolic process Source: Reactome
  15. transmembrane transport Source: Reactome
  16. viral process Source: Reactome
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

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RANBP2
Synonyms:NUP358
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9848. RANBP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
  3. mitochondrion Source: Ensembl
  4. nuclear inclusion body Source: UniProtKB
  5. nuclear membrane Source: UniProtKB
  6. nuclear pore Source: UniProtKB
  7. nuclear pore nuclear basket Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
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 (PubMed:19118815).1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti585 – 5851T → M in IIAE3. 1 Publication
VAR_054997
Natural varianti653 – 6531T → I in IIAE3. 1 Publication
VAR_054998
Natural varianti656 – 6561I → V in IIAE3. 1 Publication
VAR_054999

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2632 – 26321V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
Mutagenesisi2634 – 26341I → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
Mutagenesisi2635 – 26351V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
Mutagenesisi2640 – 26401P → A: No effect on SUMO E3 ligase activity. 1 Publication
Mutagenesisi2645 – 26451K → A: No effect on SUMO E3 ligase activity. 1 Publication
Mutagenesisi2651 – 26511L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
Mutagenesisi2652 – 26521K → A: No effect on SUMO E3 ligase activity. 1 Publication
Mutagenesisi2653 – 26531L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
Mutagenesisi2654 – 26541P → A: Impairs SUMO E3 ligase activity. 1 Publication
Mutagenesisi2655 – 26551P → A: No effect on SUMO E3 ligase activity. 1 Publication
Mutagenesisi2656 – 26561T → A: Impairs SUMO E3 ligase activity. 1 Publication
Mutagenesisi2657 – 26571F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
Mutagenesisi2658 – 26581F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
Mutagenesisi2659 – 26591C → S or A: Impairs SUMO E3 ligase activity. 1 Publication
Mutagenesisi2676 – 26761D → A: Impairs SUMO E3 ligase activity. 1 Publication
Mutagenesisi2677 – 26771F → A: Impairs SUMO E3 ligase activity. 1 Publication
Mutagenesisi2689 – 26891Y → A: Impairs SUMO E3 ligase activity. 1 Publication

Organism-specific databases

MIMi608033. phenotype.
Orphaneti263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA34209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 32243224E3 SUMO-protein ligase RanBP2PRO_0000204913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphothreonine3 Publications
Modified residuei21 – 211Phosphoserine4 Publications
Modified residuei781 – 7811Phosphoserine2 Publications
Modified residuei788 – 7881PhosphoserineBy similarity
Modified residuei837 – 8371Phosphoserine1 Publication
Modified residuei948 – 9481Phosphoserine2 Publications
Modified residuei955 – 9551Phosphoserine3 Publications
Modified residuei1107 – 11071Phosphoserine1 Publication
Modified residuei1110 – 11101Phosphoserine2 Publications
Modified residuei1144 – 11441Phosphothreonine2 Publications
Modified residuei1160 – 11601Phosphoserine3 Publications
Modified residuei1396 – 13961Phosphothreonine2 Publications
Modified residuei1412 – 14121Phosphothreonine1 Publication
Modified residuei1443 – 14431Phosphoserine1 Publication
Modified residuei1456 – 14561Phosphoserine2 Publications
Modified residuei1509 – 15091Phosphoserine2 Publications
Modified residuei1573 – 15731Phosphoserine1 Publication
Modified residuei1835 – 18351Phosphoserine1 Publication
Modified residuei1869 – 18691Phosphoserine1 Publication
Modified residuei1871 – 18711Phosphoserine1 Publication
Modified residuei1977 – 19771N6-acetyllysineBy similarity
Modified residuei2246 – 22461PhosphoserineBy similarity
Modified residuei2270 – 22701Phosphoserine2 Publications
Modified residuei2293 – 22931PhosphothreonineBy similarity
Modified residuei2297 – 22971PhosphoserineBy similarity
Modified residuei2510 – 25101PhosphoserineBy similarity
Cross-linki2592 – 2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei2613 – 26131Phosphothreonine1 Publication
Modified residuei2668 – 26681Phosphoserine3 Publications
Modified residuei2741 – 27411Phosphoserine1 Publication
Modified residuei2743 – 27431Phosphothreonine1 Publication
Modified residuei2900 – 29001Phosphoserine4 Publications
Modified residuei3207 – 32071Phosphoserine2 Publications

Post-translational modificationi

Polyubiquitinated by PARK2, which leads to proteasomal degradation.1 Publication
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

Keywords - PTMi

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

Proteomic databases

MaxQBiP49792.
PaxDbiP49792.
PeptideAtlasiP49792.
PRIDEiP49792.

2D gel databases

OGPiP49792.

PTM databases

PhosphoSiteiP49792.

Expressioni

Gene expression databases

BgeeiP49792.
CleanExiHS_RANBP2.
ExpressionAtlasiP49792. baseline and differential.
GenevestigatoriP49792.

Organism-specific databases

HPAiHPA018437.
HPA023960.

Interactioni

Subunit structurei

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).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046263EBI-973138,EBI-641062
PARK2O6026011EBI-973138,EBI-716346
PDLIM3Q53GG53EBI-973138,EBI-5658852

Protein-protein interaction databases

BioGridi111839. 102 interactions.
DIPiDIP-37654N.
IntActiP49792. 40 interactions.
MINTiMINT-191403.
STRINGi9606.ENSP00000283195.

Structurei

Secondary structure

1
3224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi22 – 265Combined sources
Helixi29 – 3810Combined sources
Helixi42 – 5514Combined sources
Helixi60 – 7213Combined sources
Helixi76 – 8914Combined sources
Helixi94 – 10714Combined sources
Helixi112 – 12413Combined sources
Helixi129 – 14113Combined sources
Beta strandi1190 – 120415Combined sources
Beta strandi1206 – 12094Combined sources
Beta strandi1211 – 122717Combined sources
Beta strandi1231 – 12355Combined sources
Turni1237 – 12393Combined sources
Beta strandi1242 – 12443Combined sources
Beta strandi1263 – 12708Combined sources
Beta strandi1277 – 12848Combined sources
Helixi1288 – 130013Combined sources
Beta strandi2028 – 20303Combined sources
Beta strandi2032 – 204615Combined sources
Turni2047 – 20504Combined sources
Beta strandi2051 – 206515Combined sources
Beta strandi2071 – 20777Combined sources
Turni2078 – 20814Combined sources
Beta strandi2082 – 20887Combined sources
Beta strandi2095 – 20973Combined sources
Beta strandi2105 – 21117Combined sources
Beta strandi2113 – 21153Combined sources
Beta strandi2117 – 21259Combined sources
Helixi2129 – 214517Combined sources
Turni2146 – 21483Combined sources
Beta strandi2632 – 26376Combined sources
Helixi2642 – 26509Combined sources
Helixi2657 – 26615Combined sources
Beta strandi2663 – 26653Combined sources
Helixi2677 – 26826Combined sources
Turni2683 – 26864Combined sources
Turni2926 – 29294Combined sources
Beta strandi2930 – 294415Combined sources
Turni2945 – 29484Combined sources
Beta strandi2949 – 296315Combined sources
Turni2964 – 29674Combined sources
Beta strandi2968 – 29747Combined sources
Turni2976 – 29783Combined sources
Beta strandi2981 – 29866Combined sources
Beta strandi2994 – 29963Combined sources
Beta strandi3000 – 300910Combined sources
Beta strandi3016 – 302611Combined sources
Helixi3027 – 304721Combined sources
Beta strandi3065 – 30728Combined sources
Beta strandi3075 – 308410Combined sources
Turni3086 – 30883Combined sources
Helixi3090 – 310112Combined sources
Turni3102 – 31043Combined sources
Beta strandi3112 – 31176Combined sources
Turni3118 – 31203Combined sources
Beta strandi3121 – 31244Combined sources
Turni3127 – 31293Combined sources
Beta strandi3130 – 31334Combined sources
Beta strandi3157 – 31604Combined sources
Beta strandi3168 – 31703Combined sources
Beta strandi3172 – 31776Combined sources
Helixi3180 – 31823Combined sources
Turni3183 – 31853Combined sources
Beta strandi3188 – 31947Combined sources
Helixi3196 – 32038Combined sources
Beta strandi3216 – 32238Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP49792.
SMRiP49792. Positions 3-145, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati26 – 5934TPR 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati60 – 9334TPR 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati94 – 12835TPR 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati165 – 20137TPR 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati287 – 31933TPR 51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati583 – 61634TPR 61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati648 – 68134TPR 71 PublicationPROSITE-ProRule annotationAdd
BLAST
Domaini1171 – 1307137RanBD1 1PROSITE-ProRule annotationAdd
BLAST
Domaini2012 – 2148137RanBD1 2PROSITE-ProRule annotationAdd
BLAST
Domaini2309 – 2445137RanBD1 3PROSITE-ProRule annotationAdd
BLAST
Repeati2633 – 26855311 PublicationAdd
BLAST
Repeati2711 – 27615121 PublicationAdd
BLAST
Domaini2911 – 3046136RanBD1 4PROSITE-ProRule annotationAdd
BLAST
Domaini3067 – 3223157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2631 – 26355Interaction with sumoylated RANGAP1
Regioni2633 – 27611292 X 50 AA approximate repeatsAdd
BLAST
Regioni2633 – 271078Required for E3 SUMO-ligase activityAdd
BLAST
Regioni2633 – 268553Interaction with UBE2IAdd
BLAST
Regioni2686 – 276176Interaction with SUMO1Add
BLAST

Domaini

Contains a dozen F-X-F-G repeats in the C-terminal half.1 Publication
The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (PubMed:23353830). Only about half of the residues that surround the PPIA active site cleft are conserved.1 Publication

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 4 RanBD1 domains.PROSITE-ProRule annotation
Contains 8 RanBP2-type zinc fingers.PROSITE-ProRule annotation
Contains 7 TPR repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1351 – 138131RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1415 – 144430RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1479 – 150830RanBP2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1543 – 157230RanBP2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1606 – 163530RanBP2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1665 – 169430RanBP2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1724 – 175330RanBP2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1781 – 181030RanBP2-type 8PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiSATKCIA.
OrthoDBiEOG7X0VG5.
PhylomeDBiP49792.
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_like_dom.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF12185. 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]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00160. RanBD. 4 hits.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. 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]

Sequencei

Sequence statusi: Complete.

P49792-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC
60 70 80 90 100
TYINVQERDP KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI
110 120 130 140 150
AELLCKNDVT DGRAKYWLER AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL
160 170 180 190 200
FDLIQSELYV RPDDVHVNIR LVEVYRSTKR LKDAVAHCHE AERNIALRSS
210 220 230 240 250
LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA NLMLLTLSTR
260 270 280 290 300
DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
310 320 330 340 350
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR
360 370 380 390 400
LSQSGHMLLN LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF
410 420 430 440 450
LGSDDIGNID VREPELEDLT RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL
460 470 480 490 500
PGIRKWLKQL FHHLPHETSR LETNAPESIC ILDLEVFLLG VVYTSHLQLK
510 520 530 540 550
EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH RKAVPGNVAK
560 570 580 590 600
LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG
610 620 630 640 650
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA
660 670 680 690 700
HITFAILDAV NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS
710 720 730 740 750
PEEQEECKNY LRKTRDYLIK IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM
760 770 780 790 800
QELEDYSEGG PLYKNGSLRN ADSEIKHSTP SPTRYSLSPS KSYKYSPKTP
810 820 830 840 850
PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR WPTENYGPDS
860 870 880 890 900
VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
910 920 930 940 950
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA
960 970 980 990 1000
TGILSPRGDD YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE
1010 1020 1030 1040 1050
FGKTNFVQPM PGEGLRPSLP TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ
1060 1070 1080 1090 1100
VVTQPPPAAY SNSESLLGLL TSDKPLQGDG YSGAKPIPGG QTIGPRNTFN
1110 1120 1130 1140 1150
FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS VFGTPTLETA
1160 1170 1180 1190 1200
NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
1210 1220 1230 1240 1250
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP
1260 1270 1280 1290 1300
DMKLTPNAGS DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE
1310 1320 1330 1340 1350
AQSILKAPGT NVAMASNQAV RIVKEPTSHD NKDICKSDAG NLNFEFQVAK
1360 1370 1380 1390 1400
KEGSWWHCNS CSLKNASTAK KCVSCQNLNP SNKELVGPPL AETVFTPKTS
1410 1420 1430 1440 1450
PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN TKSANKSGSS
1460 1470 1480 1490 1500
FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA
1510 1520 1530 1540 1550
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS
1560 1570 1580 1590 1600
SCLVRNEANA TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE
1610 1620 1630 1640 1650
GMFTKKEGQW DCSVCLVRNE ASATKCIACQ NPGKQNQTTS AVSTPASSET
1660 1670 1680 1690 1700
SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA SATKCIACQN PGKQNQTTSA
1710 1720 1730 1740 1750
VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS ATKCIACQCP
1760 1770 1780 1790 1800
SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK
1810 1820 1830 1840 1850
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS
1860 1870 1880 1890 1900
KFGNTEQGFK FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF
1910 1920 1930 1940 1950
GISEPGNQEK KSEKPLENGT GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL
1960 1970 1980 1990 2000
AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS SQYGKMANKA NTSGDFEKDD
2010 2020 2030 2040 2050
DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV KLFRFDAEVS
2060 2070 2080 2090 2100
QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG
2110 2120 2130 2140 2150
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP
2160 2170 2180 2190 2200
LQTPHKLVDT GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG
2210 2220 2230 2240 2250
TGAAGASDTT IKPNPENTGP TLEWDNYDLR EDALDDSVSS SSVHASPLAS
2260 2270 2280 2290 2300
SPVRKNLFRF GESTTGFNFS FKSALSPSKS PAKLNQSGTS VGTDEESDVT
2310 2320 2330 2340 2350
QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY RYDKDVGQWK
2360 2370 2380 2390 2400
ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER
2410 2420 2430 2440 2450
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT
2460 2470 2480 2490 2500
PHVSRSSTPR ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST
2510 2520 2530 2540 2550
SETTPKAVVS PPKFVFGSES VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN
2560 2570 2580 2590 2600
APLKSNNSET SSVAQSGSES KVEPKKCELS KNSDIEQSSD SKVKNLFASF
2610 2620 2630 2640 2650
PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP TAEQKALATK
2660 2670 2680 2690 2700
LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE
2710 2720 2730 2740 2750
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG
2760 2770 2780 2790 2800
EDFQSELQKV QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT
2810 2820 2830 2840 2850
KSISSPSVSS ETMDKPVDLS TRKEIDTDST SQGESKIVSF GFGSSTGLSF
2860 2870 2880 2890 2900
ADLASSNSGD FAFGSKDKNF QWANTGAAVF GTQSVGTQSA GKVGEDEDGS
2910 2920 2930 2940 2950
DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL YRWDRDVSQW
2960 2970 2980 2990 3000
KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN
3010 3020 3030 3040 3050
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG
3060 3070 3080 3090 3100
HVSLAAELSK ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC
3110 3120 3130 3140 3150
TGEKGFGFKN SIFHRVIPDF VCQGGDITKH DGTGGQSIYG DKFEDENFDV
3160 3170 3180 3190 3200
KHTGPGLLSM ANQGQNTNNS QFVITLKKAE HLDFKHVVFG FVKDGMDTVK
3210 3220
KIESFGSPKG SVCRRITITE CGQI
Length:3,224
Mass (Da):358,199
Last modified:December 6, 2005 - v2
Checksum:i4CD9A3D5E77183FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti777 – 7771H → R in AAC41758. (PubMed:7775481)Curated
Sequence conflicti2207 – 22071S → A in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2210 – 22101T → P in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2216 – 22161E → V in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2436 – 24361F → C in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2475 – 24751T → P in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2531 – 25311K → N in AAA85838. (PubMed:7724562)Curated
Sequence conflicti2545 – 25451F → C(PubMed:7724562)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti548 – 5481V → L.
Corresponds to variant rs1057954 [ dbSNP | Ensembl ].
VAR_029765
Natural varianti580 – 5801E → K.
Corresponds to variant rs4012065 [ dbSNP | Ensembl ].
VAR_029766
Natural varianti581 – 5811C → Y.
Corresponds to variant rs1057957 [ dbSNP | Ensembl ].
VAR_029767
Natural varianti585 – 5851T → M in IIAE3. 1 Publication
VAR_054997
Natural varianti653 – 6531T → I in IIAE3. 1 Publication
VAR_054998
Natural varianti656 – 6561I → V in IIAE3. 1 Publication
VAR_054999
Natural varianti725 – 7251S → G.
Corresponds to variant rs17414315 [ dbSNP | Ensembl ].
VAR_050575
Natural varianti784 – 7841R → K.1 Publication
Corresponds to variant rs2912838 [ dbSNP | Ensembl ].
VAR_023939
Natural varianti1870 – 18701P → L.
Corresponds to variant rs2889846 [ dbSNP | Ensembl ].
VAR_029768
Natural varianti1892 – 18921P → A.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].
VAR_014886
Natural varianti1892 – 18921P → R.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].
VAR_050576

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2079.1.
PIRiS58884.
RefSeqiNP_006258.3. NM_006267.4.
UniGeneiHs.199561.
Hs.715056.

Genome annotation databases

EnsembliENST00000283195; ENSP00000283195; ENSG00000153201.
GeneIDi5903.
KEGGihsa:5903.
UCSCiuc002tem.4. human.

Polymorphism databases

DMDMi83305554.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2079.1.
PIRi S58884.
RefSeqi NP_006258.3. NM_006267.4.
UniGenei Hs.199561.
Hs.715056.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RRP X-ray 2.96 B/D 1171-1304 [» ]
1XKE NMR - A 2028-2154 [» ]
1Z5S X-ray 3.01 D 2631-2711 [» ]
3UIN X-ray 2.60 D 2629-2695 [» ]
3UIO X-ray 2.60 D 2631-2695 [» ]
3UIP X-ray 2.29 D 2631-2695 [» ]
4GA0 X-ray 1.15 A 1-145 [» ]
4I9Y X-ray 1.75 A/B/C/D/E/F 3062-3224 [» ]
4L6E X-ray 2.50 A 2907-3050 [» ]
4LQW X-ray 1.95 A/B 3057-3224 [» ]
ProteinModelPortali P49792.
SMRi P49792. Positions 3-145, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111839. 102 interactions.
DIPi DIP-37654N.
IntActi P49792. 40 interactions.
MINTi MINT-191403.
STRINGi 9606.ENSP00000283195.

PTM databases

PhosphoSitei P49792.

Polymorphism databases

DMDMi 83305554.

2D gel databases

OGPi P49792.

Proteomic databases

MaxQBi P49792.
PaxDbi P49792.
PeptideAtlasi P49792.
PRIDEi P49792.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283195 ; ENSP00000283195 ; ENSG00000153201 .
GeneIDi 5903.
KEGGi hsa:5903.
UCSCi uc002tem.4. human.

Organism-specific databases

CTDi 5903.
GeneCardsi GC02P109335.
H-InvDB HIX0002358.
HGNCi HGNC:9848. RANBP2.
HPAi HPA018437.
HPA023960.
MIMi 601181. gene.
608033. phenotype.
neXtProti NX_P49792.
Orphaneti 263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBi PA34209.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5171.
GeneTreei ENSGT00760000119119.
HOGENOMi HOG000089994.
HOVERGENi HBG092361.
InParanoidi P49792.
KOi K12172.
OMAi SATKCIA.
OrthoDBi EOG7X0VG5.
PhylomeDBi P49792.
TreeFami TF314797.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSi RANBP2. human.
EvolutionaryTracei P49792.
GeneWikii RANBP2.
GenomeRNAii 5903.
NextBioi 22964.
PROi P49792.
SOURCEi Search...

Gene expression databases

Bgeei P49792.
CleanExi HS_RANBP2.
ExpressionAtlasi P49792. baseline and differential.
Genevestigatori P49792.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
2.30.29.30. 4 hits.
2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR020892. 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_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF12185. 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 ]
PRINTSi PR00153. CSAPPISMRASE.
SMARTi SM00160. RanBD. 4 hits.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view ]
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. 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. 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. 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. Cited for: VARIANTS IIAE3 MET-585; ILE-653 AND VAL-656.

Entry informationi

Entry nameiRBP2_HUMAN
AccessioniPrimary (citable) accession number: P49792
Secondary accession number(s): Q13074
, Q15280, Q53TE2, Q59FH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3