P49792 (RBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RANBP2
Synonyms:	NUP358

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3224 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Ref.6 Ref.7 Ref.10 Ref.29 Ref.30
Pathway	Protein modification; protein sumoylation.
Subunit structure	Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with PARK2. Interacts with sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform PML-4) Ref.10 Ref.11 Ref.12 Ref.15 Ref.22 Ref.29 Ref.30
Subcellular location	Nucleus. Nucleus membrane. Nucleus › nuclear pore complex. Note: Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. Ref.8 Ref.32
Domain	Contains a dozen F-X-F-G repeats in the C-terminal half. The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (Ref.32). Only about half of the residues that surround the PPIA active site cleft are conserved. Ref.32
Post-translational modification	Polyubiquitinated by PARK2, which leads to proteasomal degradation. The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC By similarity.
Involvement in disease	Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. Note: The disease is caused by mutations affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (Ref.33). Ref.33
Sequence similarities	Contains 1 PPIase cyclophilin-type domain. Contains 4 RanBD1 domains. Contains 8 RanBP2-type zinc fingers. Contains 7 TPR repeats.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport Ubl conjugation pathway mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Ligase
PTM	Disulfide bond Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cytokine-mediated signaling pathway Traceable author statement. Source: Reactome glucose transport Traceable author statement. Source: Reactome mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mitotic nuclear envelope disassembly Traceable author statement. Source: Reactome negative regulation of glucokinase activity Inferred from electronic annotation. Source: Ensembl protein folding Inferred from electronic annotation. Source: InterPro protein import into nucleus Traceable author statement Ref.2. Source: ProtInc protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC protein sumoylation Inferred from direct assay PubMed 17264123PubMed 22155184. Source: UniProtKB regulation of gluconeogenesis involved in cellular glucose homeostasis Inferred from electronic annotation. Source: Ensembl regulation of glucose transport Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome viral process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Ensembl nuclear inclusion body Inferred from direct assay Ref.8. Source: UniProtKB nuclear membrane Inferred from direct assay Ref.8. Source: UniProtKB nuclear pore nuclear basket Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW Ran GTPase binding Traceable author statement Ref.2. Source: ProtInc ligase activity Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	3	EBI-973138,EBI-641062
PARK2	O60260	11	EBI-973138,EBI-716346
PDLIM3	Q53GG5	3	EBI-973138,EBI-5658852

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3224

3224

E3 SUMO-protein ligase RanBP2

PRO_0000204913

Regions

Repeat

26 – 59

34

TPR 1

Repeat

60 – 93

34

TPR 2

Repeat

94 – 128

35

TPR 3

Repeat

165 – 201

37

TPR 4

Repeat

287 – 319

33

TPR 5

Repeat

583 – 616

34

TPR 6

Repeat

648 – 681

34

TPR 7

Domain

1171 – 1307

137

RanBD1 1

Domain

2012 – 2148

137

RanBD1 2

Domain

2309 – 2445

137

RanBD1 3

Repeat

2633 – 2685

53

1

Repeat

2711 – 2761

51

2

Domain

2911 – 3046

136

RanBD1 4

Domain

3067 – 3223

157

PPIase cyclophilin-type

Zinc finger

1351 – 1381

31

RanBP2-type 1

Zinc finger

1415 – 1444

30

RanBP2-type 2

Zinc finger

1479 – 1508

30

RanBP2-type 3

Zinc finger

1543 – 1572

30

RanBP2-type 4

Zinc finger

1606 – 1635

30

RanBP2-type 5

Zinc finger

1665 – 1694

30

RanBP2-type 6

Zinc finger

1724 – 1753

30

RanBP2-type 7

Zinc finger

1781 – 1810

30

RanBP2-type 8

Region

2631 – 2635

5

Interaction with sumoylated RANGAP1

Region

2633 – 2761

129

2 X 50 AA approximate repeats

Region

2633 – 2710

78

Required for E3 SUMO-ligase activity

Region

2633 – 2685

53

Interaction with UBE2I

Region

2686 – 2761

76

Interaction with SUMO1

Amino acid modifications

Modified residue

19

1

Phosphothreonine Ref.19 Ref.23 Ref.24

Modified residue

21

1

Phosphoserine Ref.16 Ref.19 Ref.23 Ref.24

Modified residue

781

1

Phosphoserine Ref.19 Ref.24

Modified residue

788

1

Phosphoserine By similarity

Modified residue

837

1

Phosphoserine Ref.24

Modified residue

948

1

Phosphoserine Ref.19 Ref.24

Modified residue

955

1

Phosphoserine Ref.19 Ref.23 Ref.24

Modified residue

1107

1

Phosphoserine Ref.23

Modified residue

1110

1

Phosphoserine Ref.19 Ref.24

Modified residue

1144

1

Phosphothreonine Ref.16 Ref.19

Modified residue

1160

1

Phosphoserine Ref.19 Ref.24 Ref.26

Modified residue

1396

1

Phosphothreonine Ref.19 Ref.23

Modified residue

1412

1

Phosphothreonine Ref.24

Modified residue

1443

1

Phosphoserine Ref.19

Modified residue

1456

1

Phosphoserine Ref.19 Ref.26

Modified residue

1509

1

Phosphoserine Ref.19 Ref.24

Modified residue

1573

1

Phosphoserine Ref.19

Modified residue

1835

1

Phosphoserine Ref.24

Modified residue

1869

1

Phosphoserine Ref.19

Modified residue

1871

1

Phosphoserine Ref.23

Modified residue

2246

1

Phosphoserine By similarity

Modified residue

2270

1

Phosphoserine Ref.19 Ref.23

Modified residue

2293

1

Phosphothreonine By similarity

Modified residue

2297

1

Phosphoserine By similarity

Modified residue

2510

1

Phosphoserine By similarity

Modified residue

2613

1

Phosphothreonine Ref.19

Modified residue

2668

1

Phosphoserine Ref.19 Ref.23 Ref.26

Modified residue

2741

1

Phosphoserine Ref.19

Modified residue

2743

1

Phosphothreonine Ref.19

Modified residue

2900

1

Phosphoserine Ref.19 Ref.23 Ref.24 Ref.26

Modified residue

3207

1

Phosphoserine Ref.24 Ref.26

Cross-link

2592

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.10

Natural variations

Natural variant

548

1

V → L.
Corresponds to variant rs1057954 [ dbSNP | Ensembl ].

VAR_029765

Natural variant

580

1

E → K.
Corresponds to variant rs4012065 [ dbSNP | Ensembl ].

VAR_029766

Natural variant

581

1

C → Y.
Corresponds to variant rs1057957 [ dbSNP | Ensembl ].

VAR_029767

Natural variant

585

1

T → M in IIAE3. Ref.33

VAR_054997

Natural variant

653

1

T → I in IIAE3. Ref.33

VAR_054998

Natural variant

656

1

I → V in IIAE3. Ref.33

VAR_054999

Natural variant

725

1

S → G.
Corresponds to variant rs17414315 [ dbSNP | Ensembl ].

VAR_050575

Natural variant

784

1

R → K. Ref.2
Corresponds to variant rs2912838 [ dbSNP | Ensembl ].

VAR_023939

Natural variant

1870

1

P → L.
Corresponds to variant rs2889846 [ dbSNP | Ensembl ].

VAR_029768

Natural variant

1892

1

P → A.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].

VAR_014886

Natural variant

1892

1

P → R.
Corresponds to variant rs12770 [ dbSNP | Ensembl ].

VAR_050576

Experimental info

Mutagenesis

2632

1

V → K: Abolishes interaction with sumoylated RANGAP1. Ref.11

Mutagenesis

2634

1

I → K: Abolishes interaction with sumoylated RANGAP1. Ref.11

Mutagenesis

2635

1

V → K: Abolishes interaction with sumoylated RANGAP1. Ref.11

Mutagenesis

2640

1

P → A: No effect on SUMO E3 ligase activity. Ref.10

Mutagenesis

2645

1

K → A: No effect on SUMO E3 ligase activity. Ref.10

Mutagenesis

2651

1

L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10

Mutagenesis

2652

1

K → A: No effect on SUMO E3 ligase activity. Ref.10

Mutagenesis

2653

1

L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10

Mutagenesis

2654

1

P → A: Impairs SUMO E3 ligase activity. Ref.10

Mutagenesis

2655

1

P → A: No effect on SUMO E3 ligase activity. Ref.10

Mutagenesis

2656

1

T → A: Impairs SUMO E3 ligase activity. Ref.10

Mutagenesis

2657

1

F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10

Mutagenesis

2658

1

F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. Ref.10

Mutagenesis

2659

1

C → S or A: Impairs SUMO E3 ligase activity. Ref.10

Mutagenesis

2676

1

D → A: Impairs SUMO E3 ligase activity. Ref.10

Mutagenesis

2677

1

F → A: Impairs SUMO E3 ligase activity. Ref.10

Mutagenesis

2689

1

Y → A: Impairs SUMO E3 ligase activity. Ref.10

Sequence conflict

777

1

H → R in AAC41758. Ref.1

Sequence conflict

2207

1

S → A in AAA85838. Ref.5

Sequence conflict

2210

1

T → P in AAA85838. Ref.5

Sequence conflict

2216

1

E → V in AAA85838. Ref.5

Sequence conflict

2436

1

F → C in AAA85838. Ref.5

Sequence conflict

2475

1

T → P in AAA85838. Ref.5

Sequence conflict

2531

1

K → N in AAA85838. Ref.5

Sequence conflict

2545

1

F → C Ref.5

Secondary structure

1

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3224

Helix Strand Turn

Details...

Helix

5 – 18

14

Helix

22 – 26

5

Helix

29 – 38

10

Helix

42 – 55

14

Helix

60 – 72

13

Helix

76 – 89

14

Helix

94 – 107

14

Helix

112 – 124

13

Helix

129 – 141

13

Beta strand

1190 – 1204

15

Beta strand

1206 – 1209

4

Beta strand

1211 – 1227

17

Beta strand

1231 – 1235

5

Turn

1237 – 1239

3

Beta strand

1242 – 1244

3

Beta strand

1263 – 1270

8

Beta strand

1277 – 1284

8

Helix

1288 – 1300

13

Beta strand

2028 – 2030

3

Beta strand

2032 – 2046

15

Turn

2047 – 2050

4

Beta strand

2051 – 2065

15

Beta strand

2071 – 2077

7

Turn

2078 – 2081

4

Beta strand

2082 – 2088

7

Beta strand

2095 – 2097

3

Beta strand

2105 – 2111

7

Beta strand

2113 – 2115

3

Beta strand

2117 – 2125

9

Helix

2129 – 2145

17

Turn

2146 – 2148

3

Beta strand

2632 – 2637

6

Helix

2642 – 2650

9

Helix

2657 – 2661

5

Beta strand

2663 – 2665

3

Helix

2677 – 2682

6

Turn

2683 – 2686

4

Turn

2926 – 2929

4

Beta strand

2930 – 2944

15

Turn

2945 – 2948

4

Beta strand

2949 – 2963

15

Turn

2964 – 2967

4

Beta strand

2968 – 2974

7

Turn

2976 – 2978

3

Beta strand

2981 – 2986

6

Beta strand

2994 – 2996

3

Beta strand

3000 – 3009

10

Beta strand

3016 – 3026

11

Helix

3027 – 3047

21

Beta strand

3065 – 3072

8

Beta strand

3075 – 3084

10

Turn

3086 – 3088

3

Helix

3090 – 3101

12

Turn

3102 – 3104

3

Beta strand

3112 – 3117

6

Turn

3118 – 3120

3

Beta strand

3121 – 3124

4

Turn

3127 – 3129

3

Beta strand

3130 – 3133

4

Beta strand

3157 – 3160

4

Beta strand

3168 – 3170

3

Beta strand

3172 – 3177

6

Helix

3180 – 3182

3

Turn

3183 – 3185

3

Beta strand

3188 – 3194

7

Helix

3196 – 3203

8

Beta strand

3216 – 3223

8

Sequences

	Sequence		Length	Mass (Da)
	P49792 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 4CD9A3D5E77183FB	FASTA	3,224	358,199
	10 20 30 40 50 60 MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP 70 80 90 100 110 120 KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWLER 130 140 150 160 170 180 AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR 190 200 210 220 230 240 LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA 250 260 270 280 290 300 NLMLLTLSTR DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM 310 320 330 340 350 360 GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN 370 380 390 400 410 420 LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLT 430 440 450 460 470 480 RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPHETSR LETNAPESIC 490 500 510 520 530 540 ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH 550 560 570 580 590 600 RKAVPGNVAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG 610 620 630 640 650 660 RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV 670 680 690 700 710 720 NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK 730 740 750 760 770 780 IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP 790 800 810 820 830 840 SPTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR 850 860 870 880 890 900 WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 910 920 930 940 950 960 PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD 970 980 990 1000 1010 1020 YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP 1030 1040 1050 1060 1070 1080 TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG 1090 1100 1110 1120 1130 1140 YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS 1150 1160 1170 1180 1190 1200 VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK 1210 1220 1230 1240 1250 1260 LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS 1270 1280 1290 1300 1310 1320 DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVAMASNQAV 1330 1340 1350 1360 1370 1380 RIVKEPTSHD NKDICKSDAG NLNFEFQVAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP 1390 1400 1410 1420 1430 1440 SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN 1450 1460 1470 1480 1490 1500 TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA 1510 1520 1530 1540 1550 1560 ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA 1570 1580 1590 1600 1610 1620 TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE 1630 1640 1650 1660 1670 1680 ASATKCIACQ NPGKQNQTTS AVSTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA 1690 1700 1710 1720 1730 1740 SATKCIACQN PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS 1750 1760 1770 1780 1790 1800 ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK 1810 1820 1830 1840 1850 1860 CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS KFGNTEQGFK 1870 1880 1890 1900 1910 1920 FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENGT 1930 1940 1950 1960 1970 1980 GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS 1990 2000 2010 2020 2030 2040 SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV 2050 2060 2070 2080 2090 2100 KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG 2110 2120 2130 2140 2150 2160 SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT 2170 2180 2190 2200 2210 2220 GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP 2230 2240 2250 2260 2270 2280 TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS 2290 2300 2310 2320 2330 2340 PAKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY 2350 2360 2370 2380 2390 2400 RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER 2410 2420 2430 2440 2450 2460 VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR 2470 2480 2490 2500 2510 2520 ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST SETTPKAVVS PPKFVFGSES 2530 2540 2550 2560 2570 2580 VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPKKCELS 2590 2600 2610 2620 2630 2640 KNSDIEQSSD SKVKNLFASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP 2650 2660 2670 2680 2690 2700 TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE 2710 2720 2730 2740 2750 2760 ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV 2770 2780 2790 2800 2810 2820 QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS 2830 2840 2850 2860 2870 2880 TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF 2890 2900 2910 2920 2930 2940 GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL 2950 2960 2970 2980 2990 3000 YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN 3010 3020 3030 3040 3050 3060 NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK 3070 3080 3090 3100 3110 3120 ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF 3130 3140 3150 3160 3170 3180 VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFVITLKKAE 3190 3200 3210 3220 HLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQI

References

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

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L41840 Genomic DNA. Translation: AAC41758.1.
D42063 mRNA. Translation: BAA07662.1.
AC010095 Genomic DNA. Translation: AAY14984.1.
AB209483 mRNA. Translation: BAD92720.1.
U19248 mRNA. Translation: AAA85838.1.

PIR

S58884.

RefSeq

NP_006258.3. NM_006267.4.

UniGene

Hs.199561.
Hs.715056.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P49792.

SMR

P49792. Positions 3-145, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

111839. 90 interactions.

DIP

DIP-37654N.

IntAct

P49792. 39 interactions.

MINT

MINT-191403.

STRING

9606.ENSP00000283195.

PTM databases

PhosphoSite

P49792.

Polymorphism databases

DMDM

83305554.

2D gel databases

OGP

P49792.

Proteomic databases

PaxDb

P49792.

PeptideAtlas

P49792.

PRIDE

P49792.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000283195; ENSP00000283195; ENSG00000153201.

GeneID

5903.

KEGG

hsa:5903.

UCSC

uc002tem.4. human.

Organism-specific databases

CTD

5903.

GeneCards

GC02P109335.

H-InvDB

HIX0002358.

HGNC

HGNC:9848. RANBP2.

HPA

HPA018437.
HPA023960.

MIM

601181. gene.
608033. phenotype.

neXtProt

NX_P49792.

Orphanet

263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.

PharmGKB

PA34209.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5171.

HOGENOM

HOG000089994.

HOVERGEN

HBG092361.

InParanoid

P49792.

KO

K12172.

OMA

SATKCIA.

OrthoDB

EOG7X0VG5.

PhylomeDB

P49792.

TreeFam

TF314797.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6900. Immune System.

UniPathway

UPA00886.

Gene expression databases

ArrayExpress

P49792.

Bgee

P49792.

CleanEx

HS_RANBP2.

Genevestigator

P49792.

Family and domain databases

Gene3D

1.25.40.10. 2 hits.
2.30.29.30. 4 hits.

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR022011. IR1-M.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]

Pfam

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]

PRINTS

PR00153. CSAPPISMRASE.

SMART

SM00160. RanBD. 4 hits.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view]

SUPFAM

SSF50891. SSF50891. 1 hit.

PROSITE

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]

ProtoNet

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Other

ChiTaRS

RANBP2. human.

EvolutionaryTrace

P49792.

GeneWiki

RANBP2.

GenomeRNAi

5903.

NextBio

22964.

PRO

P49792.

SOURCE

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Entry information

Entry name

RBP2_HUMAN

Accession

Primary (citable) accession number: P49792
Secondary accession number(s): Q13074 , Q15280, Q53TE2, Q59FH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 6, 2005
Last modified:	February 19, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.