Q9H6Z4 (RANB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ran-binding protein 3
Short name=RanBP3

Gene names

Name:

RANBP3

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. Ref.1 Ref.6 Ref.7 Ref.8 Ref.12
Subunit structure	Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling. Ref.1 Ref.6 Ref.7 Ref.8 Ref.12
Subcellular location	Cytoplasm. Nucleus Ref.12.
Tissue specificity	Widely expressed with high levels in testis and heart. Ref.1
Sequence similarities	Contains 1 RanBD1 domain.
Sequence caution	The sequence AAH04349.1 differs from that shown. Reason: Aberrant splicing. The sequence CAB43293.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular transport Inferred from electronic annotation. Source: InterPro protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: LIFEdb
Molecular_function	Ran GTPase binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RCC1	P18754	2	EBI-992681,EBI-992720

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H6Z4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9H6Z4-2)

Also known as: Ranbp3-a;

The sequence of this isoform differs from the canonical sequence as follows:
     226-230: Missing.

Isoform 3 (identifier: Q9H6Z4-3)

Also known as: Ranbp3-b;

The sequence of this isoform differs from the canonical sequence as follows:
     27-94: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 567

567

Ran-binding protein 3

PRO_0000097165

Regions

Domain

378 – 518

141

RanBD1

Compositional bias

76 – 81

6

Poly-Pro

Compositional bias

537 – 543

7

Poly-Asp

Amino acid modifications

Modified residue

21

1

N6-acetyllysine Ref.14

Modified residue

100

1

Phosphoserine Ref.11

Modified residue

101

1

Phosphoserine Ref.11

Modified residue

108

1

Phosphoserine Ref.9 Ref.11

Modified residue

115

1

Phosphotyrosine By similarity

Modified residue

124

1

Phosphothreonine Ref.11

Modified residue

219

1

Phosphoserine By similarity

Modified residue

221

1

Phosphoserine By similarity

Modified residue

333

1

Phosphoserine Ref.11 Ref.13 Ref.17

Modified residue

353

1

Phosphoserine Ref.11

Modified residue

355

1

Phosphoserine Ref.11

Modified residue

539

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

27 – 94

68

Missing in isoform 3.

VSP_011163

Alternative sequence

226 – 230

5

Missing in isoform 2.

VSP_011162

Natural variant

314

1

A → V.
Corresponds to variant rs10417885 [ dbSNP | Ensembl ].

VAR_051303

Experimental info

Sequence conflict

358 – 359

2

SS → PF in CAA69956. Ref.1

Sequence conflict

367

1

E → G in CAA69957. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

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.

.

.

567

Helix Strand Turn

Details...

Turn

389 – 391

3

Beta strand

399 – 412

14

Turn

413 – 416

4

Beta strand

417 – 432

16

Turn

434 – 436

3

Beta strand

439 – 447

9

Turn

448 – 450

3

Beta strand

453 – 458

6

Beta strand

465 – 469

5

Beta strand

472 – 476

5

Beta strand

487 – 491

5

Helix

494 – 519

26

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 203B5A900512743C	FASTA	567	60,210
	10 20 30 40 50 60 MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE 70 80 90 100 110 120 HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK 130 140 150 160 170 180 RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP 190 200 210 220 230 240 QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES 250 260 270 280 290 300 SNASEEEACE KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL 310 320 330 340 350 360 QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA AESGSESSSQ 370 380 390 400 410 420 EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN VLQMQCKLFV FDKTSQSWVE 430 440 450 460 470 480 RGRGLLRLND MASTDDGTLQ SRLVMRTQGS LRLILNTKLW AQMQIDKASE KSIRITAMDT 490 500 510 520 530 540 EDQGVKVFLI SASSKDTGQL YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD 550 560 DDDVLAPSGA TAAGAGDEGD GQTTGST
	Isoform 2 (Ranbp3-a) [UniParc]. Checksum: 453AF2CD380BA7F1	FASTA	562	59,694
	10 20 30 40 50 60 MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH GTGHPESAGE 70 80 90 100 110 120 HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS SPEGGEDSDR EDGNYCPPVK 130 140 150 160 170 180 RERTSSLTQF PPSQSEERSS GFRLKPPTLI HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP 190 200 210 220 230 240 QPKALSQTVP SSGTNGVSLP ADCTGAVPAA SPDTAAWRSP SEAADEEKEP QKNESSNASE 250 260 270 280 290 300 EEACEKKDPA TQQAFVFGQN LRDRVKLINE SVDEADMENA GHPSADTPTA TNYFLQYISS 310 320 330 340 350 360 SLENSTNSAD ASSNKFVFGQ NMSERVLSPP KLNEVSSDAN RENAAAESGS ESSSQEATPE 370 380 390 400 410 420 KESLAESAAA YTKATARKCL LEKVEVITGE EAESNVLQMQ CKLFVFDKTS QSWVERGRGL 430 440 450 460 470 480 LRLNDMASTD DGTLQSRLVM RTQGSLRLIL NTKLWAQMQI DKASEKSIRI TAMDTEDQGV 490 500 510 520 530 540 KVFLISASSK DTGQLYAALH HRILALRSRV EQEQEAKMPA PEPGAAPSNE EDDSDDDDVL 550 560 APSGATAAGA GDEGDGQTTG ST
	Isoform 3 (Ranbp3-b) [UniParc]. Checksum: 3356FC66E6A21796	FASTA	499	53,411
	10 20 30 40 50 60 MADLANEEKP AIAPPVFVFQ KDKGQKRSAG GSSPEGGEDS DREDGNYCPP VKRERTSSLT 70 80 90 100 110 120 QFPPSQSEER SSGFRLKPPT LIHGQAPSAG LPSQKPKEQQ RSVLRPAVLQ APQPKALSQT 130 140 150 160 170 180 VPSSGTNGVS LPADCTGAVP AASPDTAAWR SPSEAADEVC ALEEKEPQKN ESSNASEEEA 190 200 210 220 230 240 CEKKDPATQQ AFVFGQNLRD RVKLINESVD EADMENAGHP SADTPTATNY FLQYISSSLE 250 260 270 280 290 300 NSTNSADASS NKFVFGQNMS ERVLSPPKLN EVSSDANREN AAAESGSESS SQEATPEKES 310 320 330 340 350 360 LAESAAAYTK ATARKCLLEK VEVITGEEAE SNVLQMQCKL FVFDKTSQSW VERGRGLLRL 370 380 390 400 410 420 NDMASTDDGT LQSRLVMRTQ GSLRLILNTK LWAQMQIDKA SEKSIRITAM DTEDQGVKVF 430 440 450 460 470 480 LISASSKDTG QLYAALHHRI LALRSRVEQE QEAKMPAPEP GAAPSNEEDD SDDDDVLAPS 490 GATAAGAGDE GDGQTTGST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human RanBP3, a group of nuclear RanGTP binding proteins." Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H. FEBS Lett. 427:330-336(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CHC1.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Colon and Testis.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[4]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM 3). Tissue: Eye.
[6]	"RanBP3 influences interactions between CRM1 and its nuclear protein export substrates." Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U. EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH XPO1.
[7]	"Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export." Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G. J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH XPO1.
[8]	"Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor." Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G. J. Biol. Chem. 277:17385-17388(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHC1.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[11]	"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 SER-100; SER-101; SER-108; THR-124; SER-333; SER-353; SER-355 AND SER-539, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling." Dai F., Lin X., Chang C., Feng X.H. Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, FUNCTION.
[13]	"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 SER-333, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, MASS SPECTROMETRY.
[15]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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-333, MASS SPECTROMETRY.
[18]	"Solution structure of the RAN_BP1 domain of RAN-binding protein-3." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 380-516.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y08697 mRNA. Translation: CAA69956.1.
Y08698 mRNA. Translation: CAA69957.1.
AK025300 mRNA. Translation: BAB15106.1.
AK314343 mRNA. Translation: BAG36985.1.
AL050149 mRNA. Translation: CAB43293.1. Different initiation.
AC004602 Genomic DNA. Translation: AAC14485.1.
AC104532 Genomic DNA. No translation available.
AC093050 Genomic DNA. No translation available.
AC005784 Genomic DNA. No translation available.
BC004349 mRNA. Translation: AAH04349.1. Sequence problems.

IPI

IPI00026337.
IPI00179121.
IPI00456728.
IPI00456729.

PIR

T08778.

RefSeq

NP_003615.2. NM_003624.2.
NP_015559.2. NM_007320.2.
NP_015561.1. NM_007322.2.

UniGene

Hs.531752.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CRF	NMR	-	A	380-511	[»]
2Y8F	X-ray	2.10	A/B/C/D	388-522	[»]
2Y8G	X-ray	1.61	A/B	388-522	[»]

ProteinModelPortal

Q9H6Z4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H6Z4. 4 interactions.

STRING

9606.ENSP00000341483.

PTM databases

PhosphoSite

Q9H6Z4.

Polymorphism databases

DMDM

51316528.

Proteomic databases

PaxDb

Q9H6Z4.

PeptideAtlas

Q9H6Z4.

PRIDE

Q9H6Z4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000034275; ENSP00000034275; ENSG00000031823.
ENST00000340578; ENSP00000341483; ENSG00000031823.
ENST00000439268; ENSP00000404837; ENSG00000031823.

GeneID

8498.

KEGG

hsa:8498.

UCSC

uc002mdv.3. human.
uc002mdx.3. human.
uc002mdy.3. human.

Organism-specific databases

CTD

8498.

GeneCards

GC19M005916.

HGNC

HGNC:9850. RANBP3.

HPA

HPA043375.
HPA043389.

MIM

603327. gene.

neXtProt

NX_Q9H6Z4.

PharmGKB

PA34211.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304969.

HOVERGEN

HBG061383.

InParanoid

Q9H6Z4.

KO

K15304.

OMA

EQEAKMP.

PhylomeDB

Q9H6Z4.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.

Gene expression databases

ArrayExpress

Q9H6Z4.

Bgee

Q9H6Z4.

CleanEx

HS_RANBP3.

Genevestigator

Q9H6Z4.

GermOnline

ENSG00000031823. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]

Pfam

PF00638. Ran_BP1. 1 hit.
[Graphical view]

SMART

SM00160. RanBD. 1 hit.
[Graphical view]

PROSITE

PS50196. RANBD1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RANBP3. human.

EvolutionaryTrace

Q9H6Z4.

GenomeRNAi

8498.

NextBio

31793.

SOURCE

Search...

Entry information

Entry name

RANB3_HUMAN

Accession

Primary (citable) accession number: Q9H6Z4
Secondary accession number(s): B2RAT8 , O60405, O75759, O75760, Q9BT47, Q9UG74

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 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.