O95218 (ZRAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger Ran-binding domain-containing protein 2

Alternative name(s):
Zinc finger protein 265
Zinc finger, splicing

Gene names

Name:	ZRANB2
Synonyms:	ZIS, ZNF265

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection. Ref.8
Subunit structure	Interacts with the C-terminal half of SNRNP70, the Arg/Ser-rich domain of AKAP17A as well as with U2AF1 and CLK1. Ref.8 Ref.13
Subcellular location	Nucleus Ref.8.
Domain	The RanBP2-type zinc fingers mediate binding to RNA.
Post-translational modification	Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the ZRANB2 family. Contains 2 RanBP2-type zinc fingers.
Sequence caution	The sequence AAD09746.1 differs from that shown. Reason: Frameshift at position 236. The sequence AAD09747.1 differs from that shown. Reason: Frameshift at position 236. The sequence BAD92805.1 differs from that shown. Reason: Intron retention. The sequence CAB66879.1 differs from that shown. Reason: Frameshift at position 236.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing Traceable author statement. Source: ProtInc mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Traceable author statement. Source: ProtInc
Molecular function	RNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.13. Source: IntAct sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKAP17A	Q02040	4	EBI-1051583,EBI-1042725
ARRB1	P49407	4	EBI-1051583,EBI-743313
ARRB2	P32121	4	EBI-1051583,EBI-714559

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95218-1)

Also known as: ZIS-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: O95218-2)

Also known as: ZIS-2;

The sequence of this isoform differs from the canonical sequence as follows:
     310-330: RRHRSSSGSSHSGSRSSSKKK → SQVIGENTKQP

Note: Phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

Zinc finger Ran-binding domain-containing protein 2

PRO_0000066585

Regions

Zinc finger

9 – 40

32

RanBP2-type 1

Zinc finger

65 – 94

30

RanBP2-type 2

Region

151 – 324

174

Required for nuclear targeting

Compositional bias

198 – 262

65

Arg/Ser-rich

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.18

Modified residue

54

1

N6-acetyllysine Ref.22

Modified residue

114

1

Phosphotyrosine By similarity

Modified residue

120

1

Phosphoserine Ref.10 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

153

1

Phosphoserine Ref.10 Ref.18 Ref.19 Ref.21

Modified residue

181

1

Phosphoserine Ref.10 Ref.11 Ref.18

Modified residue

188

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.15 Ref.18 Ref.20 Ref.21

Modified residue

193

1

Phosphoserine Ref.10 Ref.20

Modified residue

290

1

Phosphoserine By similarity

Modified residue

294

1

Phosphoserine By similarity

Modified residue

303

1

Phosphothreonine Ref.10 Ref.18

Modified residue

305

1

Phosphoserine Ref.10 Ref.12 Ref.18 Ref.21

Modified residue

307

1

Phosphoserine Ref.10 Ref.12 Ref.18 Ref.21

Natural variations

Alternative sequence

310 – 330

21

RRHRS…SSKKK → SQVIGENTKQP in isoform 2.

VSP_024945

Natural variant

207

1

R → G. Ref.6 Ref.7
Corresponds to variant rs11583800 [ dbSNP | Ensembl ].

VAR_030783

Experimental info

Sequence conflict

41

1

E → G in BAD96578. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

330

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Turn

18 – 20

3

Beta strand

32 – 34

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ZIS-1) [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 99BE2D12EBE0FF8E	FASTA	330	37,404
	10 20 30 40 50 60 MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS 70 80 90 100 110 120 RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES 130 140 150 160 170 180 DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL 190 200 210 220 230 240 SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR 250 260 270 280 290 300 SRSSSRERSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERNRKRSRS RSSSSGDRKK 310 320 330 RRTRSRSPER RHRSSSGSSH SGSRSSSKKK
	Isoform 2 (ZIS-2) [UniParc]. Checksum: 15F1DFB7CD6CF611	FASTA	320	36,318
	10 20 30 40 50 60 MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS 70 80 90 100 110 120 RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES 130 140 150 160 170 180 DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL 190 200 210 220 230 240 SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR 250 260 270 280 290 300 SRSSSRERSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERNRKRSRS RSSSSGDRKK 310 320 RRTRSRSPES QVIGENTKQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, characterization and mapping of the human ZIS (zinc-finger, splicing) gene." Nakano M., Yoshiura K., Oikawa M., Miyoshi O., Yamada K., Kondo S., Miwa N., Soeda E., Jinno Y., Fujii T., Niikawa N. Gene 225:59-65(1998) [PubMed: 9931435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Fetal brain.
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Uterus.
[3]	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] (ISOFORM 2). Tissue: Brain.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-207.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLY-207. Tissue: Skin.
[8]	"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing." Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J. J. Cell Biol. 154:25-32(2001) [PubMed: 11448987] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNRNP70; U2AF1 AND CLK1.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181; SER-188; SER-193; THR-303; SER-305 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-188, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-307, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265." Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J. Nucleic Acids Res. 34:4976-4986(2006) [PubMed: 16982639] [Abstract] Cited for: INTERACTION WITH AKAP17A.
[14]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: T-cell.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-120; SER-181; SER-188; THR-303; SER-153; SER-305 AND SER-307, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-153, MASS SPECTROMETRY. Tissue: Liver.
[20]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-193, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-188; SER-305 AND SER-307, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54, MASS SPECTROMETRY.
[23]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"The structure of the zinc finger domain from human splicing factor ZNF265 fold." Plambeck C.A., Kwan A.H.Y., Adams D.J., Westman B.J., van der Weyden L., Medcalf R.L., Morris B.J., Mackay J.P. J. Biol. Chem. 278:22805-22811(2003) [PubMed: 12657633] [Abstract] Cited for: STRUCTURE BY NMR OF 1-40, RNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF065391 mRNA. Translation: AAD09746.1. Frameshift.
AF065392 mRNA. Translation: AAD09747.1. Frameshift.
AL136945 mRNA. Translation: CAB66879.1. Frameshift.
AB209568 mRNA. Translation: BAD92805.1. Sequence problems.
AK222858 mRNA. Translation: BAD96578.1.
AL512443 Genomic DNA. Translation: CAH70058.1.
AL512443 Genomic DNA. Translation: CAH70059.1.
CH471059 Genomic DNA. Translation: EAX06433.1.
CH471059 Genomic DNA. Translation: EAX06435.1.
BC039814 mRNA. Translation: AAH39814.1.

IPI

IPI00029400.
IPI00219866.

RefSeq

NP_005446.2. NM_005455.4.
NP_976225.1. NM_203350.2.

UniGene

Hs.194718.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N0Z	NMR	-	A	1-40	[»]
2K1P	NMR	-	A	65-95	[»]
3G9Y	X-ray	1.40	A	65-95	[»]

ProteinModelPortal

O95218.

SMR

O95218. Positions 1-40, 67-95.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95218. 5 interactions.

STRING

O95218.

PTM databases

PhosphoSite

O95218.

Proteomic databases

PRIDE

O95218.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370920; ENSP00000359958; ENSG00000132485.

GeneID

9406.

KEGG

hsa:9406.

UCSC

uc001dfs.1. human.
uc001dft.1. human.

Organism-specific databases

CTD

9406.

GeneCards

GC01M071528.

H-InvDB

HIX0199826.

HGNC

HGNC:13058. ZRANB2.

MIM

604347. gene.

neXtProt

NX_O95218.

PharmGKB

PA37636.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11969.

GeneTree

ENSGT00600000084415.

HOVERGEN

HBG066285.

OMA

FGGGYND.

OrthoDB

EOG42V8H3.

PhylomeDB

O95218.

Gene expression databases

ArrayExpress

O95218.

Bgee

O95218.

CleanEx

HS_ZRANB2.

Genevestigator

O95218.

GermOnline

ENSG00000132485. Homo sapiens.

Family and domain databases

InterPro

IPR017337. UCP037956_Znf_RanB2.
IPR001876. Znf_RanBP2.
[Graphical view]

Pfam

PF00641. zf-RanBP. 2 hits.
[Graphical view]

PIRSF

PIRSF037956. UCP037956_ZnF_Ran. 1 hit.

SMART

SM00547. ZnF_RBZ. 2 hits.
[Graphical view]

PROSITE

PS01358. ZF_RANBP2_1. 2 hits.
PS50199. ZF_RANBP2_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

35236.

SOURCE

Search...

Entry information

Entry name

ZRAB2_HUMAN

Accession

Primary (citable) accession number: O95218
Secondary accession number(s): D3DQ75 , Q53GS3, Q59F92, Q5VV33, Q5VV34, Q8IXN6, Q9UP63

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2007
Last modified:	January 25, 2012
This is version 107 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.