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Entry version 66 (07 Oct 2020)
Sequence version 1 (21 Mar 2012)
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Protein

E3 SUMO-protein ligase RanBP2

Gene

RANBP2

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (By similarity). Binds single-stranded RNA (in vitro) (PubMed:22959972). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.By similarity1 Publication

Caution

Despite the presence of a PPIase cyclophilin-type domain, it has probably no peptidyl-prolyl cis-trans isomerase activity.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-ProRule annotationAdd BLAST30

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding, Transferase
Biological processmRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00886

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 SUMO-protein ligase RanBP2 (EC:2.3.2.-By similarity)
Alternative name(s):
358 kDa nucleoporin
Nuclear pore complex protein Nup358
Nucleoporin Nup358
Ran-binding protein 2
Short name:
RanBP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RANBP2
Synonyms:NUP358
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPan troglodytes (Chimpanzee)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9598 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002277 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004245241 – 3224E3 SUMO-protein ligase RanBP2Add BLAST3224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19PhosphothreonineBy similarity1
Modified residuei21PhosphoserineBy similarity1
Modified residuei779PhosphothreonineBy similarity1
Modified residuei781PhosphoserineBy similarity1
Modified residuei788PhosphoserineBy similarity1
Modified residuei837PhosphoserineBy similarity1
Modified residuei945Asymmetric dimethylarginineBy similarity1
Modified residuei948PhosphoserineBy similarity1
Modified residuei955PhosphoserineBy similarity1
Modified residuei1016Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei1016Omega-N-methylarginine; alternateBy similarity1
Modified residuei1098PhosphothreonineBy similarity1
Modified residuei1103PhosphoserineBy similarity1
Modified residuei1107PhosphoserineBy similarity1
Modified residuei1110PhosphoserineBy similarity1
Modified residuei1144PhosphothreonineBy similarity1
Modified residuei1160PhosphoserineBy similarity1
Modified residuei1249PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1396PhosphothreonineBy similarity1
Modified residuei1412PhosphothreonineBy similarity1
Cross-linki1414Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1443PhosphoserineBy similarity1
Modified residuei1450PhosphoserineBy similarity1
Modified residuei1456PhosphoserineBy similarity1
Modified residuei1509PhosphoserineBy similarity1
Modified residuei1520PhosphoserineBy similarity1
Modified residuei1573PhosphoserineBy similarity1
Cross-linki1596Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1655Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1714Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1835PhosphoserineBy similarity1
Modified residuei1869PhosphoserineBy similarity1
Modified residuei1871PhosphoserineBy similarity1
Modified residuei1977N6-acetyllysineBy similarity1
Modified residuei2005PhosphothreonineBy similarity1
Modified residuei2008PhosphoserineBy similarity1
Cross-linki2022Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2153PhosphothreonineBy similarity1
Modified residuei2246PhosphoserineBy similarity1
Modified residuei2251PhosphoserineBy similarity1
Modified residuei2270PhosphoserineBy similarity1
Modified residuei2280PhosphoserineBy similarity1
Modified residuei2290PhosphoserineBy similarity1
Modified residuei2293PhosphothreonineBy similarity1
Modified residuei2297PhosphoserineBy similarity1
Modified residuei2462PhosphoserineBy similarity1
Modified residuei2493PhosphoserineBy similarity1
Modified residuei2510PhosphoserineBy similarity1
Cross-linki2522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2526PhosphoserineBy similarity1
Cross-linki2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki2612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2613PhosphothreonineBy similarity1
Modified residuei2666PhosphotyrosineBy similarity1
Modified residuei2668PhosphoserineBy similarity1
Modified residuei2741PhosphoserineBy similarity1
Modified residuei2743PhosphothreonineBy similarity1
Cross-linki2792Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2805PhosphoserineBy similarity1
Cross-linki2815Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2900PhosphoserineBy similarity1
Modified residuei3207PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Polyubiquitinated by PRKN, which leads to proteasomal degradation.By similarity
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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
H2QII6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSPTRG00000012332, Expressed in testis and 7 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the nuclear pore complex.

Forms a complex with NXT1, NXF1 and RANGAP1.

Forms a tight complex with RANBP1 and UBE2I.

Interacts with SUMO1 but not SUMO2.

Interacts with PRKN.

Interacts with sumoylated RANGAP1.

Interacts with CDCA8.

Interacts with PML (isoform PML-4).

Interacts with BICD2.

Interacts with MCM3AP isoform GANP.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9598.ENSPTRP00000021122

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
H2QII6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati26 – 59TPR 1PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati60 – 93TPR 2PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati94 – 128TPR 3PROSITE-ProRule annotation1 PublicationAdd BLAST35
Repeati165 – 201TPR 4PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati287 – 319TPR 5PROSITE-ProRule annotation1 PublicationAdd BLAST33
Repeati583 – 616TPR 6PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati648 – 681TPR 7PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati1001 – 10021By similarity2
Repeati1101 – 11022By similarity2
Repeati1142 – 11433By similarity2
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1171 – 1307RanBD1 1PROSITE-ProRule annotationAdd BLAST137
Repeati1459 – 14604By similarity2
Repeati1523 – 15245By similarity2
Repeati1586 – 15876By similarity2
Repeati1852 – 18537By similarity2
Repeati1861 – 18628By similarity2
Repeati1900 – 19019By similarity2
Repeati1938 – 193910By similarity2
Repeati1961 – 196211By similarity2
Domaini2012 – 2148RanBD1 2PROSITE-ProRule annotationAdd BLAST137
Repeati2260 – 226112By similarity2
Domaini2309 – 2445RanBD1 3PROSITE-ProRule annotationAdd BLAST137
Repeati2516 – 251713By similarity2
Repeati2535 – 253614By similarity2
Repeati2545 – 254615By similarity2
Repeati2633 – 268511 PublicationAdd BLAST53
Repeati2711 – 276121 PublicationAdd BLAST51
Repeati2840 – 284116By similarity2
Repeati2842 – 284317By similarity2
Repeati2863 – 286418By similarity2
Repeati2880 – 288119By similarity2
Domaini2911 – 3046RanBD1 4PROSITE-ProRule annotationAdd BLAST136
Domaini3067 – 3223PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157
Repeati3106 – 310720By similarity2
Repeati3189 – 319021By similarity2
Repeati3205 – 320622By similarity2

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1001 – 320622 X 2 AA repeats of F-GCuratedAdd BLAST2206
Regioni2147 – 2287Interaction with BICD2By similarityAdd BLAST141
Regioni2631 – 2635Interaction with sumoylated RANGAP1By similarity5
Regioni2633 – 27612 X 50 AA approximate repeatsAdd BLAST129
Regioni2633 – 2710Required for E3 SUMO-ligase activityBy similarityAdd BLAST78
Regioni2633 – 2685Interaction with UBE2IBy similarityAdd BLAST53
Regioni2686 – 2761Interaction with SUMO1By similarityAdd BLAST76

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro). Only about half of the residues that surround the PPIA active site cleft are conserved (By similarity).By similarity
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited.Curated

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RanBP2 E3 ligase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0864, Eukaryota
KOG0865, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000378_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
H2QII6

TreeFam database of animal gene trees

More...
TreeFami
TF314797

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.10, 1 hit
2.30.29.30, 4 hits
2.40.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029000, Cyclophilin-like_dom_sf
IPR020892, Cyclophilin-type_PPIase_CS
IPR002130, Cyclophilin-type_PPIase_dom
IPR022011, IR1-M
IPR011993, PH-like_dom_sf
IPR000156, Ran_bind_dom
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf
IPR019734, TPR_repeat
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12185, IR1-M, 2 hits
PF00160, Pro_isomerase, 1 hit
PF00638, Ran_BP1, 4 hits
PF00641, zf-RanBP, 8 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00153, CSAPPISMRASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00160, RanBD, 4 hits
SM00028, TPR, 1 hit
SM00547, ZnF_RBZ, 8 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452, SSF48452, 1 hit
SSF50891, SSF50891, 1 hit
SSF90209, SSF90209, 7 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

H2QII6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRSKADVER YIASVQGSTP SPRQKSIKGF YFAKLYYEAK EYDLAKKYIC
60 70 80 90 100
TYINVQERDP KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI
110 120 130 140 150
AELLCKNDVT DGRAKYWVER AAKLFPGSPA VYKLKEQLLD 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
DVQESRELLE SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
310 320 330 340 350
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR
360 370 380 390 400
LSQSGHMLLN LSRGKQDFLR EIVETFANKS GQSALYDALF SSQSPKDTSF
410 420 430 440 450
LGSDDIGNID VREPELEDLA RYDVGAIRAH DGSLQHLTWL GLQWNSLPAL
460 470 480 490 500
PGIRKWLKQL FHHLPQETSR LETNAPESIC ILDLEVFLLG VVYTSHLQLK
510 520 530 540 550
EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH RKAVPGNAAK
560 570 580 590 600
LRLLVQHEIN TLRAQEKHGL QPALLVHWAK CLQKTGSGLN SFYDQREYIG
610 620 630 640 650
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA
660 670 680 690 700
HITFAILDVV NGNIEDAMTA FESIQSVVSY WNLALIFHRK AEDIENDALS
710 720 730 740 750
PEEQEECKNY LRKTRDYLIK IIDDSDSNLS VVKKLPVPLE SVKEMLKSVM
760 770 780 790 800
QELEAYSEGG PLYTNGSLRN ADSEIKHSTP SHTRYSLSPS 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 NVATASNQAV RIVKEPTSHD NKDICKSDAG NLNFEFQFAK
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 ASATKCVACQ NPGKQNQTTS AVSTPASSET
1660 1670 1680 1690 1700
SRAPKSGFEG MFTKKEGQWD CSVCLVRNEA SATKCIACQS 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 DSPGSQVGTG FKSNFSEKAS
1860 1870 1880 1890 1900
KFGNTEQGFK FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF
1910 1920 1930 1940 1950
GISEPGNQEK KSEKPLENDT GFQAQDISGQ KNGSGVIFGQ 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 PGKLNQSGTS 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
VWLWTAYDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT
2460 2470 2480 2490 2500
PHVSRSSTPR ESPCGKIAVA VLEETTRERT DVTQGDDVAD AASEVEVSST
2510 2520 2530 2540 2550
SETTTKAVVS PPKFVFGSES VKSIFSSEKS KPFAFGNTSA TGSLFGFSFN
2560 2570 2580 2590 2600
APLKSNNSET SSVAQSGSES KVEPNKCELS KNSDIEQSSD SKVKNLSASF
2610 2620 2630 2640 2650
PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP TAEQKALATK
2660 2670 2680 2690 2700
LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL EGSEKCRPLE
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 QFFITLKKAE LLDFKHVVFG FVKDGMDTVK
3210 3220
KIESFGSPKG SVCRRITITE CGQI
Length:3,224
Mass (Da):358,148
Last modified:March 21, 2012 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i005EBC43EDEAACBB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AACZ03015911 Genomic DNA No translation available.

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACZ03015911 Genomic DNA No translation available.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GA1X-ray1.15A1-145[»]
4GA2X-ray0.95A1-145[»]
SMRiH2QII6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000021122

Proteomic databases

PaxDbiH2QII6

Phylogenomic databases

eggNOGiKOG0864, Eukaryota
KOG0865, Eukaryota
HOGENOMiCLU_000378_1_0_1
InParanoidiH2QII6
TreeFamiTF314797

Enzyme and pathway databases

UniPathwayiUPA00886

Gene expression databases

BgeeiENSPTRG00000012332, Expressed in testis and 7 other tissues

Family and domain databases

Gene3Di1.25.40.10, 1 hit
2.30.29.30, 4 hits
2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000, Cyclophilin-like_dom_sf
IPR020892, Cyclophilin-type_PPIase_CS
IPR002130, Cyclophilin-type_PPIase_dom
IPR022011, IR1-M
IPR011993, PH-like_dom_sf
IPR000156, Ran_bind_dom
IPR013026, TPR-contain_dom
IPR011990, TPR-like_helical_dom_sf
IPR019734, TPR_repeat
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
PfamiView protein in Pfam
PF12185, IR1-M, 2 hits
PF00160, Pro_isomerase, 1 hit
PF00638, Ran_BP1, 4 hits
PF00641, zf-RanBP, 8 hits
PRINTSiPR00153, CSAPPISMRASE
SMARTiView protein in SMART
SM00160, RanBD, 4 hits
SM00028, TPR, 1 hit
SM00547, ZnF_RBZ, 8 hits
SUPFAMiSSF48452, SSF48452, 1 hit
SSF50891, SSF50891, 1 hit
SSF90209, SSF90209, 7 hits
PROSITEiView protein in 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBP2_PANTR
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: H2QII6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: March 21, 2012
Last modified: October 7, 2020
This is version 66 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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