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Entry version 113 (12 Aug 2020)
Sequence version 2 (23 Jan 2007)
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Protein

Tripartite motif-containing protein 5

Gene

TRIM5

Organism
Macaca mulatta (Rhesus macaque)
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

Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV-agm). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<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 ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination 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 fingeri15 – 60RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri92 – 133B box-typePROSITE-ProRule annotationAdd BLAST42

<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 functionTransferase
Biological processAntiviral defense, Autophagy, Immunity, Innate immunity, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00143

<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:
Tripartite motif-containing protein 5 (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase TRIM5Curated
TRIM5alpha
<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:TRIM5
<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>OrganismiMacaca mulatta (Rhesus macaque)
<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 identifieri9544 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
<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
  • UP000006718 <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

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi165I → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi172W → K: No effect on dimerization or higher order self-association; when associated with K-176. 1 Publication1
Mutagenesisi176I → K: No effect on dimerization or higher order self-association; when associated with K-172. 1 Publication1
Mutagenesisi194L → K: Fails to dimerise and exhibits reduced higher order self association. 1 Publication1
Mutagenesisi202L → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi205L → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi216L → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi219S → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi230M → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi234I → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi237L → K: No effect on dimerization or higher order self-association. 1 Publication1
Mutagenesisi247 – 249DLL → KDD: No effect on dimerization but exhibits a 3-fold decrease in the efficiency of higher order association. 1 Publication3

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00002734652 – 497Tripartite motif-containing protein 5Add BLAST496

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 residuei2N-acetylalanineBy similarity1
Modified residuei87PhosphoserineBy 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

Degraded in a proteasome-independent fashion in the absence of viral infection but in a proteasome-dependent fashion following exposure to restriction sensitive virus.By similarity
Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

<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
ENSMMUG00000000335, Expressed in spleen and 22 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

Can form homodimers and homotrimers. In addition to lower-order dimerization, also exhibits a higher-order multimerization and both low- and high-order multimerizations are essential for its restriction activity.

Interacts with MAP3K7/TAK1, TAB2 and TAB3 (By similarity).

Interacts with HSPA8/HSC70, PSMC2, PSMC4, PSMC5 and PSMD7 (PubMed:20053985, PubMed:22078707).

Interacts with SQSTM1 (PubMed:20357094, PubMed:25127057).

Interacts (via B30.2/SPRY domain) with HSPA1A/B.

Interacts with TRIM6 and TRIM34 (PubMed:21680743).

Interacts with BECN1; GABARAP (PubMed:25127057).

Interacts with ULK1 (phosphorylated form), GABARAPL1, GABARAPL2, MAP1LC3A and MAP1LC3C (By similarity).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q0PF16
With#Exp.IntAct
itself3EBI-923856,EBI-923856

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
695095, 11 interactors

Protein interaction database and analysis system

More...
IntActi
Q0PF16, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9544.ENSMMUP00000000454

<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

1497
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
Q0PF16

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 <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>Domaini283 – 497B30.2/SPRYPROSITE-ProRule annotationAdd BLAST215

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>Regioni187 – 200Required for interaction with GABARAP and for autophagy1 PublicationAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili137 – 225Sequence analysisAdd BLAST89

<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 B box-type zinc finger domain and the coiled-coil domain contribute to the higher and low order multimerization respectively which is essential for restriction activity (By similarity). The coiled coil domain is important for higher order multimerization by promoting the initial dimerization (PubMed:21680743).By similarity1 Publication
The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs.1 Publication
The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization.2 Publications

<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 TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 60RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri92 – 133B box-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2177, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013137_0_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q0PF16

KEGG Orthology (KO)

More...
KOi
K10648

Identification of Orthologs from Complete Genome Data

More...
OMAi
LTNFNYC

Database of Orthologous Groups

More...
OrthoDBi
740493at2759

TreeFam database of animal gene trees

More...
TreeFami
TF338674

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00021, BBOX, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.920, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
IPR003879, Butyrophylin_SPRY
IPR013320, ConA-like_dom_sf
IPR003877, SPRY_dom
IPR032917, TRIM5
IPR027370, Znf-RING_LisH
IPR000315, Znf_B-box
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

The PANTHER Classification System

More...
PANTHERi
PTHR24103:SF416, PTHR24103:SF416, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00622, SPRY, 1 hit
PF00643, zf-B_box, 1 hit
PF13445, zf-RING_UBOX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01407, BUTYPHLNCDUF

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00336, BBOX, 1 hit
SM00184, RING, 1 hit
SM00449, SPRY, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899, SSF49899, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50188, B302_SPRY, 1 hit
PS50119, ZF_BBOX, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

<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>Sequences (2)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q0PF16-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASGILLNVK EEVTCPICLE LLTEPLSLHC GHSFCQACIT ANHKKSMLYK
60 70 80 90 100
EGERSCPVCR ISYQPENIQP NRHVANIVEK LREVKLSPEE GQKVDHCARH
110 120 130 140 150
GEKLLLFCQE DSKVICWLCE RSQEHRGHHT FLMEEVAQEY HVKLQTALEM
160 170 180 190 200
LRQKQQEAEK LEADIREEKA SWKIQIDYDK TNVSADFEQL REILDWEESN
210 220 230 240 250
ELQNLEKEEE DILKSLTKSE TEMVQQTQYM RELISELEHR LQGSMMDLLQ
260 270 280 290 300
GVDGIIKRIE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RELTDARRYW
310 320 330 340 350
VDVTLAPNNI SHAVIAEDKR QVSSRNPQIM YQAPGTLFTF PSLTNFNYCT
360 370 380 390 400
GVLGSQSITS GKHYWEVDVS KKSAWILGVC AGFQSDAMYN IEQNENYQPK
410 420 430 440 450
YGYWVIGLQE GVKYSVFQDG SSHTPFAPFI VPLSVIICPD RVGVFVDYEA
460 470 480 490
CTVSFFNITN HGFLIYKFSQ CSFSKPVFPY LNPRKCTVPM TLCSPSS
Length:497
Mass (Da):57,299
Last modified:January 23, 2007 - v2
<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:i950166879B2E1A6F
GO
Isoform 2 (identifier: Q0PF16-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     301-333: VDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQA → GKEKSHYHQPPCGLSLLLSLSFRILYSLLGLVF
     334-497: Missing.

Show »
Length:333
Mass (Da):39,027
Checksum:i33D4B364F2DCB7EC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti7L → V in AAT48102 (PubMed:15249690).Curated1
Sequence conflicti174I → T in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti177D → Q in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti184S → L in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti192E → D in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti218K → N in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti221T → M in ABG67967 (Ref. 5) Curated1
Sequence conflicti229 – 230YM → SL in AAX86682 (PubMed:16226405).Curated2
Sequence conflicti236E → D in AAX86682 (PubMed:16226405).Curated1
Sequence conflicti236E → D in ABG67966 (Ref. 5) Curated1
Sequence conflicti307P → T in AAT48102 (PubMed:15249690).Curated1
Sequence conflicti307P → T in ABL14041 (PubMed:17142324).Curated1
Sequence conflicti307P → T in AAS48505 (Ref. 4) Curated1
Sequence conflicti333A → S in ABG67966 (Ref. 5) Curated1
Sequence conflicti339 – 341TFP → Q in ABG67966 (Ref. 5) Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_022569301 – 333VDVTL…IMYQA → GKEKSHYHQPPCGLSLLLSL SFRILYSLLGLVF in isoform 2. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_022570334 – 497Missing in isoform 2. 1 PublicationAdd BLAST164

Sequence databases

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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
AY625001 mRNA Translation: AAT48102.1
AY899886 AY899885 Genomic DNA Translation: AAX86682.1
EF113914 mRNA Translation: ABL14041.1
AY523632 mRNA Translation: AAS48505.1
AY523633 mRNA Translation: AAS48506.1
DQ842020 mRNA Translation: ABG67966.1
DQ842021 mRNA Translation: ABG67967.1

NCBI Reference Sequences

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RefSeqi
NP_001028082.1, NM_001032910.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
574288

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mcc:574288

Keywords - Coding sequence diversityi

Alternative splicing

<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
AY625001 mRNA Translation: AAT48102.1
AY899886 AY899885 Genomic DNA Translation: AAX86682.1
EF113914 mRNA Translation: ABL14041.1
AY523632 mRNA Translation: AAS48505.1
AY523633 mRNA Translation: AAS48506.1
DQ842020 mRNA Translation: ABG67966.1
DQ842021 mRNA Translation: ABG67967.1
RefSeqiNP_001028082.1, NM_001032910.1

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
2LM3NMR-A292-497[»]
3UV9X-ray1.55A292-325[»]
A350-497[»]
4B3NX-ray3.30A/B275-493[»]
4TKPX-ray2.08B2-92[»]
5EIUX-ray1.91A/D89-159[»]
A/D226-265[»]
5F7TX-ray2.29E/F/H/L89-159[»]
E/F/H/L226-265[»]
5IEAX-ray3.26A/B/C/D/F/K89-159[»]
A/B/C/D/F/K226-265[»]
5K3QX-ray1.80A/B/C/D94-154[»]
A/B/C/D229-261[»]
5W9AX-ray2.74A/B95-287[»]
SMRiQ0PF16
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi695095, 11 interactors
IntActiQ0PF16, 1 interactor
STRINGi9544.ENSMMUP00000000454

Genome annotation databases

GeneIDi574288
KEGGimcc:574288

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
85363

Phylogenomic databases

eggNOGiKOG2177, Eukaryota
HOGENOMiCLU_013137_0_3_1
InParanoidiQ0PF16
KOiK10648
OMAiLTNFNYC
OrthoDBi740493at2759
TreeFamiTF338674

Enzyme and pathway databases

UniPathwayiUPA00143

Gene expression databases

BgeeiENSMMUG00000000335, Expressed in spleen and 22 other tissues

Family and domain databases

CDDicd00021, BBOX, 1 hit
Gene3Di2.60.120.920, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
IPR003879, Butyrophylin_SPRY
IPR013320, ConA-like_dom_sf
IPR003877, SPRY_dom
IPR032917, TRIM5
IPR027370, Znf-RING_LisH
IPR000315, Znf_B-box
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PANTHERiPTHR24103:SF416, PTHR24103:SF416, 1 hit
PfamiView protein in Pfam
PF00622, SPRY, 1 hit
PF00643, zf-B_box, 1 hit
PF13445, zf-RING_UBOX, 1 hit
PRINTSiPR01407, BUTYPHLNCDUF
SMARTiView protein in SMART
SM00336, BBOX, 1 hit
SM00184, RING, 1 hit
SM00449, SPRY, 1 hit
SUPFAMiSSF49899, SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50188, B302_SPRY, 1 hit
PS50119, ZF_BBOX, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

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 nameiTRIM5_MACMU
<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: Q0PF16
Secondary accession number(s): Q0PF17
, Q2YEN1, Q6GX25, Q6QWE9, Q6QWF0
<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: January 23, 2007
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 113 of the entry and version 2 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
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