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Entry version 75 (12 Aug 2020)
Sequence version 1 (01 Dec 2001)
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Protein

F-box only protein 5-A

Gene

fbxo5-a

Organism
Xenopus laevis (African clawed frog)
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

Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC) (PubMed:15314241). Binds to the APC activator cdc20 to prevent APC activation (PubMed:11389834). Can also bind directly to the APC to inhibit substrate-binding (PubMed:11751633). Required to arrest unfertilized eggs at metaphase of meiosis II, by preventing their release from metaphase of meiosis II, through inhibition of APC-dependent cyclin B destruction leading to stabilization of cyclin B-cdk1 complex activity (PubMed:11976684).4 Publications

<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 fingeri319 – 367ZBR-typePROSITE-ProRule annotationAdd BLAST49

<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

Biological processCell cycle, Cell division, Mitosis, 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:
F-box only protein 5-ACurated
Alternative name(s):
Early mitotic inhibitor 1-A
<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:fbxo5-a
Synonyms:emi1-a
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-953951, fbxo5.S

<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, Cytoskeleton, 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>Mutagenesisi10S → A: Not mitotically degraded; when associated with A-29; A-105; A-123 and A-328. Does not affect fbxo5 proteolysis. Impairs pin1 interaction. Impairs pin1 interaction; when associated with A-29. Impairs pin1 interaction; when associated with A-29 and A-105. Impairs pin1 interaction; when associated with A-29; A-105 and A-123. Impairs pin1 interaction; when associated with A-29; A-105; A-123 and A-328. Proteolysated in the presence of Pin1. Degraded at G2 phase. 2 Publications1
Mutagenesisi29S → A: Not mitotically degraded; when associated with A-10; A-105; A-123 and A-328. Delays fbxo5 proteolysis. Does not affect pin1 interaction. Impairs pin1 interaction; when associated with A-10. Impairs pin1 interaction; when associated with A-10 and A-105. Impairs pin1 interaction; when associated with A-10; A-105 and A-123. Impairs pin1 interaction; when associated with A-10; A-105; A-123 and A-328. 2 Publications1
Mutagenesisi95S → A: Does not affect protein expression in meiosis II; when associated with A-99. Does not affect protein expression in entered M phase; when associated with A-99. Mostly inhibits the degradation of cyclin B at the meiosis I exit, maintains cdk1 activity at a high level, and arrests meiosis I at metaphase; when associated with A-99. 1 Publication1
Mutagenesisi99S → A: Does not affect protein expression in meiosis II; when associated with A-95. Does not affect protein expression in entered M phase; when associated with A-95. Mostly inhibits the degradation of cyclin B at the meiosis I exit, maintains cdk1 activity at a high level, and arrests meiosis I at metaphase; when associated with A-95. 1 Publication1
Mutagenesisi105S → A: Not mitotically degraded; when associated with A-10; A-29; A-123 and A-328. Does not affect fbxo5 proteolysis. Does not affect pin1 interaction. Impairs pin1 interaction; when associated with A-10 and A-29. Impairs pin1 interaction; when associated with A-10; A-29 and A-123. Impairs pin1 interaction; when associated with A-10; A-29; A-123 and A-328. 2 Publications1
Mutagenesisi123T → A: Not mitotically degraded; when associated with A-10; A-29; A-105 and A-328. Delays fbxo5 proteolysis. Does not affect pin1 interaction. Impairs pin1 interaction; when associated with A-10; A-29 and A-105. Impairs pin1 interaction; when associated with A-10; A-29; A-105 and A-328. 2 Publications1
Mutagenesisi198 – 199EL → AA: Abolishes binding to skp1. 1 Publication2
Mutagenesisi328S → A: Not mitotically degraded; when associated with A-10; A-29; A-105 and A-123. Does not affect fbxo5 proteolysis. Does not affect pin1 interaction. Impairs pin1 interaction; when associated with A-10; A-29; A-105 and A-123. 2 Publications1
Mutagenesisi341C → S: Does not inhibit APC. 1 Publication1
Mutagenesisi346C → S: Does not inhibit APC. 1 Publication1
Mutagenesisi351C → S: Does not inhibit APC. 1 Publication1
Mutagenesisi354C → S: Does not inhibit APC; when associated with S-356. 1 Publication1
Mutagenesisi356C → S: Does not inhibit APC; when associated with S-354. 1 Publication1
Mutagenesisi364C → S: Does not inhibit APC. 1 Publication1

<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_00002580101 – 392F-box only protein 5-AAdd BLAST392

<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

Proteolysed; proteolysis is induced by both cyclin B-cdk1 and cyclin A-cdk1/2 complex through probable phosphorylation. Proteolysis is inhibited by pin1 during G2.1 Publication

<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

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Accumulates before mitosis with levels increasing in S phase and decreasing in M phase (PubMed:11389834). Weakly detected in cycling egg at the stage just before entry into M phase, but not detected in immature (stage VI), metaphase-I and metaphase-II oocytes, and cycling egg that has entered in M phase. Destroyed at every M phase during both meiotic cycles and during cleavage cycles (PubMed:15314241). Decreases at metaphase and completly disappears as cells exited mitosis. First observed at 4 h (S phase) reaching a peak at 7 h (G2 phase), and then a subsequent decrease from 9 to 10 h corresponding to early and late M phases, respectively (PubMed:17159919).3 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is first activated after the gastrula stage of development.1 Publication

<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 a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity).

Interacts with btrc (PubMed:17159919).

Interacts with skp1 (PubMed:11389834).

Interacts with cdc20 (PubMed:11976684, PubMed:11389834).

Interacts with pin1; stabilizes fbxo5 by preventing its association with btrc in an isomerization-dependent pathway; this interaction is present during G2 phase and prevents fbxo5 degradation (PubMed:17159919).

Interacts with plk1 (PubMed:17159919).

By similarity3 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

Hide details

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q90Z80

Protein interaction database and analysis system

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IntActi
Q90Z80, 3 interactors

Molecular INTeraction database

More...
MINTi
Q90Z80

<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

3D structure databases

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

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SMRi
Q90Z80

Database of comparative protein structure models

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ModBasei
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>Domaini197 – 244F-boxSequence analysisAdd BLAST48

<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 C-terminal region is required for APC inhibition.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri319 – 367ZBR-typePROSITE-ProRule annotationAdd BLAST49

Keywords - Domaini

Zinc-finger

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K10292

Identification of Orthologs from Complete Genome Data

More...
OMAi
WRRVICE

Database of Orthologous Groups

More...
OrthoDBi
521317at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036047, F-box-like_dom_sf
IPR001810, F-box_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00646, F-box, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81383, SSF81383, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51872, ZF_ZBR, 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>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.

Q90Z80-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMCGFASNQS PKKLSSKKSS ATNVHLEISP VKHHPPCKVY ENVQGSCLDS
60 70 80 90 100
AICTTVAKCA DLTDDLPVHN KENLLHRLND LETNSYEEYS ALQDSGYSSI
110 120 130 140 150
LQNDSPCQDE TDRKVSDIQV RETPKNFMSY QRPFHTLSKI NLPILRFEEA
160 170 180 190 200
VCSTLKKMRK TNKKIDWNAV DVVCGGNYGL EHLIGKSMGL ERFDILAELF
210 220 230 240 250
HRDFKHLLTK ILRHLSAMDL INVISVSTTW RKLLQKDNWA YNAYKLGCKE
260 270 280 290 300
LCEKRAKVSS HTATRDESLC RVPLASVQKV AASSLCTSKK QSKNKNGGLS
310 320 330 340 350
CNRLAEFIEV AQTLKNDQSL KVCVDCGSPA KHDPCLHRAI CTRESCKLDF
360 370 380 390
CTRCSCKYHF SKSCLMSKPG SYRIPSEPLP GSKKSKQNLR RL
Length:392
Mass (Da):44,142
Last modified:December 1, 2001 - 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:i06E6627033263612
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

More...
DDBJi
Links Updated
AF319594 mRNA Translation: AAK62272.1
BC088910 mRNA Translation: AAH88910.1

NCBI Reference Sequences

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RefSeqi
NP_001082122.1, NM_001088653.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
398237

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:398237

<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
AF319594 mRNA Translation: AAK62272.1
BC088910 mRNA Translation: AAH88910.1
RefSeqiNP_001082122.1, NM_001088653.1

3D structure databases

SMRiQ90Z80
ModBaseiSearch...

Protein-protein interaction databases

ELMiQ90Z80
IntActiQ90Z80, 3 interactors
MINTiQ90Z80

Genome annotation databases

GeneIDi398237
KEGGixla:398237

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
398237
XenbaseiXB-GENE-953951, fbxo5.S

Phylogenomic databases

KOiK10292
OMAiWRRVICE
OrthoDBi521317at2759

Enzyme and pathway databases

UniPathwayiUPA00143

Family and domain databases

InterProiView protein in InterPro
IPR036047, F-box-like_dom_sf
IPR001810, F-box_dom
PfamiView protein in Pfam
PF00646, F-box, 1 hit
SUPFAMiSSF81383, SSF81383, 1 hit
PROSITEiView protein in PROSITE
PS51872, ZF_ZBR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiFBX5A_XENLA
<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: Q90Z80
<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: October 31, 2006
Last sequence update: December 1, 2001
Last modified: August 12, 2020
This is version 75 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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