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Entry version 225 (08 May 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Coagulation factor XIII A chain

Gene

F13A1

Organism
Homo sapiens (Human)
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

Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3151 Publication1
Active sitei3741 Publication1
Active sitei3971 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi437Calcium1 Publication1
Metal bindingi439Calcium1 Publication1
Metal bindingi486Calcium1 Publication1
Metal bindingi491Calcium1 Publication1

<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 functionAcyltransferase, Transferase
Biological processBlood coagulation, Hemostasis
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

<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_and_taxonomy_section">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:
Coagulation factor XIII A chain (EC:2.3.2.131 Publication)
Short name:
Coagulation factor XIIIa
Alternative name(s):
Protein-glutamine gamma-glutamyltransferase A chain
Transglutaminase A chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:F13A1
Synonyms:F13A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3531 F13A1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
134570 gene+phenotype

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00488

<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, Secreted

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Factor XIII subunit A deficiency (FA13AD)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07761938R → Q in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 1 PublicationCorresponds to variant dbSNP:rs759324596Ensembl.1
Natural variantiVAR_074280167P → L in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077620168Y → C in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074281172R → Q in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074282274G → V in FA13AD. 1 Publication1
Natural variantiVAR_077621290P → R in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074283343H → Y in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074284347A → D in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074285376W → R in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074286414S → L in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074287416Q → R in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074288530L → P in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077622541R → Q in FA13AD; decreased intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077623593G → S in FA13AD; no effect on intracellular protein abundance; increased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074289602Q → K in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077624612R → H in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077625669D → G in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_007474682R → H in FA13AD. 1 Publication1
Natural variantiVAR_074290704R → Q in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074291716R → G in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2162

MalaCards human disease database

More...
MalaCardsi
F13A1
MIMi134570 gene+phenotype
613225 phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
331 Congenital factor XIII deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4530

Drug and drug target database

More...
DrugBanki
DB00130 L-Glutamine
DB02340 N-Acetyl-Serine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
F13A1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
119720

<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_processing_section">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 methionineiRemoved2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000336462 – 38Activation peptideAdd BLAST37
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003364739 – 732Coagulation factor XIII A chainAdd BLAST694

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-acetylserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi614N-linked (GlcNAc...) asparagine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

The activation peptide is released by thrombin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei38 – 39Cleavage; by thrombin; to produce active factor XIII-A2

Keywords - PTMi

Acetylation, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P00488

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00488

MaxQB - The MaxQuant DataBase

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MaxQBi
P00488

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

More...
PaxDbi
P00488

PeptideAtlas

More...
PeptideAtlasi
P00488

PRoteomics IDEntifications database

More...
PRIDEi
P00488

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51255

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P00488

2D gel databases

USC-OGP 2-DE database

More...
OGPi
P00488

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00488

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P00488

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P00488

<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
ENSG00000124491 Expressed in 215 organ(s), highest expression level in esophagus

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P00488 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P00488 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB002155
HPA001804

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Tetramer of two A chains (F13A1) and two B (F13B) chains.2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108460, 11 interactors

Database of interacting proteins

More...
DIPi
DIP-377N

Protein interaction database and analysis system

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IntActi
P00488, 10 interactors

Molecular INTeraction database

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MINTi
P00488

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000264870

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00488

<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

1732
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

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SMRi
P00488

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00488

<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

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFMV Eukaryota
ENOG410XQEZ LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231695

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00488

KEGG Orthology (KO)

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KOi
K03917

Database of Orthologous Groups

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OrthoDBi
297055at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P00488

TreeFam database of animal gene trees

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TreeFami
TF324278

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 3 hits
3.90.260.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034810 Factor_XIII_A
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR038765 Papain-like_cys_pep_sf
IPR002931 Transglutaminase-like
IPR036985 Transglutaminase-like_sf
IPR023608 Transglutaminase_animal
IPR013808 Transglutaminase_AS
IPR008958 Transglutaminase_C
IPR036238 Transglutaminase_C_sf
IPR001102 Transglutaminase_N

The PANTHER Classification System

More...
PANTHERi
PTHR11590:SF42 PTHR11590:SF42, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00927 Transglut_C, 2 hits
PF01841 Transglut_core, 1 hit
PF00868 Transglut_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000459 TGM_EBP42, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00460 TGc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49309 SSF49309, 2 hits
SSF54001 SSF54001, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00547 TRANSGLUTAMINASES, 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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P00488-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS
60 70 80 90 100
VHLFKERWDT NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF
110 120 130 140 150
RVEYVIGRYP QENKGTYIPV PIVSELQSGK WGAKIVMRED RSVRLSIQSS
160 170 180 190 200
PKCIVGKFRM YVAVWTPYGV LRTSRNPETD TYILFNPWCE DDAVYLDNEK
210 220 230 240 250
EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL YVMDRAQMDL
260 270 280 290 300
SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL
310 320 330 340 350
LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ
360 370 380 390 400
MDIFLEEDGN VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP
410 420 430 440 450
QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDL IYITAKKDGT
460 470 480 490 500
HVVENVDATH IGKLIVTKQI GGDGMMDITD TYKFQEGQEE ERLALETALM
510 520 530 540 550
YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF RNNSHNRYTI
560 570 580 590 600
TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL
610 620 630 640 650
EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT
660 670 680 690 700
VQFTNPLKET LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV
710 720 730
SGHRKLIASM SSDSLRHVYG ELDVQIQRRP SM
Length:732
Mass (Da):83,267
Last modified:January 23, 2007 - v4
<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:i51A83A9B8B1370D4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9NQP5Q9NQP5_HUMAN
Coagulation factor XIII A chain
F13A1
138Annotation score:

Annotation score:1 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>
A6PVK5A6PVK5_HUMAN
Coagulation factor XIII A chain
F13A1
185Annotation score:

Annotation score:1 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>
H0Y796H0Y796_HUMAN
Coagulation factor XIII A chain
F13A1
147Annotation score:

Annotation score:1 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>
H0Y4W5H0Y4W5_HUMAN
Coagulation factor XIII A chain
F13A1
102Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA52489 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD92089 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti36Missing AA sequence (PubMed:4811064).Curated1
Sequence conflicti89F → L in AAA52488 (PubMed:3026437).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

There are four main allelic forms of this protein; F13A*1A, F13A*1B, F13A*2A and F13A*2B. In addition two other intermediate forms (F13A*2A and F13A*2B) seem to exist. The sequence shown is that of F13A*2B.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01392735V → L Higher specific activity. 3 PublicationsCorresponds to variant dbSNP:rs5985EnsemblClinVar.1
Natural variantiVAR_07761938R → Q in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 1 PublicationCorresponds to variant dbSNP:rs759324596Ensembl.1
Natural variantiVAR_02091040V → I1 Publication1
Natural variantiVAR_074280167P → L in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077620168Y → C in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074281172R → Q in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_020911205Y → F1 PublicationCorresponds to variant dbSNP:rs3024477Ensembl.1
Natural variantiVAR_074282274G → V in FA13AD. 1 Publication1
Natural variantiVAR_077621290P → R in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074283343H → Y in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074284347A → D in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074285376W → R in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074286414S → L in FA13AD; unknown pathological significance. 1 Publication1
Natural variantiVAR_074287416Q → R in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074288530L → P in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077622541R → Q in FA13AD; decreased intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_013928551T → I1 PublicationCorresponds to variant dbSNP:rs5984Ensembl.1
Natural variantiVAR_007471565P → L in allele F13A*1A, allele F13A*2A and allele F13*(2)A. 3 PublicationsCorresponds to variant dbSNP:rs5982EnsemblClinVar.1
Natural variantiVAR_013929589L → Q1 PublicationCorresponds to variant dbSNP:rs5983Ensembl.1
Natural variantiVAR_077623593G → S in FA13AD; no effect on intracellular protein abundance; increased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074289602Q → K in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_077624612R → H in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_060545650T → I1 PublicationCorresponds to variant dbSNP:rs17852475Ensembl.1
Natural variantiVAR_007472651V → I in allele F13A*2A and allele F13A*2B. 3 PublicationsCorresponds to variant dbSNP:rs5987EnsemblClinVar.1
Natural variantiVAR_007473652Q → E in allele F13A*1A and allele F13A*1B. 5 PublicationsCorresponds to variant dbSNP:rs5988Ensembl.1
Natural variantiVAR_077625669D → G in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_007474682R → H in FA13AD. 1 Publication1
Natural variantiVAR_074290704R → Q in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1
Natural variantiVAR_074291716R → G in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness. 2 Publications1

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
M14539 mRNA Translation: AAA52489.1 Different initiation.
M14354 mRNA Translation: AAA52488.1
M22001
, M21987, M21988, M21989, M21990, M21991, M21992, M21993, M21995, M21996, M21997, M21998, M21999, M22000 Genomic DNA Translation: AAA52415.1
AB208852 mRNA Translation: BAD92089.1 Different initiation.
AF418272 Genomic DNA Translation: AAL12161.1
AL157775 Genomic DNA No translation available.
AL391420 Genomic DNA No translation available.
AL133326 Genomic DNA No translation available.
BC027963 mRNA Translation: AAH27963.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4496.1

Protein sequence database of the Protein Information Resource

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PIRi
A35583 EKHUX

NCBI Reference Sequences

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RefSeqi
NP_000120.2, NM_000129.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000264870; ENSP00000264870; ENSG00000124491

Database of genes from NCBI RefSeq genomes

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GeneIDi
2162

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2162

UCSC genome browser

More...
UCSCi
uc003mwv.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Factor XIII entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14539 mRNA Translation: AAA52489.1 Different initiation.
M14354 mRNA Translation: AAA52488.1
M22001
, M21987, M21988, M21989, M21990, M21991, M21992, M21993, M21995, M21996, M21997, M21998, M21999, M22000 Genomic DNA Translation: AAA52415.1
AB208852 mRNA Translation: BAD92089.1 Different initiation.
AF418272 Genomic DNA Translation: AAL12161.1
AL157775 Genomic DNA No translation available.
AL391420 Genomic DNA No translation available.
AL133326 Genomic DNA No translation available.
BC027963 mRNA Translation: AAH27963.1
CCDSiCCDS4496.1
PIRiA35583 EKHUX
RefSeqiNP_000120.2, NM_000129.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1EVUX-ray2.01A/B2-732[»]
1EX0X-ray2.00A/B2-732[»]
1F13X-ray2.10A/B2-732[»]
1FIEX-ray2.50A/B2-732[»]
1GGTX-ray2.65A/B2-732[»]
1GGUX-ray2.10A/B2-732[»]
1GGYX-ray2.50A/B2-732[»]
1QRKX-ray2.50A/B2-732[»]
4KTYX-ray1.98A/B2-732[»]
5MHLX-ray2.40A/B2-732[»]
5MHMX-ray2.12A/B2-732[»]
5MHNX-ray2.48A/B2-732[»]
5MHOX-ray2.92A/B2-732[»]
SMRiP00488
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108460, 11 interactors
DIPiDIP-377N
IntActiP00488, 10 interactors
MINTiP00488
STRINGi9606.ENSP00000264870

Chemistry databases

BindingDBiP00488
ChEMBLiCHEMBL4530
DrugBankiDB00130 L-Glutamine
DB02340 N-Acetyl-Serine

PTM databases

iPTMnetiP00488
PhosphoSitePlusiP00488

Polymorphism and mutation databases

BioMutaiF13A1
DMDMi119720

2D gel databases

OGPiP00488

Proteomic databases

EPDiP00488
jPOSTiP00488
MaxQBiP00488
PaxDbiP00488
PeptideAtlasiP00488
PRIDEiP00488
ProteomicsDBi51255
TopDownProteomicsiP00488

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2162
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264870; ENSP00000264870; ENSG00000124491
GeneIDi2162
KEGGihsa:2162
UCSCiuc003mwv.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2162
DisGeNETi2162

GeneCards: human genes, protein and diseases

More...
GeneCardsi
F13A1
HGNCiHGNC:3531 F13A1
HPAiCAB002155
HPA001804
MalaCardsiF13A1
MIMi134570 gene+phenotype
613225 phenotype
neXtProtiNX_P00488
Orphaneti331 Congenital factor XIII deficiency
PharmGKBiPA162

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IFMV Eukaryota
ENOG410XQEZ LUCA
HOGENOMiHOG000231695
InParanoidiP00488
KOiK03917
OrthoDBi297055at2759
PhylomeDBiP00488
TreeFamiTF324278

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
F13A1 human
EvolutionaryTraceiP00488

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Coagulation_factor_XIII,_A1_polypeptide

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2162
PMAP-CutDBiP00488

Protein Ontology

More...
PROi
PR:P00488

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000124491 Expressed in 215 organ(s), highest expression level in esophagus
ExpressionAtlasiP00488 baseline and differential
GenevisibleiP00488 HS

Family and domain databases

Gene3Di2.60.40.10, 3 hits
3.90.260.10, 1 hit
InterProiView protein in InterPro
IPR034810 Factor_XIII_A
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR038765 Papain-like_cys_pep_sf
IPR002931 Transglutaminase-like
IPR036985 Transglutaminase-like_sf
IPR023608 Transglutaminase_animal
IPR013808 Transglutaminase_AS
IPR008958 Transglutaminase_C
IPR036238 Transglutaminase_C_sf
IPR001102 Transglutaminase_N
PANTHERiPTHR11590:SF42 PTHR11590:SF42, 1 hit
PfamiView protein in Pfam
PF00927 Transglut_C, 2 hits
PF01841 Transglut_core, 1 hit
PF00868 Transglut_N, 1 hit
PIRSFiPIRSF000459 TGM_EBP42, 1 hit
SMARTiView protein in SMART
SM00460 TGc, 1 hit
SUPFAMiSSF49309 SSF49309, 2 hits
SSF54001 SSF54001, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS00547 TRANSGLUTAMINASES, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiF13A_HUMAN
<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: P00488
Secondary accession number(s): Q59HA7
, Q8N6X2, Q96P24, Q9BX29
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 225 of the entry and version 4 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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