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P00488

- F13A_HUMAN

UniProt

P00488 - F13A_HUMAN

Protein

Coagulation factor XIII A chain

Gene

F13A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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.

    Catalytic activityi

    Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei38 – 392Cleavage; by thrombin; to produce active factor XIII-A
    Active sitei315 – 3151
    Active sitei374 – 3741
    Active sitei397 – 3971
    Metal bindingi437 – 4371Calcium
    Metal bindingi439 – 4391Calcium
    Metal bindingi486 – 4861Calcium
    Metal bindingi491 – 4911Calcium

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein-glutamine gamma-glutamyltransferase activity Source: Reactome

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. peptide cross-linking Source: Ensembl
    3. platelet activation Source: Reactome
    4. platelet degranulation Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_1439. Common Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coagulation factor XIII A chain (EC:2.3.2.13)
    Short name:
    Coagulation factor XIIIa
    Alternative name(s):
    Protein-glutamine gamma-glutamyltransferase A chain
    Transglutaminase A chain
    Gene namesi
    Name:F13A1
    Synonyms:F13A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3531. F13A1.

    Subcellular locationi

    Cytoplasm. Secreted
    Note: Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Factor XIII subunit A deficiency (FA13AD) [MIM:613225]: An autosomal recessive hematologic disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti682 – 6821R → H in FA13AD. 1 Publication
    VAR_007474

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi134570. gene+phenotype.
    613225. phenotype.
    Orphaneti331. Congenital factor XIII deficiency.
    PharmGKBiPA162.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Propeptidei2 – 3837Activation peptidePRO_0000033646Add
    BLAST
    Chaini39 – 732694Coagulation factor XIII A chainPRO_0000033647Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Glycosylationi614 – 6141N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    The activation peptide is released by thrombin.

    Keywords - PTMi

    Acetylation, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP00488.
    PaxDbiP00488.
    PRIDEiP00488.

    2D gel databases

    OGPiP00488.

    PTM databases

    PhosphoSiteiP00488.

    Miscellaneous databases

    PMAP-CutDBP00488.

    Expressioni

    Gene expression databases

    ArrayExpressiP00488.
    BgeeiP00488.
    CleanExiHS_F13A1.
    GenevestigatoriP00488.

    Organism-specific databases

    HPAiCAB002155.
    HPA001804.

    Interactioni

    Subunit structurei

    Tetramer of two A chains and two B chains.

    Protein-protein interaction databases

    BioGridi108460. 11 interactions.
    DIPiDIP-377N.
    IntActiP00488. 9 interactions.
    MINTiMINT-7966415.
    STRINGi9606.ENSP00000264870.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 324
    Helixi42 – 443
    Beta strandi48 – 525
    Helixi60 – 645
    Beta strandi68 – 714
    Beta strandi74 – 785
    Beta strandi81 – 9111
    Turni95 – 973
    Beta strandi100 – 1056
    Beta strandi107 – 1093
    Helixi112 – 1143
    Beta strandi116 – 12510
    Beta strandi132 – 1398
    Beta strandi142 – 1487
    Beta strandi156 – 16611
    Beta strandi169 – 1724
    Helixi177 – 1793
    Beta strandi181 – 1844
    Helixi199 – 2057
    Beta strandi210 – 2178
    Beta strandi220 – 2278
    Helixi235 – 24511
    Helixi250 – 2523
    Helixi256 – 26611
    Turni270 – 2723
    Beta strandi275 – 2784
    Helixi290 – 2923
    Helixi297 – 30610
    Beta strandi310 – 3134
    Helixi315 – 32915
    Beta strandi333 – 34311
    Beta strandi345 – 35511
    Beta strandi359 – 3613
    Turni363 – 3653
    Beta strandi369 – 38113
    Beta strandi384 – 3863
    Beta strandi392 – 3965
    Beta strandi402 – 4043
    Beta strandi406 – 4149
    Helixi415 – 4195
    Beta strandi425 – 4284
    Helixi429 – 4379
    Beta strandi439 – 4457
    Turni447 – 4493
    Beta strandi451 – 46111
    Beta strandi464 – 4685
    Beta strandi470 – 4734
    Beta strandi475 – 4773
    Helixi479 – 4824
    Helixi489 – 50113
    Beta strandi519 – 5279
    Beta strandi534 – 5429
    Beta strandi544 – 5463
    Beta strandi548 – 55912
    Beta strandi565 – 57814
    Beta strandi580 – 59011
    Helixi592 – 5954
    Helixi596 – 5983
    Beta strandi604 – 61310
    Turni614 – 6174
    Beta strandi618 – 6269
    Beta strandi633 – 6397
    Beta strandi647 – 6548
    Beta strandi657 – 6593
    Beta strandi661 – 67010
    Turni671 – 6733
    Beta strandi674 – 68411
    Beta strandi689 – 6968
    Beta strandi702 – 71110
    Beta strandi713 – 72614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00488.
    SMRiP00488. Positions 6-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00488.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG80379.
    HOGENOMiHOG000231695.
    HOVERGENiHBG004342.
    InParanoidiP00488.
    KOiK03917.
    OrthoDBiEOG7WT40M.
    PhylomeDBiP00488.
    TreeFamiTF324278.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00488-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS    50
    VHLFKERWDT NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF 100
    RVEYVIGRYP QENKGTYIPV PIVSELQSGK WGAKIVMRED RSVRLSIQSS 150
    PKCIVGKFRM YVAVWTPYGV LRTSRNPETD TYILFNPWCE DDAVYLDNEK 200
    EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL YVMDRAQMDL 250
    SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL 300
    LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ 350
    MDIFLEEDGN VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP 400
    QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDL IYITAKKDGT 450
    HVVENVDATH IGKLIVTKQI GGDGMMDITD TYKFQEGQEE ERLALETALM 500
    YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF RNNSHNRYTI 550
    TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL 600
    EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT 650
    VQFTNPLKET LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV 700
    SGHRKLIASM SSDSLRHVYG ELDVQIQRRP SM 732
    Length:732
    Mass (Da):83,267
    Last modified:January 23, 2007 - v4
    Checksum:i51A83A9B8B1370D4
    GO

    Sequence cautioni

    The sequence AAA52489.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD92089.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361Missing AA sequence (PubMed:4811064)Curated
    Sequence conflicti89 – 891F → L in AAA52488. (PubMed:3026437)Curated

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351V → L Higher specific activity. 2 Publications
    Corresponds to variant rs5985 [ dbSNP | Ensembl ].
    VAR_013927
    Natural varianti40 – 401V → I.1 Publication
    VAR_020910
    Natural varianti205 – 2051Y → F.1 Publication
    Corresponds to variant rs3024477 [ dbSNP | Ensembl ].
    VAR_020911
    Natural varianti351 – 3511M → K.
    Corresponds to variant rs2230848 [ dbSNP | Ensembl ].
    VAR_057350
    Natural varianti551 – 5511T → I.1 Publication
    Corresponds to variant rs5984 [ dbSNP | Ensembl ].
    VAR_013928
    Natural varianti565 – 5651P → L in allele F13A*1A, allele F13A*2A and allele F13*(2)A. 3 Publications
    Corresponds to variant rs5982 [ dbSNP | Ensembl ].
    VAR_007471
    Natural varianti589 – 5891L → Q.1 Publication
    Corresponds to variant rs5983 [ dbSNP | Ensembl ].
    VAR_013929
    Natural varianti650 – 6501T → I.1 Publication
    Corresponds to variant rs17852475 [ dbSNP | Ensembl ].
    VAR_060545
    Natural varianti651 – 6511V → I in allele F13A*2A and allele F13A*2B. 3 Publications
    Corresponds to variant rs5987 [ dbSNP | Ensembl ].
    VAR_007472
    Natural varianti652 – 6521Q → E in allele F13A*1A and allele F13A*1B. 5 Publications
    Corresponds to variant rs5988 [ dbSNP | Ensembl ].
    VAR_007473
    Natural varianti682 – 6821R → H in FA13AD. 1 Publication
    VAR_007474

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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, AL133326, AL391420 Genomic DNA. Translation: CAC36886.3.
    AL391420, AL133326, AL157775 Genomic DNA. Translation: CAI39797.2.
    AL133326, AL157775, AL391420 Genomic DNA. Translation: CAO03607.1.
    BC027963 mRNA. Translation: AAH27963.1.
    CCDSiCCDS4496.1.
    PIRiA35583. EKHUX.
    RefSeqiNP_000120.2. NM_000129.3.
    XP_006715073.1. XM_006715010.1.
    UniGeneiHs.335513.

    Genome annotation databases

    EnsembliENST00000264870; ENSP00000264870; ENSG00000124491.
    GeneIDi2162.
    KEGGihsa:2162.
    UCSCiuc003mwv.3. human.

    Polymorphism databases

    DMDMi119720.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Factor XIII entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 , AL133326 , AL391420 Genomic DNA. Translation: CAC36886.3 .
    AL391420 , AL133326 , AL157775 Genomic DNA. Translation: CAI39797.2 .
    AL133326 , AL157775 , AL391420 Genomic DNA. Translation: CAO03607.1 .
    BC027963 mRNA. Translation: AAH27963.1 .
    CCDSi CCDS4496.1.
    PIRi A35583. EKHUX.
    RefSeqi NP_000120.2. NM_000129.3.
    XP_006715073.1. XM_006715010.1.
    UniGenei Hs.335513.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EVU X-ray 2.01 A/B 2-732 [» ]
    1EX0 X-ray 2.00 A/B 2-732 [» ]
    1F13 X-ray 2.10 A/B 2-732 [» ]
    1FIE X-ray 2.50 A/B 2-732 [» ]
    1GGT X-ray 2.65 A/B 2-732 [» ]
    1GGU X-ray 2.10 A/B 2-732 [» ]
    1GGY X-ray 2.50 A/B 2-732 [» ]
    1QRK X-ray 2.50 A/B 2-732 [» ]
    4KTY X-ray 1.98 A/B 2-732 [» ]
    ProteinModelPortali P00488.
    SMRi P00488. Positions 6-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108460. 11 interactions.
    DIPi DIP-377N.
    IntActi P00488. 9 interactions.
    MINTi MINT-7966415.
    STRINGi 9606.ENSP00000264870.

    Chemistry

    BindingDBi P00488.
    ChEMBLi CHEMBL4530.
    DrugBanki DB00130. L-Glutamine.

    PTM databases

    PhosphoSitei P00488.

    Polymorphism databases

    DMDMi 119720.

    2D gel databases

    OGPi P00488.

    Proteomic databases

    MaxQBi P00488.
    PaxDbi P00488.
    PRIDEi P00488.

    Protocols and materials databases

    DNASUi 2162.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264870 ; ENSP00000264870 ; ENSG00000124491 .
    GeneIDi 2162.
    KEGGi hsa:2162.
    UCSCi uc003mwv.3. human.

    Organism-specific databases

    CTDi 2162.
    GeneCardsi GC06M006089.
    HGNCi HGNC:3531. F13A1.
    HPAi CAB002155.
    HPA001804.
    MIMi 134570. gene+phenotype.
    613225. phenotype.
    neXtProti NX_P00488.
    Orphaneti 331. Congenital factor XIII deficiency.
    PharmGKBi PA162.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80379.
    HOGENOMi HOG000231695.
    HOVERGENi HBG004342.
    InParanoidi P00488.
    KOi K03917.
    OrthoDBi EOG7WT40M.
    PhylomeDBi P00488.
    TreeFami TF324278.

    Enzyme and pathway databases

    Reactomei REACT_1439. Common Pathway.

    Miscellaneous databases

    EvolutionaryTracei P00488.
    GeneWikii Coagulation_factor_XIII,_A1_polypeptide.
    GenomeRNAii 2162.
    NextBioi 8735.
    PMAP-CutDB P00488.
    PROi P00488.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00488.
    Bgeei P00488.
    CleanExi HS_F13A1.
    Genevestigatori P00488.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence of the a subunit of human factor XIII."
      Ichinose A., Hendrickson L.E., Fujikawa K., Davie E.W.
      Biochemistry 25:6900-6906(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-651.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor."
      Ichinose A., Davie E.W.
      Proc. Natl. Acad. Sci. U.S.A. 85:5829-5833(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-565.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-652.
      Tissue: Brain.
    5. SeattleSNPs variation discovery resource
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-35; ILE-40; PHE-205; LEU-565; ILE-651 AND GLU-652.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-652.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-650 AND GLU-652.
      Tissue: Pancreas.
    8. "Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta."
      Takahashi N., Takahashi Y., Putnam F.W.
      Proc. Natl. Acad. Sci. U.S.A. 83:8019-8023(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-731, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    9. "Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin."
      Takagi T., Doolittle R.F.
      Biochemistry 13:750-756(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-44.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614.
      Tissue: Plasma.
    11. "Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII."
      Yee V.C., Pedersen L.C., Trong I.L., Bishop P.D., Stenkamp R.E., Teller D.C.
      Proc. Natl. Acad. Sci. U.S.A. 91:7296-7300(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    12. "Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII."
      Yee V.C., Pedersen L.C., Bishop P.D., Stenkamp R.E., Teller D.C.
      Thromb. Res. 78:389-397(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    13. "Two non-proline cis peptide bonds may be important for factor XIII function."
      Weiss M.S., Metzner H.J., Hilgenfeld R.
      FEBS Lett. 423:291-296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    14. "Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography."
      Fox B.A., Yee V.C., Pedersen L.C., le Trong I., Bishop P.D., Stenkamp R.E., Teller D.C.
      J. Biol. Chem. 274:4917-4923(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    15. "Molecular basis for subtypic differences of the 'a' subunit of coagulation factor XIII with description of the genesis of the subtypes."
      Suzuki K., Iwata M., Ito S., Matsui K., Uchida A., Mizoi Y.
      Hum. Genet. 94:129-135(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM.
    16. "Identification of a point mutation in factor XIII A subunit deficiency."
      Board P., Coggan M., Miloszewski K.
      Blood 80:937-941(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA13AD HIS-682.
    17. "The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity."
      Kangsadalampai S., Board P.G.
      Blood 92:2766-2770(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT LEU-35.
    18. Cited for: VARIANTS LEU-35; ILE-551; LEU-565; GLN-589; ILE-651 AND GLU-652.

    Entry informationi

    Entry nameiF13A_HUMAN
    AccessioniPrimary (citable) accession number: P00488
    Secondary accession number(s): Q59HA7
    , Q8N6X2, Q96P24, Q9BX29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 184 of the entry and version 4 of the sequence. [Complete history]
    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.

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

    External Data

    Dasty 3