Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00488

- F13A_HUMAN

UniProt

P00488 - F13A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP00488.
CleanExiHS_F13A1.
ExpressionAtlasiP00488. baseline and differential.
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.
GeneTreeiENSGT00760000119108.
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

        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
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.
GeneTreei ENSGT00760000119108.
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

Bgeei P00488.
CleanExi HS_F13A1.
ExpressionAtlasi P00488. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 185 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