P00488 (F13A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coagulation factor XIII A chain
Short name=Coagulation factor XIIIa
EC=2.3.2.13

Alternative name(s):
Protein-glutamine gamma-glutamyltransferase A chain
Transglutaminase A chain

Gene names

Name:	F13A1
Synonyms:	F13A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Tetramer of two A chains and two B chains.
Subcellular location	Cytoplasm. Secreted. Note: Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.
Post-translational modification	The activation peptide is released by thrombin.
Polymorphism	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.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.
Sequence caution	The sequence AAA52489.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD92089.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptide cross-linking Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9

Propeptide

2 – 38

37

Activation peptide

PRO_0000033646

Chain

39 – 732

694

Coagulation factor XIII A chain

PRO_0000033647

Sites

Active site

315

1

Active site

374

1

Active site

397

1

Metal binding

437

1

Calcium

Metal binding

439

1

Calcium

Metal binding

486

1

Calcium

Metal binding

491

1

Calcium

Site

38 – 39

2

Cleavage; by thrombin; to produce active factor XIII-A

Amino acid modifications

Modified residue

2

1

N-acetylserine

Glycosylation

614

1

N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant

35

1

V → L Higher specific activity. Ref.5 Ref.17 Ref.18
Corresponds to variant rs5985 [ dbSNP | Ensembl ].

VAR_013927

Natural variant

40

1

V → I. Ref.5

VAR_020910

Natural variant

205

1

Y → F. Ref.5
Corresponds to variant rs3024477 [ dbSNP | Ensembl ].

VAR_020911

Natural variant

351

1

M → K.
Corresponds to variant rs2230848 [ dbSNP | Ensembl ].

VAR_057350

Natural variant

551

1

T → I. Ref.18
Corresponds to variant rs5984 [ dbSNP | Ensembl ].

VAR_013928

Natural variant

565

1

P → L in allele F13A*1A, allele F13A*2A and allele F13*(2)A. Ref.3 Ref.5 Ref.18
Corresponds to variant rs5982 [ dbSNP | Ensembl ].

VAR_007471

Natural variant

589

1

L → Q. Ref.18
Corresponds to variant rs5983 [ dbSNP | Ensembl ].

VAR_013929

Natural variant

650

1

T → I. Ref.7
Corresponds to variant rs17852475 [ dbSNP | Ensembl ].

VAR_060545

Natural variant

651

1

V → I in allele F13A*2A and allele F13A*2B. Ref.1 Ref.5 Ref.18
Corresponds to variant rs5987 [ dbSNP | Ensembl ].

VAR_007472

Natural variant

652

1

Q → E in allele F13A*1A and allele F13A*1B. Ref.4 Ref.5 Ref.6 Ref.7 Ref.18
Corresponds to variant rs5988 [ dbSNP | Ensembl ].

VAR_007473

Natural variant

682

1

R → H in FA13AD. Ref.16

VAR_007474

Experimental info

Sequence conflict

36

1

Missing AA sequence Ref.9

Sequence conflict

89

1

F → L in AAA52488. Ref.1

Secondary structure

1

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732

Helix Strand Turn

Details...

Beta strand

29 – 32

4

Helix

42 – 44

3

Beta strand

48 – 52

5

Helix

60 – 65

6

Beta strand

68 – 71

4

Beta strand

73 – 78

6

Beta strand

81 – 91

11

Turn

95 – 97

3

Beta strand

100 – 105

6

Beta strand

107 – 109

3

Helix

112 – 114

3

Beta strand

116 – 120

5

Beta strand

122 – 125

4

Beta strand

132 – 139

8

Beta strand

142 – 148

7

Beta strand

156 – 166

11

Beta strand

169 – 172

4

Helix

177 – 179

3

Beta strand

181 – 184

4

Helix

199 – 205

7

Beta strand

210 – 217

8

Beta strand

220 – 227

8

Helix

235 – 245

11

Helix

250 – 252

3

Helix

256 – 267

12

Beta strand

270 – 272

3

Beta strand

274 – 278

5

Helix

290 – 292

3

Helix

297 – 306

10

Beta strand

310 – 313

4

Helix

315 – 329

15

Beta strand

333 – 341

9

Beta strand

350 – 355

6

Beta strand

357 – 359

3

Turn

363 – 365

3

Beta strand

371 – 381

11

Beta strand

384 – 386

3

Beta strand

392 – 402

11

Beta strand

404 – 414

11

Helix

415 – 420

6

Beta strand

425 – 428

4

Helix

429 – 437

9

Beta strand

439 – 445

7

Turn

447 – 449

3

Beta strand

451 – 457

7

Beta strand

464 – 468

5

Beta strand

470 – 473

4

Beta strand

475 – 477

3

Helix

479 – 482

4

Helix

489 – 499

11

Turn

500 – 502

3

Beta strand

519 – 525

7

Beta strand

534 – 542

9

Beta strand

544 – 546

3

Beta strand

548 – 559

12

Beta strand

565 – 578

14

Beta strand

582 – 590

9

Helix

592 – 595

4

Turn

596 – 598

3

Beta strand

604 – 613

10

Turn

614 – 616

3

Beta strand

619 – 627

9

Beta strand

634 – 639

6

Beta strand

647 – 654

8

Beta strand

657 – 659

3

Beta strand

661 – 670

10

Turn

671 – 673

3

Beta strand

674 – 684

11

Beta strand

689 – 696

8

Beta strand

702 – 711

10

Beta strand

718 – 727

10

Sequences

	Sequence		Length	Mass (Da)
	P00488 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 51A83A9B8B1370D4	FASTA	732	83,267
	10 20 30 40 50 60 MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS VHLFKERWDT 70 80 90 100 110 120 NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF RVEYVIGRYP QENKGTYIPV 130 140 150 160 170 180 PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD 190 200 210 220 230 240 TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL 250 260 270 280 290 300 YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL 310 320 330 340 350 360 LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN 370 380 390 400 410 420 VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH 430 440 450 460 470 480 GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD 490 500 510 520 530 540 TYKFQEGQEE ERLALETALM YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF 550 560 570 580 590 600 RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL 610 620 630 640 650 660 EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VQFTNPLKET 670 680 690 700 710 720 LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG 730 ELDVQIQRRP SM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Characterization of cDNA coding for human factor XIIIa." Grundmann U., Amann E., Zettlmeissl G., Kuepper H.A. Proc. Natl. Acad. Sci. U.S.A. 83:8024-8028(1986) [PubMed] [Europe PMC] [Abstract] 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.
[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, MASS SPECTROMETRY. 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]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-35; ILE-551; LEU-565; GLN-589; ILE-651 AND GLU-652.
[19]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
+	Additional computationally mapped references.

Web resources

GeneReviews

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Factor XIII entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00297550.

PIR

EKHUX. A35583.

RefSeq

NP_000120.2. NM_000129.3.

UniGene

Hs.335513.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00488.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-377N.

IntAct

P00488. 1 interaction.

STRING

9606.ENSP00000264870.

PTM databases

PhosphoSite

P00488.

Polymorphism databases

DMDM

119720.

2D gel databases

OGP

P00488.

Proteomic databases

PaxDb

P00488.

PRIDE

P00488.

Protocols and materials databases

DNASU

2162.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264870; ENSP00000264870; ENSG00000124491.

GeneID

2162.

KEGG

hsa:2162.

UCSC

uc003mwv.3. human.

Organism-specific databases

CTD

2162.

GeneCards

GC06M006089.

HGNC

HGNC:3531. F13A1.

HPA

CAB002155.
HPA001804.

MIM

134570. gene+phenotype.
613225. phenotype.

neXtProt

NX_P00488.

Orphanet

331. Congenital factor XIII deficiency.

PharmGKB

PA162.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80379.

HOGENOM

HOG000231695.

HOVERGEN

HBG004342.

InParanoid

P00488.

KO

K03917.

OrthoDB

EOG45QHCK.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00488.

Bgee

P00488.

CleanEx

HS_F13A1.

Genevestigator

P00488.

GermOnline

ENSG00000124491. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

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]

PANTHER

PTHR11590. PTHR11590. 1 hit.

Pfam

PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000459. TGM_EBP42. 1 hit.

SMART

SM00460. TGc. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.
SSF49309. Transglut_C. 2 hits.

PROSITE

PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P00488.

ChEMBL

CHEMBL4530.

DrugBank

DB00130. L-Glutamine.

EvolutionaryTrace

P00488.

GenomeRNAi

2162.

NextBio

8735.

PMAP-CutDB

P00488.

SOURCE

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Entry information

Entry name

F13A_HUMAN

Accession

Primary (citable) accession number: P00488
Secondary accession number(s): Q59HA7 , Q8N6X2, Q96P24, Q9BX29

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 169 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.