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Protein

Coagulation factor XIII B chain

Gene

F13B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143278-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor XIII B chain
Alternative name(s):
Fibrin-stabilizing factor B subunit
Protein-glutamine gamma-glutamyltransferase B chain
Transglutaminase B chain
Gene namesi
Name:F13B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3534. F13B.

Subcellular locationi

  • Secreted 2 Publications

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor XIII subunit B deficiency (FA13BD)4 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.
See also OMIM:613235
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07456325C → R in FA13BD; may disrupt a disulfide bond; impaired subcellular location leading to accumulation in the endoplasmic reticulum; impaired interaction with F13A1; impaired structure. 2 Publications1
Natural variantiVAR_074564101I → N in FA13BD; impaired interaction with F13A1. 2 PublicationsCorresponds to variant rs753009140dbSNPEnsembl.1
Natural variantiVAR_074565136L → F in FA13BD; unknown pathological significance. 2 PublicationsCorresponds to variant rs757094432dbSNPEnsembl.1
Natural variantiVAR_074566237V → I in FA13BD; unknown pathological significance. 2 PublicationsCorresponds to variant rs145637157dbSNPEnsembl.1
Natural variantiVAR_074567336C → F in FA13BD; may disrupt a disulfide bond; impaired interaction with F13A1; impaired structure. 2 PublicationsCorresponds to variant rs778826479dbSNPEnsembl.1
Natural variantiVAR_074568421V → E in FA13BD; impaired interaction with F13A1. 2 Publications1
Natural variantiVAR_074569448P → S in FA13BD; impaired interaction with F13A1; impaired structure. 2 Publications1
Natural variantiVAR_007475450C → F in FA13BD. 1 PublicationCorresponds to variant rs121913075dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2165.
MalaCardsiF13B.
MIMi134580. gene+phenotype.
613235. phenotype.
OpenTargetsiENSG00000143278.
Orphaneti331. Congenital factor XIII deficiency.
PharmGKBiPA27944.

Chemistry databases

ChEMBLiCHEMBL3351193.

Polymorphism and mutation databases

BioMutaiF13B.
DMDMi145559473.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000002122221 – 661Coagulation factor XIII B chainAdd BLAST641

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 76PROSITE-ProRule annotation
Disulfide bondi59 ↔ 87PROSITE-ProRule annotation
Disulfide bondi91 ↔ 135PROSITE-ProRule annotation
Disulfide bondi118 ↔ 146PROSITE-ProRule annotation
Disulfide bondi153 ↔ 197PROSITE-ProRule annotation
Glycosylationi162N-linked (GlcNAc...)1 Publication1
Disulfide bondi180 ↔ 208PROSITE-ProRule annotation
Disulfide bondi213 ↔ 255PROSITE-ProRule annotation
Disulfide bondi241 ↔ 267PROSITE-ProRule annotation
Disulfide bondi274 ↔ 316PROSITE-ProRule annotation
Disulfide bondi302 ↔ 327PROSITE-ProRule annotation
Disulfide bondi336 ↔ 378PROSITE-ProRule annotation
Disulfide bondi364 ↔ 389PROSITE-ProRule annotation
Disulfide bondi396 ↔ 439PROSITE-ProRule annotation
Disulfide bondi425 ↔ 450PROSITE-ProRule annotation
Disulfide bondi454 ↔ 505PROSITE-ProRule annotation
Disulfide bondi486 ↔ 515PROSITE-ProRule annotation
Disulfide bondi524 ↔ 567PROSITE-ProRule annotation
Glycosylationi545N-linked (GlcNAc...)1 Publication1
Disulfide bondi553 ↔ 578PROSITE-ProRule annotation
Disulfide bondi582 ↔ 636PROSITE-ProRule annotation
Disulfide bondi616 ↔ 646PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP05160.
PaxDbiP05160.
PeptideAtlasiP05160.
PRIDEiP05160.

PTM databases

iPTMnetiP05160.
PhosphoSitePlusiP05160.

Expressioni

Gene expression databases

BgeeiENSG00000143278.
CleanExiHS_F13B.
GenevisibleiP05160. HS.

Organism-specific databases

HPAiHPA003827.
HPA052139.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108463. 2 interactors.
STRINGi9606.ENSP00000356382.

Structurei

3D structure databases

ProteinModelPortaliP05160.
SMRiP05160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 88Sushi 1PROSITE-ProRule annotationAdd BLAST65
Domaini89 – 148Sushi 2PROSITE-ProRule annotationAdd BLAST60
Domaini151 – 210Sushi 3PROSITE-ProRule annotationAdd BLAST60
Domaini211 – 269Sushi 4PROSITE-ProRule annotationAdd BLAST59
Domaini272 – 329Sushi 5PROSITE-ProRule annotationAdd BLAST58
Domaini334 – 391Sushi 6PROSITE-ProRule annotationAdd BLAST58
Domaini394 – 452Sushi 7PROSITE-ProRule annotationAdd BLAST59
Domaini453 – 516Sushi 8PROSITE-ProRule annotationAdd BLAST64
Domaini522 – 580Sushi 9PROSITE-ProRule annotationAdd BLAST59
Domaini581 – 647Sushi 10PROSITE-ProRule annotationAdd BLAST67

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi617 – 619Cell attachment site3

Sequence similaritiesi

Contains 10 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiENOG410IE82. Eukaryota.
ENOG410YE48. LUCA.
GeneTreeiENSGT00850000132282.
HOGENOMiHOG000049250.
HOVERGENiHBG005626.
InParanoidiP05160.
KOiK03906.
OMAiPLCTRKE.
OrthoDBiEOG091G03MW.
PhylomeDBiP05160.
TreeFamiTF326157.

Family and domain databases

CDDicd00033. CCP. 7 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00084. Sushi. 8 hits.
[Graphical view]
SMARTiSM00032. CCP. 8 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 10 hits.
PROSITEiPS50923. SUSHI. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLKNLTFII ILIISGELYA EEKPCGFPHV ENGRIAQYYY TFKSFYFPMS
60 70 80 90 100
IDKKLSFFCL AGYTTESGRQ EEQTTCTTEG WSPEPRCFKK CTKPDLSNGY
110 120 130 140 150
ISDVKLLYKI QENMRYGCAS GYKTTGGKDE EVVQCLSDGW SSQPTCRKEH
160 170 180 190 200
ETCLAPELYN GNYSTTQKTF KVKDKVQYEC ATGYYTAGGK KTEEVECLTY
210 220 230 240 250
GWSLTPKCTK LKCSSLRLIE NGYFHPVKQT YEEGDVVQFF CHENYYLSGS
260 270 280 290 300
DLIQCYNFGW YPESPVCEGR RNRCPPPPLP INSKIQTHST TYRHGEIVHI
310 320 330 340 350
ECELNFEIHG SAEIRCEDGK WTEPPKCIEG QEKVACEEPP FIENGAANLH
360 370 380 390 400
SKIYYNGDKV TYACKSGYLL HGSNEITCNR GKWTLPPECV ENNENCKHPP
410 420 430 440 450
VVMNGAVADG ILASYATGSS VEYRCNEYYL LRGSKISRCE QGKWSSPPVC
460 470 480 490 500
LEPCTVNVDY MNRNNIEMKW KYEGKVLHGD LIDFVCKQGY DLSPLTPLSE
510 520 530 540 550
LSVQCNRGEV KYPLCTRKES KGMCTSPPLI KHGVIISSTV DTYENGSSVE
560 570 580 590 600
YRCFDHHFLE GSREAYCLDG MWTTPPLCLE PCTLSFTEME KNNLLLKWDF
610 620 630 640 650
DNRPHILHGE YIEFICRGDT YPAELYITGS ILRMQCDRGQ LKYPRCIPRQ
660
STLSYQEPLR T
Length:661
Mass (Da):75,511
Last modified:April 17, 2007 - v3
Checksum:i57A2FD2A0E35B812
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07456325C → R in FA13BD; may disrupt a disulfide bond; impaired subcellular location leading to accumulation in the endoplasmic reticulum; impaired interaction with F13A1; impaired structure. 2 Publications1
Natural variantiVAR_01393049M → V.1 PublicationCorresponds to variant rs6002dbSNPEnsembl.1
Natural variantiVAR_074564101I → N in FA13BD; impaired interaction with F13A1. 2 PublicationsCorresponds to variant rs753009140dbSNPEnsembl.1
Natural variantiVAR_013931115R → H.4 PublicationsCorresponds to variant rs6003dbSNPEnsembl.1
Natural variantiVAR_074565136L → F in FA13BD; unknown pathological significance. 2 PublicationsCorresponds to variant rs757094432dbSNPEnsembl.1
Natural variantiVAR_074566237V → I in FA13BD; unknown pathological significance. 2 PublicationsCorresponds to variant rs145637157dbSNPEnsembl.1
Natural variantiVAR_074567336C → F in FA13BD; may disrupt a disulfide bond; impaired interaction with F13A1; impaired structure. 2 PublicationsCorresponds to variant rs778826479dbSNPEnsembl.1
Natural variantiVAR_020612342I → T.1 PublicationCorresponds to variant rs17514281dbSNPEnsembl.1
Natural variantiVAR_013932350H → R.2 PublicationsCorresponds to variant rs5999dbSNPEnsembl.1
Natural variantiVAR_013933388E → V.1 PublicationCorresponds to variant rs5991dbSNPEnsembl.1
Natural variantiVAR_074568421V → E in FA13BD; impaired interaction with F13A1. 2 Publications1
Natural variantiVAR_074569448P → S in FA13BD; impaired interaction with F13A1; impaired structure. 2 Publications1
Natural variantiVAR_007475450C → F in FA13BD. 1 PublicationCorresponds to variant rs121913075dbSNPEnsembl.1
Natural variantiVAR_020613529L → P.1 PublicationCorresponds to variant rs17549671dbSNPEnsembl.1
Natural variantiVAR_013934543Y → S.1 PublicationCorresponds to variant rs6001dbSNPEnsembl.1
Natural variantiVAR_013935569D → E.3 PublicationsCorresponds to variant rs6000dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64554 Genomic DNA. Translation: AAA51821.1.
M14057 mRNA. Translation: AAA88042.1.
AK290560 mRNA. Translation: BAF83249.1.
AY692223 Genomic DNA. Translation: AAT85802.1.
AL353809 Genomic DNA. Translation: CAH72549.1.
X51823 mRNA. Translation: CAA36123.1.
CCDSiCCDS1388.1.
PIRiA36397. KFHU13.
RefSeqiNP_001985.2. NM_001994.2.
UniGeneiHs.435782.

Genome annotation databases

EnsembliENST00000367412; ENSP00000356382; ENSG00000143278.
GeneIDi2165.
KEGGihsa:2165.
UCSCiuc001gtt.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Factor XIII entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64554 Genomic DNA. Translation: AAA51821.1.
M14057 mRNA. Translation: AAA88042.1.
AK290560 mRNA. Translation: BAF83249.1.
AY692223 Genomic DNA. Translation: AAT85802.1.
AL353809 Genomic DNA. Translation: CAH72549.1.
X51823 mRNA. Translation: CAA36123.1.
CCDSiCCDS1388.1.
PIRiA36397. KFHU13.
RefSeqiNP_001985.2. NM_001994.2.
UniGeneiHs.435782.

3D structure databases

ProteinModelPortaliP05160.
SMRiP05160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108463. 2 interactors.
STRINGi9606.ENSP00000356382.

Chemistry databases

ChEMBLiCHEMBL3351193.

PTM databases

iPTMnetiP05160.
PhosphoSitePlusiP05160.

Polymorphism and mutation databases

BioMutaiF13B.
DMDMi145559473.

Proteomic databases

EPDiP05160.
PaxDbiP05160.
PeptideAtlasiP05160.
PRIDEiP05160.

Protocols and materials databases

DNASUi2165.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367412; ENSP00000356382; ENSG00000143278.
GeneIDi2165.
KEGGihsa:2165.
UCSCiuc001gtt.1. human.

Organism-specific databases

CTDi2165.
DisGeNETi2165.
GeneCardsiF13B.
H-InvDBHIX0028859.
HGNCiHGNC:3534. F13B.
HPAiHPA003827.
HPA052139.
MalaCardsiF13B.
MIMi134580. gene+phenotype.
613235. phenotype.
neXtProtiNX_P05160.
OpenTargetsiENSG00000143278.
Orphaneti331. Congenital factor XIII deficiency.
PharmGKBiPA27944.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE82. Eukaryota.
ENOG410YE48. LUCA.
GeneTreeiENSGT00850000132282.
HOGENOMiHOG000049250.
HOVERGENiHBG005626.
InParanoidiP05160.
KOiK03906.
OMAiPLCTRKE.
OrthoDBiEOG091G03MW.
PhylomeDBiP05160.
TreeFamiTF326157.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143278-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.

Miscellaneous databases

GeneWikiiF13B.
GenomeRNAii2165.
PROiP05160.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143278.
CleanExiHS_F13B.
GenevisibleiP05160. HS.

Family and domain databases

CDDicd00033. CCP. 7 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00084. Sushi. 8 hits.
[Graphical view]
SMARTiSM00032. CCP. 8 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 10 hits.
PROSITEiPS50923. SUSHI. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiF13B_HUMAN
AccessioniPrimary (citable) accession number: P05160
Secondary accession number(s): A8K3E5, Q5VYL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 17, 2007
Last modified: November 30, 2016
This is version 167 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.