P62942 (FKB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A
Short name=PPIase FKBP1A
EC=5.2.1.8

Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase

Gene names

Name:	FKBP1A
Synonyms:	FKBP1, FKBP12

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	108 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	Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP1A per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Ref.13 Ref.14
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by both FK506 and rapamycin.
Subunit structure	Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7. Ref.13 Ref.14
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP1 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' protein folding Traceable author statement. Source: BHF-UCL SMAD protein complex assembly Inferred from direct assay Ref.14. Source: BHF-UCL T cell activation Non-traceable author statement Ref.2. Source: BHF-UCL beta-amyloid formation Inferred from direct assay. Source: BHF-UCL fibril organization Inferred from direct assay. Source: BHF-UCL heart trabecula formation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of protein phosphatase type 2B activity Inferred from direct assay. Source: BHF-UCL positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: UniProtKB positive regulation of protein binding Inferred from direct assay. Source: BHF-UCL positive regulation of protein ubiquitination Inferred from direct assay Ref.14. Source: BHF-UCL protein maturation by protein folding Traceable author statement. Source: BHF-UCL protein refolding Traceable author statement. Source: BHF-UCL regulation of activin receptor signaling pathway Inferred from direct assay Ref.14. Source: BHF-UCL regulation of immune response Inferred from mutant phenotype Ref.11. Source: BHF-UCL regulation of ryanodine-sensitive calcium-release channel activity Inferred from direct assay. Source: BHF-UCL ventricular cardiac muscle tissue morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	axon Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from direct assay Ref.10. Source: BHF-UCL sarcoplasmic reticulum membrane Inferred from Biological aspect of Ancestor. Source: RefGenome terminal cisterna Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	FK506 binding Inferred from direct assay. Source: BHF-UCL SMAD binding Inferred from physical interaction Ref.14. Source: BHF-UCL activin binding Inferred from physical interaction Ref.14. Source: BHF-UCL peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.2Ref.10Ref.11. Source: BHF-UCL signal transducer activity Inferred from mutant phenotype. Source: UniProtKB type I transforming growth factor beta receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10 Ref.11 Ref.12

Chain

2 – 108

107

Peptidyl-prolyl cis-trans isomerase FKBP1A

PRO_0000075289

Regions

Domain

20 – 108

89

PPIase FKBP-type

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.15

Modified residue

53

1

N6-acetyllysine Ref.16

Experimental info

Sequence conflict

60

1

W → R in CAG28541. Ref.6

Sequence conflict

91

1

I → V in CAG28541. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

108

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Beta strand

22 – 31

10

Beta strand

36 – 39

4

Helix

40 – 43

4

Beta strand

47 – 50

4

Helix

58 – 64

7

Beta strand

72 – 77

6

Helix

79 – 81

3

Turn

82 – 86

5

Turn

89 – 91

3

Sequences

	Sequence		Length	Mass (Da)
	P62942 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9CC8493C802540B4	FASTA	108	11,951
	10 20 30 40 50 60 MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW 70 80 90 100 EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin." Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N., Suzuki M. Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990) [PubMed: 1695378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and overexpression of the human FK506-binding protein FKBP." Standaert R.F., Galat A., Verdine G.L., Schreiber S.L. Nature 346:671-674(1990) [PubMed: 1696686] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains." Dilella A.G., Craig R.J. Biochemistry 30:8512-8517(1991) [PubMed: 1716149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12." Peattie D.A., Hsiao K., Benasutti M., Lippke J.A. Gene 150:251-257(1994) [PubMed: 7529739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Placenta.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Placenta.
[10]	"The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase." Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., Cryan J., Hodges P.J., Sigal N.H. J. Biol. Chem. 265:21011-21015(1990) [PubMed: 1701173] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-52.
[11]	"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase." Harding M.W., Galat A., Uehling D.E., Schreiber S.L. Nature 341:758-760(1989) [PubMed: 2477715] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17.
[12]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Platelet.
[13]	"Mechanism of TGFbeta receptor inhibition by FKBP12." Chen Y.G., Liu F., Massague J. EMBO J. 16:3866-3876(1997) [PubMed: 9233797] [Abstract] Cited for: FUNCTION IN TGFBR1 INHIBITION, INTERACTION WITH TGFBR1.
[14]	"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor." Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H. J. Mol. Endocrinol. 36:569-579(2006) [PubMed: 16720724] [Abstract] Cited for: INTERACTION WITH ACVR1B AND SMAD7, FUNCTION.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, MASS SPECTROMETRY.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein." Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L. Biochemistry 30:4774-4789(1991) [PubMed: 1709363] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin." Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L. Science 252:836-839(1991) [PubMed: 1709301] [Abstract] Cited for: STRUCTURE BY NMR.
[20]	"Solution structure of FK506 bound to FKBP-12." Lepre C.A., Thomson J.A., Moore J.M. FEBS Lett. 302:89-96(1992) [PubMed: 1375171] [Abstract] Cited for: STRUCTURE BY NMR.
[21]	"1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin." Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G., Fesik S.W. Biopolymers 33:535-550(1993) [PubMed: 7682113] [Abstract] Cited for: STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
[22]	"Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex." van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J. Science 252:839-842(1991) [PubMed: 1709302] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[23]	"Atomic structure of the rapamycin human immunophilin FKBP-12 complex." van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J. J. Am. Chem. Soc. 113:7433-7434(1991) Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[24]	"Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin." van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J. J. Mol. Biol. 229:105-124(1993) [PubMed: 7678431] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[25]	"Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12." Huse M., Chen Y.-G., Massague J., Kuriyan J. Cell 96:425-436(1999) [PubMed: 10025408] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH TGFBR1.
[26]	"X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies." Burkhard P., Taylor P., Walkinshaw M.D. J. Mol. Biol. 295:953-962(2000) [PubMed: 10656803] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34539 mRNA. Translation: AAA35844.1.
M92423, M92422 Genomic DNA. Translation: AAA58476.1.
M93060 Genomic DNA. No translation available.
X55741 Genomic DNA. Translation: CAA39272.1.
M80199 Genomic DNA. Translation: AAA58472.1.
X52220 mRNA. Translation: CAA36462.1.
BT007066 mRNA. Translation: AAP35729.1.
CR407613 mRNA. Translation: CAG28541.1.
CR542168 mRNA. Translation: CAG46965.1.
AL136531, AL109658 Genomic DNA. Translation: CAH72382.1.
AL109658, AL136531 Genomic DNA. Translation: CAI22728.1.
CH471133 Genomic DNA. Translation: EAX10633.1.
CH471133 Genomic DNA. Translation: EAX10634.1.
CH471133 Genomic DNA. Translation: EAX10635.1.
BC001925 mRNA. Translation: AAH01925.3.
BC005147 mRNA. Translation: AAH05147.1.

IPI

IPI00413778.

PIR

A35780. I65284.

RefSeq

NP_000792.1. NM_000801.4.
NP_463460.1. NM_054014.3.

UniGene

Hs.471933.
Hs.700839.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A7X	X-ray	2.00	A/B	2-107	[»]
1B6C	X-ray	2.60	A/C/E/G	2-107	[»]
1BKF	X-ray	1.60	A	2-108	[»]
1BL4	X-ray	1.90	A/B	2-107	[»]
1D6O	X-ray	1.85	A/B	2-108	[»]
1D7H	X-ray	1.90	A/B	2-108	[»]
1D7I	X-ray	1.90	A/B	2-108	[»]
1D7J	X-ray	1.85	A/B	2-108	[»]
1EYM	X-ray	2.00	A/B	2-108	[»]
1F40	NMR	-	A	2-108	[»]
1FAP	X-ray	2.70	A	2-107	[»]
1FKB	X-ray	1.70	A	2-108	[»]
1FKD	X-ray	1.72	A	2-107	[»]
1FKF	X-ray	1.70	A	2-108	[»]
1FKG	X-ray	2.00	A	2-108	[»]
1FKH	X-ray	1.95	A	2-108	[»]
1FKI	X-ray	2.20	A/B	2-108	[»]
1FKJ	X-ray	1.70	A	2-107	[»]
1FKR	NMR	-	A	2-108	[»]
1FKS	NMR	-	A	2-108	[»]
1FKT	NMR	-	A	2-108	[»]
1J4H	X-ray	1.80	A	2-107	[»]
1J4I	X-ray	1.80	A	2-107	[»]
1J4R	X-ray	1.80	A/B/D	2-107	[»]
1NSG	X-ray	2.20	A	2-107	[»]
1QPF	X-ray	2.50	A/D	2-107	[»]
1QPL	X-ray	2.90	A/C	2-107	[»]
2DG3	X-ray	1.70	A	2-108	[»]
2DG4	X-ray	1.70	A	2-108	[»]
2DG9	X-ray	1.70	A	2-108	[»]
2FAP	X-ray	2.20	A	2-107	[»]
2FKE	X-ray	1.72	A	2-107	[»]
2PPN	X-ray	0.92	A	2-108	[»]
2PPO	X-ray	1.29	A	2-108	[»]
2PPP	X-ray	0.94	A	2-108	[»]
3FAP	X-ray	1.85	A	2-107	[»]
3H9R	X-ray	2.35	B	1-108	[»]
3MDY	X-ray	2.05	B/D	1-108	[»]
4FAP	X-ray	2.80	A	2-107	[»]

ProteinModelPortal

P62942.

SMR

P62942. Positions 2-108.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29710N.

IntAct

P62942. 2 interactions.

MINT

MINT-87893.

STRING

P62942.

PTM databases

PhosphoSite

P62942.

Polymorphism databases

DMDM

51702264.

Proteomic databases

PRIDE

P62942.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000381719; ENSP00000371138; ENSG00000088832.
ENST00000400137; ENSP00000383003; ENSG00000088832.

GeneID

2280.

KEGG

hsa:2280.

UCSC

uc002wey.1. human.

Organism-specific databases

CTD

2280.

GeneCards

GC20M001349.

H-InvDB

HIX0015564.

HGNC

HGNC:3711. FKBP1A.

HPA

CAB004639.

MIM

186945. gene.

neXtProt

NX_P62942.

PharmGKB

PA28153.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20250.

HOVERGEN

HBG051623.

InParanoid

P62942.

OrthoDB

EOG42NJ1X.

PhylomeDB

P62942.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
mtor_4pathway. mTOR signaling pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
tgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpress

P62942.

Bgee

P62942.

CleanEx

HS_FKBP1A.

Genevestigator

P62942.

GermOnline

ENSG00000088832. Homo sapiens.

Family and domain databases

InterPro

IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]

KO

K09568.

PANTHER

PTHR10516. PPIase_FKBP. 1 hit.

Pfam

PF00254. FKBP_C. 1 hit.
[Graphical view]

PROSITE

PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62942.

DrugBank

DB00337. Pimecrolimus.
DB00877. Sirolimus.
DB00864. Tacrolimus.

NextBio

9269.

PMAP-CutDB

P62942.

SOURCE

Search...

Entry information

Entry name

FKB1A_HUMAN

Accession

Primary (citable) accession number: P62942
Secondary accession number(s): D3DVW6 , P20071, Q4VC47, Q6FGD9, Q6LEU3, Q9H103, Q9H566

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 89 of the entry and version 2 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.