O95302 (FKBP9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP9
Short name=PPIase FKBP9
EC=5.2.1.8

Alternative name(s):
63 kDa FK506-binding protein
Short name=63 kDa FKBP
Short name=FKBP-63
FK506-binding protein 9
Short name=FKBP-9
Rotamase

Gene names

Name:	FKBP9
Synonyms:	FKBP60, FKBP63

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	570 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	PPIases accelerate the folding of proteins during protein synthesis.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by FK506 By similarity.
Subcellular location	Endoplasmic reticulum By similarity.
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Contains 2 EF-hand domains. Contains 4 PPIase FKBP-type domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Isomerase Rotamase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 570	546	Peptidyl-prolyl cis-trans isomerase FKBP9		PRO_0000045760
Regions
	Domain	54 – 142	89	PPIase FKBP-type 1
	Domain	166 – 254	89	PPIase FKBP-type 2
	Domain	278 – 365	88	PPIase FKBP-type 3
	Domain	389 – 477	89	PPIase FKBP-type 4
	Domain	488 – 523	36	EF-hand 1
	Domain	533 – 568	36	EF-hand 2
	Calcium binding	501 – 513	13	1 Potential
	Calcium binding	546 – 557	12	2 Potential
	Motif	567 – 570	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	174	1	N-linked (GlcNAc...) Ref.4
	Glycosylation	286	1	N-linked (GlcNAc...) Ref.4
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O95302 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: E1F44A2FA6E112F8	FASTA	570	63,084
	10 20 30 40 50 60 MAFRGWRPPP PPLLLLLLWV TGQAAPVAGL GSDAELQIER RFVPDECPRT VRSGDFVRYH 70 80 90 100 110 120 YVGTFPDGQK FDSSYDRDST FNVFVGKGQL ITGMDQALVG MCVNERRFVK IPPKLAYGNE 130 140 150 160 170 180 GVSGVIPPNS VLHFDVLLMD IWNSEDQVQI HTYFKPPSCP RTIQVSDFVR YHYNGTFLDG 190 200 210 220 230 240 TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITIPPFLAYG EDGDGKDIPG 250 260 270 280 290 300 QASLVFDVAL LDLHNPKDSI SIENKVVPEN CERISQSGDF LRYHYNGTLL DGTLFDSSYS 310 320 330 340 350 360 RNRTFDTYIG QGYVIPGMDE GLLGVCIGEK RRIVVPPHLG YGEEGRGNIP GSAVLVFDIH 370 380 390 400 410 420 VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL 430 440 450 460 470 480 GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVAGL 490 500 510 520 530 540 PEGYMFIWNG EVSPNLFEEI DKDGNGEVLL EEFSEYIHAQ VASGKGKLAP GFDAELIVKN 550 560 570 MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[2]	"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]. Tissue: Kidney, Liver, Lung and PNS.
[3]	"Biochemical analysis of mouse FKBP60, a novel member of the FKBP family." Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S. Biochim. Biophys. Acta 1446:295-307(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-570.
[4]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-174; ASN-286 AND ASN-397.
[5]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK128597 mRNA. Translation: BAG54697.1. BC007443 mRNA. Translation: AAH07443.2. BC064418 mRNA. Translation: AAH64418.1. BC072422 mRNA. Translation: AAH72422.1. BC101723 mRNA. Translation: AAI01724.1. BC112053 mRNA. Translation: AAI12054.1. AF089745 mRNA. Translation: AAC78853.1.
IPI	IPI00182126.
RefSeq	NP_009201.2. NM_007270.3.
UniGene	Hs.103934.
3D structure databases
ProteinModelPortal	O95302.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95302. 1 interaction.
STRING	9606.ENSP00000242209.
PTM databases
PhosphoSite	O95302.
Proteomic databases
PRIDE	O95302.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242209; ENSP00000242209; ENSG00000122642.
GeneID	11328.
KEGG	hsa:11328.
UCSC	uc003tdh.3. human.
Organism-specific databases
CTD	11328.
GeneCards	GC07P032997.
H-InvDB	HIX0006586. HIX0167892.
HGNC	HGNC:3725. FKBP9.
HPA	HPA012595.
neXtProt	NX_O95302.
PharmGKB	PA28166.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG051620.
InParanoid	O95302.
KO	K09575.
PhylomeDB	O95302.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	O95302.
Bgee	O95302.
CleanEx	HS_FKBP9.
Genevestigator	O95302.
GermOnline	ENSG00000122642. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
PANTHER	PTHR10516. PTHR10516. 1 hit.
Pfam	PF00254. FKBP_C. 4 hits. [Graphical view]
SMART	SM00054. EFh. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. PS00014. ER_TARGET. 1 hit. PS50059. FKBP_PPIASE. 4 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	11328.
NextBio	43031.

Entry information

Entry name

FKBP9_HUMAN

Accession

Primary (citable) accession number: O95302
Secondary accession number(s): B3KY35 , Q2M2A1, Q3MIR7, Q6IN76, Q6P2N1, Q96EX5, Q96IJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	January 10, 2006
Last modified:	May 1, 2013
This is version 118 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.