Reviewed, UniProtKB/Swiss-Prot P23284 (PPIB_HUMAN)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase B
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin B
    S-cyclophilin
      Short name=SCYLP
    CYP-S1

Gene names

Name:	PPIB
Synonyms:	CYPB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	216 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. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Cyclosporin A (CsA) inhibits CYPB.
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.12 Ref.13
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Contains 1 PPIase cyclophilin-type domain.
Caution	It is uncertain whether Met-1 or Met-9 is the initiator.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Ref.8 Traceable author statement. Source: ProtInc endoplasmic reticulum lumen Ref.12 Non-traceable author statement. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Ref.8 Non-traceable author statement. Source: UniProtKB unfolded protein binding Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TMBIM4	Q9HC24	1	EBI-359252,EBI-1045545
VHL	P40337	1	EBI-359252,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Ref.8

Chain

34 – 216

183

Peptidyl-prolyl cis-trans isomerase B

PRO_0000025479

Regions

Domain

47 – 204

158

PPIase cyclophilin-type

Motif

213 – 216

4

Prevents secretion from ER

Amino acid modifications

Glycosylation

148

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

60

1

V → L: dbSNP rs11558595.

VAR_047711

Experimental info

Sequence conflict

5

1

S → R in AAA52150. Ref.8

Sequence conflict

216

1

E → D in CAG33110. Ref.3

Secondary structure

1

.

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216

Helix Strand Turn

Details...

Beta strand

41 – 52

12

Beta strand

55 – 64

10

Turn

66 – 68

3

Helix

70 – 81

12

Turn

82 – 84

3

Beta strand

92 – 97

6

Turn

98 – 100

3

Beta strand

101 – 104

4

Turn

107 – 109

3

Beta strand

110 – 113

4

Beta strand

137 – 140

4

Beta strand

152 – 157

6

Helix

160 – 162

3

Turn

163 – 165

3

Beta strand

168 – 174

7

Helix

176 – 183

8

Beta strand

193 – 195

3

Beta strand

197 – 212

16

Sequences

	Sequence		Length	Mass (Da)
	P23284-1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 2D0410A07AA9E420	FASTA	216	23,743
	10 20 30 40 50 60 MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV 70 80 90 100 110 120 IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG 130 140 150 160 170 180 ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR 190 200 210 KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel secreted cyclophilin-like protein (SCYLP)." Spik G., Haendler B., Delmas O., Mariller C., Chamoux M., Maes P., Tartar A., Montreuil J., Stedman K., Kocher H.P., Keller R., Hiestand P.C., Movva N.R. J. Biol. Chem. 266:10735-10738(1991) [PubMed: 2040592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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].
[4]	NIEHS SNPs program Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Prostate and Skin.
[8]	"Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence." Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., Walsh C.T. Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991) [PubMed: 2000394] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, PROTEIN SEQUENCE OF 34-48.
[9]	"An endoplasmic reticulum-specific cyclophilin." Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G. Mol. Cell. Biol. 11:3484-3491(1991) [PubMed: 1710767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-216.
[10]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 52-59; 64-76; 91-101; 138-150; 164-172 AND 197-207, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[11]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 72-84 AND 159-165.
[12]	"S-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin." Arber S., Krause K.-H., Caroni P. J. Cell Biol. 116:113-125(1992) [PubMed: 1530944] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain." Mikol V., Kallen J., Walkinshaw M.D. Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994) [PubMed: 8197205] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M63573 mRNA. Translation: AAA36601.1.
AK291149 mRNA. Translation: BAF83838.1.
CR456829 mRNA. Translation: CAG33110.1.
AY962310 Genomic DNA. Translation: AAX44050.1.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77669.1.
BC001125 mRNA. Translation: AAH01125.1.
BC008848 mRNA. Translation: AAH08848.1.
BC020800 mRNA. Translation: AAH20800.1.
BC032138 mRNA. Translation: AAH32138.1.
M60857 mRNA. Translation: AAA52150.1. Different initiation.
M60457 mRNA. Translation: AAA35733.1.

IPI

IPI00646304.

PIR

CSHUB. A39118.

RefSeq

NP_000933.1.

UniGene

Hs.434937

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CYN	X-ray	1.85	A	39-216	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P23284. 11 interactions.

PTM databases

PhosphoSite

P23284.

2-D gel databases

SWISS-2DPAGE

P23284.

Aarhus/Ghent-2DPAGE

117. NEPHGE.

OGP

P23284.

REPRODUCTION-2DPAGE

IPI00646304.

Proteomic databases

PRIDE

P23284.

Genome annotation databases

Ensembl

ENSG00000166794. Homo sapiens. [Contig view]

GeneID

5479.

KEGG

hsa:5479.

UCSC

uc002and.1. human.

Organism-specific databases

GeneCards

GC15M062235.

H-InvDB

HIX0012337.

HGNC

HGNC:9255. PPIB.

HPA

HPA012720.

MIM

123841. gene.

PharmGKB

PA33580.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P23284.

OMA

P23284. GPSTADE.

Enzyme and pathway databases

BRENDA

5.2.1.8. 247.

Pathway_Interaction_DB

syndecan_1_pathway. Syndecan-1-mediated signaling events.

Gene expression databases

Bgee

P23284.

CleanEx

HS_PPIB.

GermOnline

ENSG00000166794. Homo sapiens.

Family and domain databases

InterPro

IPR002130. PPIase_cyclophilin.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00172. L-Proline.

NextBio

21210.

SOURCE

Search...

Entry information

Entry name

PPIB_HUMAN

Accession

Primary (citable) accession number: P23284
Secondary accession number(s): A8K534, Q6IBH5, Q9BVK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 25, 2008
Last modified:	July 7, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)