Q13356 (PPIL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase-like 2
Short name=PPIase
EC=5.2.1.8

Alternative name(s):
Cyclophilin-60
Cyclophilin-like protein Cyp-60
Rotamase PPIL2

Gene names

Name:

PPIL2

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	520 AA.
Sequence status	Complete.
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).
Subcellular location	Nucleus.
Tissue specificity	Highest expression in thymus, pancreas and testis. Also detected in heart, placenta, lung, liver, skeletal muscle, kidney, spleen, prostate, ovary, small intestine and colon. Poorly detected in brain and leukocytes. Strong protein expression in lymph node (cortical, paracortical and medullar regions), thyroid (follicular epithelial cells), testis (developing spermatozoa), stomach (cells lining the gastric pit), pancreas, kidney (proximal and distal-tubule cells and collecting duct cells but not in glomeruli), endometrium and colon (goblet cells). Moderate protein expression in spleen, prostate (epithelium and squamous cell carcinomas), placenta and adrenal gland. Weak protein expression in liver, heart, breast, ovary, and lung. No protein expression in brain and bladder. High protein expression in most lymphomas and melanomas.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 1 U-box domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Isomerase Rotamase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome leukocyte migration Traceable author statement. Source: Reactome protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC protein polyubiquitination Inferred from direct assay PubMed 11435423. Source: MGI
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome nucleus Traceable author statement Ref.1. Source: UniProtKB ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-ubiquitin ligase activity Inferred from direct assay PubMed 11435423. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13356-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13356-2)

The sequence of this isoform differs from the canonical sequence as follows:
     490-520: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

Peptidyl-prolyl cis-trans isomerase-like 2

PRO_0000064171

Regions

Domain

42 – 101

60

U-box

Domain

278 – 433

156

PPIase cyclophilin-type

Coiled coil

197 – 217

21

Potential

Amino acid modifications

Modified residue

482

1

N6-acetyllysine Ref.4

Natural variations

Alternative sequence

490 – 520

31

KRAAE…DFSSW → EQQRKSPQPVPLSPCPRRSP VGVLGTSAPGSSRLPDDH in isoform 2.

VSP_005182

Experimental info

Sequence conflict

455

1

V → I in AAH28385. Ref.3

Secondary structure

1

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520

Helix Strand Turn

Details...

Beta strand

280 – 286

7

Beta strand

289 – 295

7

Turn

297 – 299

3

Helix

301 – 312

12

Turn

313 – 318

6

Beta strand

323 – 325

3

Turn

326 – 328

3

Beta strand

329 – 332

4

Beta strand

337 – 340

4

Beta strand

365 – 368

4

Beta strand

380 – 385

6

Helix

388 – 390

3

Turn

391 – 393

3

Beta strand

396 – 402

7

Helix

404 – 412

9

Turn

417 – 419

3

Beta strand

422 – 424

3

Beta strand

427 – 435

9

Helix

439 – 455

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3FFA51C3D82F0957	FASTA	520	58,823
	10 20 30 40 50 60 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 70 80 90 100 110 120 FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 130 140 150 160 170 180 TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 190 200 210 220 230 240 IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 250 260 270 280 290 300 YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 310 320 330 340 350 360 PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 370 380 390 400 410 420 TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 430 440 450 460 470 480 RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 490 500 510 520 GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW
	Isoform 2 [UniParc]. Checksum: 9B494AE6D29EBAC3	FASTA	527	59,458
	10 20 30 40 50 60 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 70 80 90 100 110 120 FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 130 140 150 160 170 180 TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 190 200 210 220 230 240 IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 250 260 270 280 290 300 YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 310 320 330 340 350 360 PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 370 380 390 400 410 420 TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 430 440 450 460 470 480 RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 490 500 510 520 GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c." Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M. Biochem. J. 314:313-319(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Lymphocyte.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"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] (ISOFORMS 1 AND 2). Tissue: Hippocampus and Kidney.
[4]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, MASS SPECTROMETRY.
[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].
[6]	"Crystal structure of the human peptidylprolyl isomerase-like 2 isoform B." Structural genomics consortium (SGC) Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U37219 mRNA. Translation: AAC50376.1.
U37220 mRNA. Translation: AAC50377.1.
U37221 mRNA. Translation: AAC50378.1.
CR456548 mRNA. Translation: CAG30434.1.
BC028385 mRNA. Translation: AAH28385.1.
BC000022 mRNA. Translation: AAH00022.1.

IPI

IPI00003824.
IPI00217324.

PIR

S64705.

RefSeq

NP_055152.1. NM_014337.3.
NP_680480.1. NM_148175.2.
NP_680481.1. NM_148176.2.

UniGene

Hs.438587.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZKC	X-ray	1.65	A/B	280-457	[»]

ProteinModelPortal

Q13356.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000390427.

PTM databases

PhosphoSite

Q13356.

Polymorphism databases

DMDM

23813917.

Proteomic databases

PaxDb

Q13356.

PeptideAtlas

Q13356.

PRIDE

Q13356.

Protocols and materials databases

DNASU

23759.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335025; ENSP00000334553; ENSG00000100023.
ENST00000398831; ENSP00000381812; ENSG00000100023.
ENST00000406385; ENSP00000384299; ENSG00000100023.
ENST00000412327; ENSP00000390427; ENSG00000100023.
ENST00000492445; ENSP00000445312; ENSG00000100023.

GeneID

23759.

KEGG

hsa:23759.

UCSC

uc002zvg.4. human.
uc002zvh.4. human.

Organism-specific databases

CTD

23759.

GeneCards

GC22P022006.

HGNC

HGNC:9261. PPIL2.

HPA

HPA035344.

MIM

607588. gene.

neXtProt

NX_Q13356.

PharmGKB

PA33588.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000177172.

HOVERGEN

HBG053655.

InParanoid

Q13356.

KO

K10598.

OMA

LQPFEYP.

PhylomeDB

Q13356.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q13356.

Bgee

Q13356.

CleanEx

HS_PPIL2.

Genevestigator

Q13356.

GermOnline

ENSG00000100023. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR026951. PPIL2.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

PANTHER

PTHR11071:SF42. PTHR11071:SF42. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SMART

SM00504. Ubox. 1 hit.
[Graphical view]

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

PPIL2. human.

EvolutionaryTrace

Q13356.

GenomeRNAi

23759.

NextBio

46699.

SOURCE

Search...

Entry information

Entry name

PPIL2_HUMAN

Accession

Primary (citable) accession number: Q13356
Secondary accession number(s): Q13357, Q8TAH2, Q9BWR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 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.