Reviewed, UniProtKB/Swiss-Prot Q13526 (PIN1_HUMAN)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
    EC=5.2.1.8
Alternative name(s):
    Rotamase Pin1
    PPIase Pin1

Gene names

Name:

PIN1

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	163 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzing pSer/Thr-Pro cis/trans isomerizations.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with STIL By similarity. Interacts with MPHOSPH1.
Subcellular location	Nucleus.
Domain	The WW domain is required for the interaction with STIL and MPHOSPH1.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
Sequence similarities	Contains 1 PpiC domain. Contains 1 WW domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of mitosis Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphoserine binding Inferred from direct assay. Source: UniProtKB phosphothreonine binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NEK6	Q9HC98	2	EBI-714158,EBI-740364
VHL	P40337	1	EBI-714158,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

PRO_0000193435

Regions

Domain

5 – 39

35

WW

Domain

52 – 163

112

PpiC

Amino acid modifications

Modified residue

108

1

Phosphoserine

Experimental info

Mutagenesis

23

1

Y → A: Reduced affinity for MPHOSPH1

Secondary structure

1

.

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.

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163

Helix Strand Turn

Details...

Beta strand

11 – 15

5

Beta strand

22 – 26

5

Turn

27 – 29

3

Beta strand

32 – 35

4

Beta strand

55 – 62

8

Beta strand

67 – 69

3

Beta strand

75 – 77

3

Helix

82 – 98

17

Beta strand

99 – 101

3

Helix

103 – 110

8

Helix

114 – 118

5

Beta strand

121 – 125

5

Helix

132 – 140

9

Beta strand

156 – 163

8

Sequences

	Sequence		Length	Mass (Da)
	Q13526-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 35391AF40B7D1E13	FASTA	163	18,243
	10 20 30 40 50 60 MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL 70 80 90 100 110 120 LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG 130 140 150 160 DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human peptidyl-prolyl isomerase essential for regulation of mitosis." Lu K.P., Hanes S.D., Hunter T. Nature 380:544-547(1996) [PubMed: 8606777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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.
[5]	"Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1." Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M. J. Biol. Chem. 276:37520-37528(2001) [PubMed: 11470801] [Abstract] Cited for: INTERACTION WITH MPHOSPH1, MUTAGENESIS OF TYR-23.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY.
[7]	"Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent." Ranganathan R., Lu K.P., Hunter T., Noel J.P. Cell 89:875-886(1997) [PubMed: 9200606] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U49070 mRNA. Translation: AAC50492.1.
CR407654 mRNA. Translation: CAG28582.1.
BT019331 mRNA. Translation: AAV38138.1.
BC002899 mRNA. Translation: AAH02899.1.

PIR

S68520.

RefSeq

NP_006212.1.

UniGene

Hs.465849

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F8A	X-ray	1.84	B	1-163	[»]
1I6C	NMR	-	A	6-44	[»]
1I8G	NMR	-	B	6-44	[»]
1I8H	NMR	-	B	6-44	[»]
1NMV	NMR	-	A	1-163	[»]
1NMW	NMR	-	A	50-163	[»]
1PIN	X-ray	1.35	A	1-163	[»]
1ZCN	X-ray	1.90	A	1-163	[»]
2F21	X-ray	1.50	A	1-163	[»]
2ITK	X-ray	1.45	A	1-163	[»]
2Q5A	X-ray	1.50	A	1-163	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13526.

PTM databases

PhosphoSite

Q13526.

Proteomic databases

PeptideAtlas

Q13526.

Genome annotation databases

Ensembl

ENSG00000127445. Homo sapiens. [Contig view]

GeneID

5300.

KEGG

hsa:5300.

Organism-specific databases

H-InvDB

HIX0014730.

HGNC

HGNC:8988. PIN1.

HPA

CAB004528.
CAB009326.

MIM

601052. gene.

PharmGKB

PA134978864.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q13526.

HOVERGEN

Q13526.

Gene expression databases

ArrayExpress

Q13526.

CleanEx

HS_PIN1.

GermOnline

ENSG00000127445. Homo sapiens.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
IPR002349. WW.
IPR001202. WW_Rsp5_WWP.
[Graphical view]

Pfam

PF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]

PRINTS

PR00403. WWDOMAIN.

SMART

SM00456. WW. 1 hit.
[Graphical view]

PROSITE

PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q13526.

NextBio

20486.

SOURCE

Search...

Entry information

Entry name

PIN1_HUMAN

Accession

Primary (citable) accession number: Q13526
Secondary accession number(s): Q53X75

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)