Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13526 (PIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

EC=5.2.1.8
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name=PPIase Pin1
Rotamase Pin1
Gene names
Name:PIN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Ref.8 Ref.10 Ref.11 Ref.17 Ref.18

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subunit structure

Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML (isoform PML-4)and BCL-6. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17 Ref.18

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. Note: Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization. Ref.9 Ref.18

Tissue specificity

The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. Ref.11 Ref.18

Domain

The WW domain is required for the interaction with STIL and KIF20B.

Post-translational modification

Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.

Sequence similarities

Contains 1 PpiC domain.

Contains 1 WW domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 20179103. Source: BHF-UCL

negative regulation of cell motility

Inferred from direct assay PubMed 20179103. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 19122240. Source: BHF-UCL

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of Rho GTPase activity

Inferred from mutant phenotype PubMed 20179103. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from genetic interaction PubMed 19638580. Source: MGI

positive regulation of ubiquitin-protein ligase activity

Inferred from direct assay PubMed 19122240. Source: BHF-UCL

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from direct assay PubMed 19122240. Source: GOC

regulation of cytokinesis

Inferred from mutant phenotype PubMed 19638580. Source: MGI

regulation of mitosis

Traceable author statement PubMed 10391244. Source: ProtInc

regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 19122240. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 19638580. Source: MGI

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 20179103. Source: BHF-UCL

   Molecular_functionGTPase activating protein binding

Inferred from physical interaction PubMed 20179103. Source: BHF-UCL

mitogen-activated protein kinase kinase binding

Inferred from physical interaction PubMed 20179103. Source: BHF-UCL

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay PubMed 19122240. Source: BHF-UCL

phosphoserine binding

Inferred from direct assay PubMed 10037602. Source: BHF-UCL

phosphothreonine binding

Inferred from direct assay PubMed 10037602. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
PRO_0000193435

Regions

Domain5 – 3935WW
Domain52 – 163112PpiC

Amino acid modifications

Modified residue461N6-acetyllysine Ref.15
Modified residue711Phosphoserine; by DAPK1 Ref.18
Modified residue1081Phosphoserine Ref.12

Experimental info

Mutagenesis231Y → A: Reduced affinity for KIF20B. Ref.7
Mutagenesis711S → D or E: Loss of activity, nuclear localization and cellular function. Ref.18

Secondary structure

................................ 163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13526 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 35391AF40B7D1E13

FASTA16318,243
        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 

« Hide

References

« Hide '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] [Europe PMC] [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]"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. expand/collapse author list , 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].
[5]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. expand/collapse author list , 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].
[6]"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: Lung.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF20B, MUTAGENESIS OF TYR-23.
[8]"Regulation of Raf-1 by direct feedback phosphorylation."
Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z., Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K.
Mol. Cell 17:215-224(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAF1.
[9]"Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients."
Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L.
Biochem. Biophys. Res. Commun. 341:1059-1065(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
[10]"Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1."
Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I.
J. Biol. Chem. 281:18201-18207(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BTX, FUNCTION.
[11]"Genotoxic stress regulates expression of the proto-oncogene Bcl6 in germinal center B cells."
Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.
Nat. Immunol. 8:1132-1139(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BCL6 STABILITY REGULATION, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons."
Buschdorf J.P., Chew L.L., Soh U.J., Liou Y.C., Low B.C.
PLoS ONE 3:E2686-E2686(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATCAY.
[14]"Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development."
Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D.
Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKX.
[15]"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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
Lim J.H., Liu Y., Reineke E., Kao H.Y.
J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML.
[18]"Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function."
Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S., Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.
Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, TISSUE SPECIFICITY.
[19]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49070 mRNA. Translation: AAC50492.1.
CR407654 mRNA. Translation: CAG28582.1.
BT019331 mRNA. Translation: AAV38138.1.
AK291074 mRNA. Translation: BAF83763.1.
CH471106 Genomic DNA. Translation: EAW84057.1.
BC002899 mRNA. Translation: AAH02899.1.
PIRS68520.
RefSeqNP_006212.1. NM_006221.3.
UniGeneHs.465849.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8AX-ray1.84B1-163[»]
1I6CNMR-A6-44[»]
1I8GNMR-B6-44[»]
1I8HNMR-B6-44[»]
1NMVNMR-A1-163[»]
1NMWNMR-A50-163[»]
1PINX-ray1.35A1-163[»]
1ZCNX-ray1.90A1-161[»]
2F21X-ray1.50A1-162[»]
2ITKX-ray1.45A1-163[»]
2KBUNMR-A6-39[»]
2KCFNMR-A6-39[»]
2LB3NMR-A6-41[»]
2M9ENMR-A6-39[»]
2M9FNMR-A6-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2Q5AX-ray1.50A1-163[»]
2XP3X-ray2.00A1-163[»]
2XP4X-ray1.80A1-163[»]
2XP5X-ray1.90A1-163[»]
2XP6X-ray1.90A1-163[»]
2XP7X-ray2.00A1-163[»]
2XP8X-ray2.10A1-163[»]
2XP9X-ray1.90A1-163[»]
2XPAX-ray1.90A1-163[»]
2XPBX-ray2.00A1-163[»]
2ZQSX-ray1.90A1-163[»]
2ZQTX-ray1.46A1-163[»]
2ZQUX-ray2.50A1-163[»]
2ZQVX-ray2.50A1-163[»]
2ZR4X-ray2.00A1-163[»]
2ZR5X-ray2.60A1-163[»]
2ZR6X-ray3.20A1-163[»]
3I6CX-ray1.30A/B45-163[»]
3IK8X-ray1.85A/B45-163[»]
3IKDX-ray2.00A/B45-163[»]
3IKGX-ray1.86A/B45-163[»]
3JYJX-ray1.87A/B45-163[»]
3KABX-ray2.19A1-163[»]
3KACX-ray2.00A/B44-163[»]
3KADX-ray1.95A1-163[»]
3KAFX-ray2.30A1-163[»]
3KAGX-ray1.90A1-163[»]
3KAHX-ray2.30A1-163[»]
3KAIX-ray1.90A1-163[»]
3KCEX-ray1.90A1-163[»]
3NTPX-ray1.76A1-163[»]
3ODKX-ray2.30A1-163[»]
3OOBX-ray1.89A1-163[»]
3TC5X-ray1.40A1-163[»]
3TCZX-ray2.10A6-163[»]
3TDBX-ray2.27A6-163[»]
4GWTX-ray2.25A6-39[»]
4GWVX-ray3.05A6-39[»]
ProteinModelPortalQ13526.
SMRQ13526. Positions 1-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111317. 154 interactions.
DIPDIP-29306N.
IntActQ13526. 79 interactions.
MINTMINT-86298.
STRING9606.ENSP00000247970.

Chemistry

BindingDBQ13526.
ChEMBLCHEMBL2288.

PTM databases

PhosphoSiteQ13526.

Polymorphism databases

DMDM3024406.

Proteomic databases

PaxDbQ13526.
PeptideAtlasQ13526.
PRIDEQ13526.

Protocols and materials databases

DNASU5300.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247970; ENSP00000247970; ENSG00000127445.
ENST00000588695; ENSP00000466962; ENSG00000127445.
GeneID5300.
KEGGhsa:5300.
UCSCuc002mmk.2. human.

Organism-specific databases

CTD5300.
GeneCardsGC19P009945.
HGNCHGNC:8988. PIN1.
HPACAB004528.
CAB009326.
MIM601052. gene.
neXtProtNX_Q13526.
PharmGKBPA33320.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0760.
HOGENOMHOG000275331.
HOVERGENHBG002101.
InParanoidQ13526.
KOK09578.
OMAFALKVGD.
PhylomeDBQ13526.
TreeFamTF101101.

Enzyme and pathway databases

BRENDA5.2.1.8. 2681.
ReactomeREACT_6900. Immune System.
SignaLinkQ13526.

Gene expression databases

ArrayExpressQ13526.
BgeeQ13526.
CleanExHS_PIN1.
GenevestigatorQ13526.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS01096. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ13526.
GeneWikiPIN1.
GenomeRNAi5300.
NextBio20486.
PROQ13526.
SOURCESearch...

Entry information

Entry namePIN1_HUMAN
AccessionPrimary (citable) accession number: Q13526
Secondary accession number(s): A8K4V9, Q53X75
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM