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

Q9Y237 (PIN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

EC=5.2.1.8
Alternative name(s):
Parvulin-14
Short name=Par14
Short name=hPar14
Parvulin-17
Short name=Par17
Short name=hPar17
Peptidyl-prolyl cis-trans isomerase Pin4
Short name=PPIase Pin4
Peptidyl-prolyl cis/trans isomerase EPVH
Short name=hEPVH
Rotamase Pin4
Gene names
Name:PIN4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA. Ref.10

Isoform 2 binds to double-stranded DNA. Ref.10

Catalytic activity

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

Subunit structure

Isoform 1 is found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes By similarity. Ref.10

Subcellular location

Isoform 1: Nucleusnucleolus. Cytoplasmcytoskeletonspindle. Cytoplasm. Note: Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1. Ref.1 Ref.2 Ref.6 Ref.7 Ref.9 Ref.10

Isoform 2: Mitochondrion. Mitochondrion matrix. Note: Imported in a time- and membrane potential-dependent manner to the mitochondrial matrix, but without concomitant processing of the protein. Directed to mitochondria by a novel N-terminal domain that functions as non-cleavable mitochondrial targeting peptide. Ref.1 Ref.2 Ref.6 Ref.7 Ref.9 Ref.10

Tissue specificity

Isoform 2 is much more stable than isoform 1 (at protein level). Ubiquitous. Isoform 1 and isoform 2 are expressed in kidney, liver, blood vessel, brain, mammary gland, skeletal muscle, small intestine and submandibularis. Isoform 1 transcripts are much more abundant than isoform 2 in each tissue analyzed. Ref.1 Ref.2 Ref.5

Domain

The PPIase domain enhances mitochondrial targeting.

Post-translational modification

Phosphorylated. Isoform 1 phosphorylation occurs both in the nucleus and the cytoplasm. Isoform 1 phosphorylation at Ser-19 does not affect its PPIase activity but is required for nuclear localization, and the dephosphorylation is a prerequisite for the binding to DNA. The unphosphorylated isoform 1 associates with the pre-rRNP complexes in the nucleus. Ref.7 Ref.10

Isoform 2 is sumoylated with SUMO2 and SUMO3. Ref.5

Sequence similarities

Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.

Contains 1 PpiC domain.

Sequence caution

The sequence AAH05234.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH70288.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI04654.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI11395.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG54532.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q9Y237-1)

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: Q9Y237-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPMAGLLKGLVRQLERFSVQQQASKM
Note: The first 25 amino acids are sufficient for mitochondrial targeting.
Isoform 3 (identifier: Q9Y237-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPMAGLLKGLVRQLERFSVQQQASKM
     80-131: GDLGWMTRGS...YHIIMVEGRK → IPSLQQHAGHHRDLRSTLISLVSYLQTTP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
PRO_0000193438

Regions

Domain35 – 12995PpiC
Region1 – 4141Necessary for association with the pre-rRNP complexes
Region1 – 2525Necessary for nuclear localization and DNA-binding

Amino acid modifications

Modified residue191Phosphoserine; by CK2 Ref.7

Natural variations

Alternative sequence11M → MPMAGLLKGLVRQLERFSVQ QQASKM in isoform 2 and isoform 3.
VSP_037754
Alternative sequence80 – 13152GDLGW…VEGRK → IPSLQQHAGHHRDLRSTLIS LVSYLQTTP in isoform 3.
VSP_046122
Isoform 2:
Natural variant161R → Q.
Corresponds to variant rs6525589 [ dbSNP | Ensembl ].
Natural variant181S → R.
Corresponds to variant rs7058353 [ dbSNP | Ensembl ].

Experimental info

Mutagenesis191S → A: Abolishes phosphorylation and reduces strongly nuclear localization. Ref.7
Mutagenesis191S → E: Does not abolish nuclear localization and reduces DNA-binding ability. Ref.7

Secondary structure

................... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 787C15BDB0701258

FASTA13113,810
        10         20         30         40         50         60 
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS 

        70         80         90        100        110        120 
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF 

       130 
GYHIIMVEGR K 

« Hide

Isoform 2 [UniParc].

Checksum: 8D4668D3ADB24740
Show »

FASTA15616,608
Isoform 3 [UniParc].

Checksum: B217F63257D92D65
Show »

FASTA13314,179

References

« Hide 'large scale' references
[1]"Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases."
Rulten S.L., Thorpe J.R., Kay J.E.
Biochem. Biophys. Res. Commun. 259:557-562(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase."
Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.
FEBS Lett. 446:278-282(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
Tissue: Brain, Prostate and Urinary bladder.
[5]"Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation."
Mueller J.W., Kessler D., Neumann D., Stratmann T., Papatheodorou P., Hartmann-Fatu C., Bayer P.
BMC Mol. Biol. 7:9-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-13 (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, SUMOYLATION, TISSUE SPECIFICITY, VARIANTS GLN-16 AND ARG-18 (ISOFORM 2).
[6]"The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae."
Kessler D., Papatheodorou P., Stratmann T., Dian E.A., Hartmann-Fatu C., Rassow J., Bayer P., Mueller J.W.
BMC Biol. 5:37-37(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 AND 48-72, ALTERNATIVE PROMOTER USAGE (ISOFORMS 1 AND 2), DNA-BINDING, SUBCELLULAR LOCATION.
[7]"Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14."
Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U., Bayer P., Fischer G.
J. Mol. Biol. 330:955-966(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, SUBCELLULAR LOCATION.
[8]"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] OF 19-131 (ISOFORM 3).
Tissue: Brain.
[9]"The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding."
Surmacz T.A., Bayer E., Rahfeld J.-U., Fischer G., Bayer P.
J. Mol. Biol. 321:235-247(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, SUBCELLULAR LOCATION.
[10]"Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage."
Fujiyama-Nakamura S., Yoshikawa H., Homma K., Hayano T., Tsujimura-Takahashi T., Izumikawa K., Ishikawa H., Miyazawa N., Yanagida M., Miura Y., Shinkawa T., Yamauchi Y., Isobe T., Takahashi N.
Mol. Cell. Proteomics 8:1552-1565(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN PRE-RRNP COMPLEXES, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[11]"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].
[12]"NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein."
Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C., Fischer G., Bayer P.
J. Mol. Biol. 301:1003-1017(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 36-131.
[13]"Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14."
Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T., Yokoyama S., Uchida T.
J. Mol. Biol. 305:917-926(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-131.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF143096 mRNA. Translation: AAD27893.1.
AB009690 mRNA. Translation: BAA82320.1.
BX119917, AL135749 Genomic DNA. Translation: CAI39856.1.
BC005234 mRNA. Translation: AAH05234.2. Different initiation.
BC070288 mRNA. Translation: AAH70288.1. Different initiation.
BC093700 mRNA. Translation: AAH93700.1.
BC104653 mRNA. Translation: AAI04654.1. Different initiation.
BC111394 mRNA. Translation: AAI11395.1. Different initiation.
BC112281 mRNA. Translation: AAI12282.1.
AM420633 Genomic DNA. Translation: CAM12362.1.
AK127605 mRNA. Translation: BAG54532.1. Different initiation.
RefSeqNP_001164218.1. NM_001170747.1.
NP_006214.2. NM_006223.3.
UniGeneHs.655623.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQ3NMR-A36-131[»]
1FJDNMR-A30-131[»]
3UI4X-ray0.80A36-131[»]
3UI5X-ray1.40A36-131[»]
3UI6X-ray0.89A36-131[»]
ProteinModelPortalQ9Y237.
SMRQ9Y237. Positions 36-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111320. 21 interactions.
DIPDIP-50838N.
IntActQ9Y237. 6 interactions.
STRING9606.ENSP00000218432.

Chemistry

BindingDBQ9Y237.
ChEMBLCHEMBL4923.

PTM databases

PhosphoSiteQ9Y237.

Polymorphism databases

DMDM20139299.

Proteomic databases

PaxDbQ9Y237.
PRIDEQ9Y237.

Protocols and materials databases

DNASU5303.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373669; ENSP00000362773; ENSG00000102309. [Q9Y237-2]
ENST00000423432; ENSP00000409154; ENSG00000102309. [Q9Y237-3]
GeneID5303.
KEGGhsa:5303.
UCSCuc004eam.3. human. [Q9Y237-2]

Organism-specific databases

CTD5303.
GeneCardsGC0XP071401.
H-InvDBHIX0016866.
HGNCHGNC:8992. PIN4.
HPAHPA054483.
MIM300252. gene.
neXtProtNX_Q9Y237.
PharmGKBPA33324.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0760.
HOVERGENHBG019150.
InParanoidQ9Y237.
KOK09579.
OMAKSGMKFN.
PhylomeDBQ9Y237.
TreeFamTF101102.

Gene expression databases

ArrayExpressQ9Y237.
BgeeQ9Y237.
CleanExHS_PIN4.
GenevestigatorQ9Y237.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
[Graphical view]
PROSITEPS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y237.
GeneWikiPIN4.
GenomeRNAi5303.
NextBio20496.
PROQ9Y237.
SOURCESearch...

Entry information

Entry namePIN4_HUMAN
AccessionPrimary (citable) accession number: Q9Y237
Secondary accession number(s): A8E0G6 expand/collapse secondary AC list , B3KXM0, F5H1P5, Q0D2H3, Q3MHV0, Q52M21, Q5HYW6, Q6IRW4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 118 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 X

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