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

P12272 (PTHR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Parathyroid hormone-related protein

Short name=PTH-rP
Short name=PTHrP
Alternative name(s):
Parathyroid hormone-like protein
Short name=PLP

Cleaved into the following 3 chains:

  1. PTHrP[1-36]
  2. PTHrP[38-94]
  3. Osteostatin
    Alternative name(s):
    PTHrP[107-139]
Gene names
Name:PTHLH
Synonyms:PTHRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Upregulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath By similarity. Promotes colon cancer cell migration and invasion in an integrin alpha-6/beta-1-dependent manner through activation of Rac1. Ref.18

Osteostatin is a potent inhibitor of osteoclastic bone resorption. Ref.18

Subunit structure

PTHrP interacts with PTH1R (via N-terminal extracellular domain). Ref.21

Subcellular location

Cytoplasm. Nucleus. Secreted.

Tissue specificity

Ubiquitous. Also expressed in the mammary gland.

Post-translational modification

There are 3 principal secretory forms, called PTHrP[1-36], PTHrP[38-94], and osteostatin (PTHrP[107-139]) arising from endoproteolytic cleavage of the initial translation product. Each of these secretory forms is believed to have one or more of its own receptors that mediates the normal paracrine, autocrine and endocrine actions.

Involvement in disease

Brachydactyly E2 (BDE2) [MIM:613382]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. Wide variability in the number of digits affected occurs from person to person, even in the same family. Some individuals are moderately short of stature. In brachydactyly type E2 variable combinations of metacarpals are involved, with shortening also of the first and third distal and the second and fifth middle phalanges.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the parathyroid hormone family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandCalcium
   Molecular functionHormone
   PTMCleavage on pair of basic residues
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 9832460. Source: MGI

cAMP metabolic process

Traceable author statement PubMed 2549037. Source: ProtInc

cell-cell signaling

Traceable author statement PubMed 2549037. Source: ProtInc

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

endoderm development

Inferred from electronic annotation. Source: Ensembl

epidermis development

Traceable author statement PubMed 8058749. Source: ProtInc

epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Traceable author statement PubMed 10828849. Source: ProtInc

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

mammary gland bud elongation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement PubMed 8058749. Source: ProtInc

negative regulation of chondrocyte differentiation

Inferred from direct assay PubMed 90087. Source: MGI

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

nipple sheath formation

Inferred from electronic annotation. Source: Ensembl

osteoblast development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP biosynthetic process

Inferred from direct assay PubMed 90087. Source: MGI

positive regulation of cell proliferation

Traceable author statement PubMed 10773581. Source: ProtInc

protein processing

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from direct assay PubMed 90087. Source: MGI

skeletal system development

Inferred from direct assay PubMed 9008714. Source: MGI

surfactant homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement PubMed 8641188. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionhormone activity

Traceable author statement Ref.3. Source: ProtInc

peptide hormone receptor binding

Inferred from direct assay Ref.21. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P12272-1)

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: P12272-2)

The sequence of this isoform differs from the canonical sequence as follows:
     176-177: Missing.
Isoform 3 (identifier: P12272-3)

The sequence of this isoform differs from the canonical sequence as follows:
     176-177: RH → TALLWGLKKKKENNRRTHHMQLMISLFKSPLLLL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 3410
PRO_0000023224
Chain37 – 177141Parathyroid hormone-related protein
PRO_0000023225
Peptide37 – 7236PTHrP[1-36]
PRO_0000023226
Peptide74 – 13057PTHrP[38-94]
PRO_0000023227
Peptide143 – 17533Osteostatin
PRO_0000023228

Regions

Region57 – 6812Important for receptor binding
Motif108 – 12922Nuclear localization signal Ref.16

Natural variations

Alternative sequence176 – 1772Missing in isoform 2.
VSP_004534
Alternative sequence176 – 1772RH → TALLWGLKKKKENNRRTHHM QLMISLFKSPLLLL in isoform 3.
VSP_004535
Natural variant441L → P in BDE2. Ref.23
VAR_063711
Natural variant601L → P in BDE2. Ref.23
VAR_063712
Natural variant1691S → T in a breast cancer sample; somatic mutation. Ref.22
VAR_036433

Experimental info

Mutagenesis571R → A: Strongly reduced affinity for PTH1R. Ref.21
Mutagenesis591F → A: Reduced affinity for PTH1R. Ref.21
Mutagenesis601L → A or K: Strongly reduced affinity for PTH1R. Ref.21
Mutagenesis631L → A: Reduced affinity for PTH1R. Ref.21
Mutagenesis641I → A: Reduced affinity for PTH1R. Ref.21
Mutagenesis681H → A: Reduced affinity for PTH1R. Ref.21

Secondary structure

........ 177
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1989. Version 1.
Checksum: 449FDFEE954C51DB

FASTA17720,194
        10         20         30         40         50         60 
MQRRLVQQWS VAVFLLSYAV PSCGRSVEGL SRRLKRAVSE HQLLHDKGKS IQDLRRRFFL 

        70         80         90        100        110        120 
HHLIAEIHTA EIRATSEVSP NSKPSPNTKN HPVRFGSDDE GRYLTQETNK VETYKEQPLK 

       130        140        150        160        170 
TPGKKKKGKP GKRKEQEKKK RRTRSAWLDS GVTGSGLEGD HLSDTSTTSL ELDSRRH 

« Hide

Isoform 2 [UniParc].

Checksum: 4FEE954C51DB3E7D
Show »

FASTA17519,901
Isoform 3 [UniParc].

Checksum: A994463A90B8EA0F
Show »

FASTA20923,942

References

« Hide 'large scale' references
[1]"A parathyroid hormone-related protein implicated in malignant hypercalcemia: cloning and expression."
Suva L.J., Winslow G.A., Wettenhall R.E.H., Hammonds R.G., Moseley J.M., Diefenbach-Jagger H., Rodda C.P., Kemp B.E., Rodriguez H., Chen E.Y., Hudson P.J., Martin T.J., Wood W.I.
Science 237:893-896(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Identification of a cDNA encoding a parathyroid hormone-like peptide from a human tumor associated with humoral hypercalcemia of malignancy."
Mangin M., Webb A.C., Dreyer B.E., Posillico J.T., Ikeda K., Weir E.C., Stewart A.F., Bander N.H., Milstone L., Barton D.E., Francke U., Broadus A.E.
Proc. Natl. Acad. Sci. U.S.A. 85:597-601(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of the human parathyroid hormone-like peptide gene. Functional and evolutionary aspects."
Yasuda T., Banville D., Hendy G.N., Goltzman D.
J. Biol. Chem. 264:7720-7725(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human renal carcinoma expresses two messages encoding a parathyroid hormone-like peptide: evidence for the alternative splicing of a single-copy gene."
Thiede M.A., Strewler G.J., Nissenson R.A., Rosenblatt M., Rodan G.A.
Proc. Natl. Acad. Sci. U.S.A. 85:4605-4609(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"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] (ISOFORM 1).
[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. 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].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[8]"Structure of the 5' flanking region of the gene encoding human parathyroid-hormone-related protein (PTHrP)."
Suva L.J., Mather K.A., Gillespie M.T., Webb G.C., Ng K.W., Winslow G.A., Wood W.I., Martin T.J., Hudson P.J.
Gene 77:95-105(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-33.
Tissue: Liver.
[9]"Parathyroid hormone-related protein purified from a human lung cancer cell line."
Moseley J.M., Kubota M., Diefenbach-Jagger H., Wettenhall R.E.H., Kemp B.E., Suva L.J., Rodda C.P., Ebeling P.R., Hudson P.J., Zajac J.D., Martin T.J.
Proc. Natl. Acad. Sci. U.S.A. 84:5048-5052(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-52.
[10]"Isolation and characterization of the human parathyroid hormone-like peptide gene."
Mangin M., Ikeda K., Dreyer B.E., Broadus A.E.
Proc. Natl. Acad. Sci. U.S.A. 86:2408-2412(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3).
[11]"A carboxyl-terminal peptide from the parathyroid hormone-related protein inhibits bone resorption by osteoclasts."
Fenton A.J., Kemp B.E., Kent G.N., Moseley J.M., Zheng M.H., Rowe D.J., Britto J.M., Martin T.J., Nicholson G.C.
Endocrinology 129:1762-1768(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
[12]"A potent inhibitor of osteoclastic bone resorption within a highly conserved pentapeptide region of parathyroid hormone-related protein; PTHrP107-111."
Fenton A.J., Kemp B.E., Hammonds R.G., Mitchelhill K., Moseley J.M., Martin T.J., Nicholson G.C.
Endocrinology 129:3424-3426(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
[13]"C-terminal parathyroid hormone-related protein inhibits proliferation and differentiation of human osteoblast-like cells."
Martinez M.E., Garcia-Ocana A., Sanchez M., Medina S., del Campo T., Valin A., Sanchez-Cabezudo M.J., Esbrit P.
J. Bone Miner. Res. 12:778-785(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
[14]"Parathyroid hormone-related protein-(107-139) inhibits bone resorption in vivo."
Cornish J., Callon K.E., Nicholson G.C., Reid I.R.
Endocrinology 138:1299-1304(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
[15]"Parathyroid hormone-related protein (PTHrP): a nucleocytoplasmic shuttling protein with distinct paracrine and intracrine roles."
Jans D.A., Thomas R.J., Gillespie M.T.
Vitam. Horm. 66:345-384(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOCYTOPLASMIC SHUTTLING.
[16]"Molecular dissection of the importin beta1-recognized nuclear targeting signal of parathyroid hormone-related protein."
Lam M.H., Hu W., Xiao C.Y., Gillespie M.T., Jans D.A.
Biochem. Biophys. Res. Commun. 282:629-634(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL.
[17]"Minireview: parathyroid hormone-related protein as an intracrine factor -- trafficking mechanisms and functional consequences."
Fiaschi-Taesch N.M., Stewart A.F.
Endocrinology 144:407-411(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[18]"PTHrP promotes colon cancer cell migration and invasion in an integrin alpha6beta4-dependent manner through activation of Rac1."
Mula R.V., Bhatia V., Falzon M.
Cancer Lett. 298:119-127(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution."
Weidler M., Marx U.C., Seidel G., Schafer W., Hoffmann E., Esswein A., Rosch P.
FEBS Lett. 444:239-244(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 37-70.
[20]"Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta."
Cingolani G., Bednenko J., Gillespie M.T., Gerace L.
Mol. Cell 10:1345-1353(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 103-130.
[21]"Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides."
Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E.
J. Biol. Chem. 284:28382-28391(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 48-70 IN COMPLEX WITH PTH1R, INTERACTION WITH PTH1R, MUTAGENESIS OF ARG-57; PHE-59; LEU-60; LEU-63; ILE-64 AND HIS-68.
[22]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-169.
[23]"Deletion and point mutations of PTHLH cause brachydactyly type E."
Klopocki E., Hennig B.P., Dathe K., Koll R., de Ravel T., Baten E., Blom E., Gillerot Y., Weigel J.F., Krueger G., Hiort O., Seemann P., Mundlos S.
Am. J. Hum. Genet. 86:434-439(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BDE2 PRO-44 AND PRO-60.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17183 Genomic DNA. Translation: AAA60221.1.
X14304 Genomic DNA. Translation: CAA32480.1.
J03580 mRNA. Translation: AAA60216.1. Sequence problems.
M24349, M24348 Genomic DNA. Translation: AAA60358.1.
M24350, M24348, M24349 Genomic DNA. Translation: AAA60359.1.
M24351, M24348, M24349 Genomic DNA. Translation: AAA60360.1.
CR541882 mRNA. Translation: CAG46680.1.
CH471094 Genomic DNA. Translation: EAW96573.1.
BC005961 mRNA. Translation: AAH05961.1.
J03802 mRNA. Translation: AAA60218.1.
M34071 mRNA. Translation: AAA60217.1.
CCDSCCDS44853.1. [P12272-1]
CCDS8715.1. [P12272-2]
PIRPTHU2L. A33360.
PTHU3L. C33360.
RefSeqNP_002811.1. NM_002820.2. [P12272-2]
NP_945315.1. NM_198964.1. [P12272-2]
NP_945316.1. NM_198965.1. [P12272-1]
NP_945317.1. NM_198966.1. [P12272-1]
XP_005253491.1. XM_005253434.1.
XP_006719178.1. XM_006719115.1. [P12272-1]
UniGeneHs.591159.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZGNMR-A37-70[»]
1ET3model-A37-70[»]
1M5NX-ray2.90Q103-130[»]
3FFDX-ray2.00P37-144[»]
3H3GX-ray1.94B48-70[»]
DisProtDP00138.
ProteinModelPortalP12272.
SMRP12272. Positions 37-70.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111716. 5 interactions.
IntActP12272. 1 interaction.
MINTMINT-1742626.
STRING9606.ENSP00000379213.

PTM databases

PhosphoSiteP12272.

Polymorphism databases

DMDM131542.

Proteomic databases

PaxDbP12272.
PRIDEP12272.

Protocols and materials databases

DNASU5744.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000201015; ENSP00000201015; ENSG00000087494. [P12272-2]
ENST00000354417; ENSP00000346398; ENSG00000087494. [P12272-3]
ENST00000395868; ENSP00000379209; ENSG00000087494. [P12272-2]
ENST00000395872; ENSP00000379213; ENSG00000087494. [P12272-1]
ENST00000535992; ENSP00000440613; ENSG00000087494. [P12272-2]
ENST00000538310; ENSP00000441890; ENSG00000087494. [P12272-3]
ENST00000539239; ENSP00000441571; ENSG00000087494. [P12272-1]
ENST00000545234; ENSP00000441765; ENSG00000087494. [P12272-1]
GeneID5744.
KEGGhsa:5744.
UCSCuc001rik.3. human. [P12272-1]

Organism-specific databases

CTD5744.
GeneCardsGC12M028111.
HGNCHGNC:9607. PTHLH.
HPAHPA035982.
MIM168470. gene.
613382. phenotype.
neXtProtNX_P12272.
Orphanet93387. Brachydactyly type E.
PharmGKBPA33952.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40343.
HOGENOMHOG000115765.
HOVERGENHBG003236.
InParanoidP12272.
OMAPATNTKN.
OrthoDBEOG7FBRK8.
PhylomeDBP12272.
TreeFamTF332953.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP12272.
BgeeP12272.
CleanExHS_PTHLH.
GenevestigatorP12272.

Family and domain databases

InterProIPR003626. PTH-rel.
IPR001415. PTH/PTH-rel.
[Graphical view]
PANTHERPTHR17223. PTHR17223. 1 hit.
PfamPF01279. Parathyroid. 1 hit.
[Graphical view]
SMARTSM00087. PTH. 1 hit.
[Graphical view]
PROSITEPS00335. PARATHYROID. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12272.
GeneWikiParathyroid_hormone-related_protein.
GenomeRNAi5744.
NextBio22362.
PMAP-CutDBP12272.
PROP12272.
SOURCESearch...

Entry information

Entry namePTHR_HUMAN
AccessionPrimary (citable) accession number: P12272
Secondary accession number(s): Q15251, Q6FH74
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 164 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM