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Q99623 (PHB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prohibitin-2
Alternative name(s):
B-cell receptor-associated protein BAP37
D-prohibitin
Repressor of estrogen receptor activity
Gene names
Name:PHB2
Synonyms:BAP, REA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases By similarity. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. Probably involved in regulating mitochondrial respiration activity and in aging. Ref.2 Ref.9 UniProtKB O35129

Subunit structure

Interacts with PHB, ESR1, HDAC1 and HDAC5 By similarity. Interacts with ZNF703. Interacts with STOML2. Ref.2 Ref.9 Ref.14 Ref.15 UniProtKB O35129

Subcellular location

Mitochondrion inner membrane By similarity. Cytoplasm By similarity. Nucleus By similarity. Note: Also cytoplasmic and nuclear By similarity. Ref.14

Developmental stage

Levels of expression in fibroblasts decrease heterogeneously during cellular aging. Ref.9

Induction

Expression increases approximately 3-fold upon entry into G1 phase compared to other phases of the cell cycle. Also induced following inhibition of mitochondrial protein synthesis by thiamphenicol. Ref.9

Sequence similarities

Belongs to the prohibitin family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionReceptor
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in thelarche

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

nuclear matrix

Inferred from direct assay Ref.14. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionestrogen receptor binding

Non-traceable author statement Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.9Ref.14Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033724EBI-358348,EBI-78473

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99623-1)

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: Q99623-2)

The sequence of this isoform differs from the canonical sequence as follows:
     203-240: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 299298Prohibitin-2
PRO_0000213884

Regions

Region19 – 4931Necessary for transcriptional repression Ref.2
Region150 – 17425Necessary for transcriptional repression Ref.2
Coiled coil190 – 23849 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.16
Modified residue1281Phosphotyrosine Ref.10
Modified residue1471N6-acetyllysine By similarity
Modified residue2001N6-acetyllysine By similarity
Modified residue2361N6-acetyllysine By similarity
Modified residue2501N6-acetyllysine Ref.12
Modified residue2621N6-acetyllysine By similarity

Natural variations

Alternative sequence203 – 24038Missing in isoform 2.
VSP_045311

Sequences

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

Last modified July 1, 1997. Version 2.
Checksum: A887CC982BF85C80

FASTA29933,296
        10         20         30         40         50         60 
MAQNLKDLAG RLPAGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI FFNRIGGVQQ 

        70         80         90        100        110        120 
DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLS RPNAQELPSM 

       130        140        150        160        170        180 
YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD 

       190        200        210        220        230        240 
DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE 

       250        260        270        280        290 
ALSKNPGYIK LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK 

« Hide

Isoform 2 [UniParc].

Checksum: F698CB300517B30A
Show »

FASTA26129,044

References

« Hide 'large scale' references
[1]"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens."
Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P., Katzenellenbogen B.S.
Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1.
Tissue: Mammary cancer.
[3]"Identification of a novel D-prohibitin from dendritic cells."
Zhang W., Wan T., Chen T., Cao X.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Dendritic cell.
[4]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus.
[5]"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] (ISOFORM 2).
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
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 1).
Tissue: Placenta and Skin.
[8]Bienvenut W.V., Lilla S., Zebisch A., Kolch W.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 108-131; 148-157; 172-191; 210-216; 225-236 AND 271-289, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[9]"Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence."
Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H., Hall P.A., Wright E.G.
Exp. Cell Res. 265:262-273(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHB, DEVELOPMENTAL STAGE, INDUCTION.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"ZNF703 gene amplification at 8p12 specifies luminal B breast cancer."
Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I., Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S., Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J., Lopez M., Borg J.P., Sotiriou C., Popovici C. expand/collapse author list , Bertucci F., Birnbaum D., Chaffanet M., Ginestier C.
EMBO Mol. Med. 3:153-166(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF703, SUBCELLULAR LOCATION.
[15]"Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STOML2.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72511 mRNA. Translation: AAC51639.1.
AF150962 mRNA. Translation: AAD38042.1.
AF178980 mRNA. Translation: AAF44345.1.
AF126021 mRNA. Translation: AAF17231.1.
AK298217 mRNA. Translation: BAG60487.1.
U47924 Genomic DNA. Translation: AAB51324.1.
BC014766 mRNA. Translation: AAH14766.1.
BC110322 mRNA. Translation: AAI10323.1.
CCDSCCDS53741.1. [Q99623-1]
CCDS58207.1. [Q99623-2]
RefSeqNP_001138303.1. NM_001144831.1. [Q99623-1]
NP_001254629.1. NM_001267700.1. [Q99623-2]
UniGeneHs.504620.

3D structure databases

ProteinModelPortalQ99623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116459. 72 interactions.
IntActQ99623. 23 interactions.
MINTMINT-142400.
STRING9606.ENSP00000382362.

PTM databases

PhosphoSiteQ99623.

Polymorphism databases

DMDM74752151.

2D gel databases

OGPQ99623.

Proteomic databases

MaxQBQ99623.
PaxDbQ99623.
PeptideAtlasQ99623.
PRIDEQ99623.

Protocols and materials databases

DNASU11331.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000440277; ENSP00000412856; ENSG00000215021. [Q99623-2]
ENST00000535923; ENSP00000441875; ENSG00000215021. [Q99623-1]
ENST00000607236; ENSP00000475972; ENSG00000269079. [Q99623-2]
ENST00000607454; ENSP00000475555; ENSG00000269079. [Q99623-1]
GeneID11331.
KEGGhsa:11331.
UCSCuc010sft.2. human.
uc021quf.1. human. [Q99623-1]

Organism-specific databases

CTD11331.
GeneCardsGC12M007074.
HGNCHGNC:30306. PHB2.
HPACAB014889.
CAB026335.
HPA039874.
MIM610704. gene.
neXtProtNX_Q99623.
PharmGKBPA142671181.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0330.
HOGENOMHOG000205692.
HOVERGENHBG004457.
InParanoidQ99623.
KOK17081.
OMAIGGVKKE.
PhylomeDBQ99623.
TreeFamTF354230.

Gene expression databases

ArrayExpressQ99623.
BgeeQ99623.
CleanExHS_PHB2.
GenevestigatorQ99623.

Family and domain databases

InterProIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERPTHR23222. PTHR23222. 1 hit.
PfamPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSPR00679. PROHIBITIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHB2. human.
GeneWikiPHB2.
GenomeRNAi11331.
NextBio43043.
PROQ99623.
SOURCESearch...

Entry information

Entry namePHB2_HUMAN
AccessionPrimary (citable) accession number: Q99623
Secondary accession number(s): B4DP75 expand/collapse secondary AC list , Q2YDA4, Q7KYU3, Q92978
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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

MIM cross-references

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

Human chromosome 12

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