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Q99623

- PHB2_HUMAN

UniProt

Q99623 - PHB2_HUMAN

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Protein

Prohibitin-2

Gene
PHB2, BAP, REA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  1. estrogen receptor binding Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. mammary gland alveolus development Source: Ensembl
  2. mammary gland branching involved in thelarche Source: Ensembl
  3. negative regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
  4. negative regulation of mammary gland epithelial cell proliferation Source: Ensembl
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. regulation of branching involved in mammary gland duct morphogenesis Source: Ensembl
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Prohibitin-2
Alternative name(s):
B-cell receptor-associated protein BAP37
D-prohibitin
Repressor of estrogen receptor activity
Gene namesi
Name:PHB2
Synonyms:BAP, REA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30306. PHB2.

Subcellular locationi

Mitochondrion inner membrane By similarity. Cytoplasm By similarity. Nucleus By similarity
Note: Also cytoplasmic and nuclear By similarity.1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrion Source: UniProt
  4. nuclear matrix Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 299298Prohibitin-2PRO_0000213884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei128 – 1281Phosphotyrosine1 Publication
Modified residuei147 – 1471N6-acetyllysine By similarity
Modified residuei200 – 2001N6-acetyllysine By similarity
Modified residuei236 – 2361N6-acetyllysine By similarity
Modified residuei250 – 2501N6-acetyllysine1 Publication
Modified residuei262 – 2621N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99623.
PaxDbiQ99623.
PeptideAtlasiQ99623.
PRIDEiQ99623.

2D gel databases

OGPiQ99623.

PTM databases

PhosphoSiteiQ99623.

Expressioni

Developmental stagei

Levels of expression in fibroblasts decrease heterogeneously during cellular aging.1 Publication

Inductioni

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.1 Publication

Gene expression databases

ArrayExpressiQ99623.
BgeeiQ99623.
CleanExiHS_PHB2.
GenevestigatoriQ99623.

Organism-specific databases

HPAiCAB014889.
CAB026335.
HPA039874.

Interactioni

Subunit structurei

Interacts with PHB, ESR1, HDAC1 and HDAC5 By similarity. Interacts with ZNF703. Interacts with STOML2.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033724EBI-358348,EBI-78473

Protein-protein interaction databases

BioGridi116459. 72 interactions.
IntActiQ99623. 23 interactions.
MINTiMINT-142400.
STRINGi9606.ENSP00000382362.

Structurei

3D structure databases

ProteinModelPortaliQ99623.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 4931Necessary for transcriptional repression1 PublicationAdd
BLAST
Regioni150 – 17425Necessary for transcriptional repression1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili190 – 23849 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the prohibitin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0330.
HOGENOMiHOG000205692.
HOVERGENiHBG004457.
InParanoidiQ99623.
KOiK17081.
OMAiIGGVKKE.
PhylomeDBiQ99623.
TreeFamiTF354230.

Family and domain databases

InterProiIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERiPTHR23222. PTHR23222. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00679. PROHIBITIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99623-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAQNLKDLAG RLPAGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI    50
FFNRIGGVQQ DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ 100
MVNISLRVLS RPNAQELPSM YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA 150
SQLITQRAQV SLLIRRELTE RAKDFSLILD DVAITELSFS REYTAAVEAK 200
QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE ALSKNPGYIK 250
LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK 299
Length:299
Mass (Da):33,296
Last modified:July 1, 1997 - v2
Checksum:iA887CC982BF85C80
GO
Isoform 2 (identifier: Q99623-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:261
Mass (Da):29,044
Checksum:iF698CB300517B30A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei203 – 24038Missing in isoform 2. VSP_045311Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53741.1. [Q99623-1]
CCDS58207.1. [Q99623-2]
RefSeqiNP_001138303.1. NM_001144831.1. [Q99623-1]
NP_001254629.1. NM_001267700.1. [Q99623-2]
UniGeneiHs.504620.

Genome annotation databases

EnsembliENST00000440277; ENSP00000412856; ENSG00000215021. [Q99623-2]
ENST00000535923; ENSP00000441875; ENSG00000215021. [Q99623-1]
ENST00000607236; ENSP00000475972; ENSG00000269079. [Q99623-2]
ENST00000607454; ENSP00000475555; ENSG00000269079. [Q99623-1]
GeneIDi11331.
KEGGihsa:11331.
UCSCiuc010sft.2. human.
uc021quf.1. human. [Q99623-1]

Polymorphism databases

DMDMi74752151.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS53741.1. [Q99623-1 ]
CCDS58207.1. [Q99623-2 ]
RefSeqi NP_001138303.1. NM_001144831.1. [Q99623-1 ]
NP_001254629.1. NM_001267700.1. [Q99623-2 ]
UniGenei Hs.504620.

3D structure databases

ProteinModelPortali Q99623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116459. 72 interactions.
IntActi Q99623. 23 interactions.
MINTi MINT-142400.
STRINGi 9606.ENSP00000382362.

PTM databases

PhosphoSitei Q99623.

Polymorphism databases

DMDMi 74752151.

2D gel databases

OGPi Q99623.

Proteomic databases

MaxQBi Q99623.
PaxDbi Q99623.
PeptideAtlasi Q99623.
PRIDEi Q99623.

Protocols and materials databases

DNASUi 11331.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000440277 ; ENSP00000412856 ; ENSG00000215021 . [Q99623-2 ]
ENST00000535923 ; ENSP00000441875 ; ENSG00000215021 . [Q99623-1 ]
ENST00000607236 ; ENSP00000475972 ; ENSG00000269079 . [Q99623-2 ]
ENST00000607454 ; ENSP00000475555 ; ENSG00000269079 . [Q99623-1 ]
GeneIDi 11331.
KEGGi hsa:11331.
UCSCi uc010sft.2. human.
uc021quf.1. human. [Q99623-1 ]

Organism-specific databases

CTDi 11331.
GeneCardsi GC12M007074.
HGNCi HGNC:30306. PHB2.
HPAi CAB014889.
CAB026335.
HPA039874.
MIMi 610704. gene.
neXtProti NX_Q99623.
PharmGKBi PA142671181.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0330.
HOGENOMi HOG000205692.
HOVERGENi HBG004457.
InParanoidi Q99623.
KOi K17081.
OMAi IGGVKKE.
PhylomeDBi Q99623.
TreeFami TF354230.

Miscellaneous databases

ChiTaRSi PHB2. human.
GeneWikii PHB2.
GenomeRNAii 11331.
NextBioi 43043.
PROi Q99623.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99623.
Bgeei Q99623.
CleanExi HS_PHB2.
Genevestigatori Q99623.

Family and domain databases

InterProi IPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view ]
PANTHERi PTHR23222. PTHR23222. 1 hit.
Pfami PF01145. Band_7. 1 hit.
[Graphical view ]
PRINTSi PR00679. PROHIBITIN.
SMARTi SM00244. PHB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHB2_HUMAN
AccessioniPrimary (citable) accession number: Q99623
Secondary accession number(s): B4DP75
, Q2YDA4, Q7KYU3, Q92978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi