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O95433 (AHSA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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:
Activator of 90 kDa heat shock protein ATPase homolog 1

Short name=AHA1
Alternative name(s):
p38
Gene names
Name:AHSA1
Synonyms:C14orf3
ORF Names:HSPC322
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cochaperone that stimulates HSP90 ATPase activity By similarity. May affect a step in the endoplasmic reticulum to Golgi trafficking.

Subunit structure

Interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatitis virus glycoprotein (VSV G). Interacts with GCH1. Interacts with SRPK1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasmcytosol. Endoplasmic reticulum. Note: May transiently interact with the endoplasmic reticulum. Ref.8

Tissue specificity

Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta. Ref.8

Induction

By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG). Ref.9

Sequence similarities

Belongs to the AHA1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GCH1P307933EBI-448610,EBI-958183
HSP90AA1P079004EBI-448610,EBI-296047

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1
PRO_0000215820

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue31N6-acetyllysine Ref.13
Modified residue1931Phosphoserine Ref.14 Ref.16
Modified residue2121N6-acetyllysine Ref.13

Experimental info

Sequence conflict67 – 682EA → CL in AAF29000. Ref.7

Secondary structure

.................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95433 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E6B686DDD8D7D729

FASTA33838,274
        10         20         30         40         50         60 
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE 

        70         80         90        100        110        120 
VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS 

       130        140        150        160        170        180 
VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA 

       190        200        210        220        230        240 
LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA 

       250        260        270        280        290        300 
TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL 

       310        320        330 
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a novel gene underexpressed in Down syndrome."
Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E., Scott H.S.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Adrenal gland.
[3]"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].
Tissue: Brain.
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 and Ovary.
[7]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338.
Tissue: Umbilical cord blood.
[8]"p38: a novel protein that associates with the vesicular stomatitis virus glycoprotein."
Sevier C.S., Machamer C.E.
Biochem. Biophys. Res. Commun. 287:574-582(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VSV G, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1."
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H., Prodromou C.
Mol. Cell 10:1307-1318(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSPCA, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
[10]"Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
Lotz G.P., Lin H., Harst A., Obermann W.M.J.
J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSPCA.
[11]"A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions."
Swick L., Kapatos G.
J. Neurochem. 97:1447-1455(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCH1.
[12]"Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRPK1.
[13]"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 ALA-2; LYS-3 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The solution structure of the C-terminal domain of human activator of 90 kDa heat shock protein ATPase homolog 1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 204-335.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243310 mRNA. Translation: CAB45684.1.
AF164791 mRNA. Translation: AAF80755.1.
AK313824 mRNA. Translation: BAG36559.1.
AF111168 Genomic DNA. Translation: AAD09623.1.
CH471061 Genomic DNA. Translation: EAW81291.1.
BC000321 mRNA. Translation: AAH00321.1.
BC007398 mRNA. Translation: AAH07398.2.
AF161440 mRNA. Translation: AAF29000.1.
PIRJC7769.
RefSeqNP_036243.1. NM_012111.2.
UniGeneHs.204041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X53NMR-A204-335[»]
ProteinModelPortalO95433.
SMRO95433. Positions 25-146, 204-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115846. 21 interactions.
IntActO95433. 10 interactions.
MINTMINT-5002315.
STRING9606.ENSP00000216479.

PTM databases

PhosphoSiteO95433.

2D gel databases

REPRODUCTION-2DPAGEIPI00030706.

Proteomic databases

PaxDbO95433.
PeptideAtlasO95433.
PRIDEO95433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216479; ENSP00000216479; ENSG00000100591.
GeneID10598.
KEGGhsa:10598.
UCSCuc001xtw.3. human.

Organism-specific databases

CTD10598.
GeneCardsGC14P077924.
HGNCHGNC:1189. AHSA1.
HPACAB006244.
HPA000903.
MIM608466. gene.
neXtProtNX_O95433.
PharmGKBPA25515.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5580.
HOGENOMHOG000242852.
HOVERGENHBG065806.
InParanoidO95433.
OMAWTEKNAT.
PhylomeDBO95433.
TreeFamTF313680.

Gene expression databases

ArrayExpressO95433.
BgeeO95433.
CleanExHS_AHSA1.
GenevestigatorO95433.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMSSF103111. SSF103111. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAHSA1. human.
EvolutionaryTraceO95433.
GeneWikiAHSA1.
GenomeRNAi10598.
NextBio40246.
PROO95433.
SOURCESearch...

Entry information

Entry nameAHSA1_HUMAN
AccessionPrimary (citable) accession number: O95433
Secondary accession number(s): B2R9L2, Q96IL6, Q9P060
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 128 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 14

Human chromosome 14: entries, gene names and cross-references to MIM