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O95433

- AHSA1_HUMAN

UniProt

O95433 - AHSA1_HUMAN

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Protein
Activator of 90 kDa heat shock protein ATPase homolog 1
Gene
AHSA1, C14orf3, HSPC322
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. ATPase activator activity Source: MGI
  2. chaperone binding Source: MGI
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of ATPase activity Source: GOC
  2. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Activator of 90 kDa heat shock protein ATPase homolog 1
Short name:
AHA1
Alternative name(s):
p38
Gene namesi
Name:AHSA1
Synonyms:C14orf3
ORF Names:HSPC322
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:1189. AHSA1.

Subcellular locationi

Cytoplasmcytosol. Endoplasmic reticulum
Note: May transiently interact with the endoplasmic reticulum.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB-SubCell
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1
PRO_0000215820Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei193 – 1931Phosphoserine2 Publications
Modified residuei212 – 2121N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95433.
PaxDbiO95433.
PeptideAtlasiO95433.
PRIDEiO95433.

2D gel databases

REPRODUCTION-2DPAGEIPI00030706.

PTM databases

PhosphoSiteiO95433.

Expressioni

Tissue specificityi

Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.1 Publication

Inductioni

By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).1 Publication

Gene expression databases

ArrayExpressiO95433.
BgeeiO95433.
CleanExiHS_AHSA1.
GenevestigatoriO95433.

Organism-specific databases

HPAiCAB006244.
HPA000903.

Interactioni

Subunit structurei

Interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatitis virus glycoprotein (VSV G). Interacts with GCH1. Interacts with SRPK1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GCH1P307933EBI-448610,EBI-958183
HSP90AA1P079004EBI-448610,EBI-296047

Protein-protein interaction databases

BioGridi115846. 21 interactions.
IntActiO95433. 10 interactions.
MINTiMINT-5002315.
STRINGi9606.ENSP00000216479.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 21712
Helixi219 – 2257
Helixi229 – 2357
Turni253 – 2564
Beta strandi261 – 2655
Turni266 – 2683
Beta strandi269 – 2768
Beta strandi285 – 2906
Beta strandi298 – 30811
Helixi309 – 3179
Turni318 – 3236
Helixi324 – 3307

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X53NMR-A204-335[»]
ProteinModelPortaliO95433.
SMRiO95433. Positions 25-146, 204-335.

Miscellaneous databases

EvolutionaryTraceiO95433.

Family & Domainsi

Sequence similaritiesi

Belongs to the AHA1 family.

Phylogenomic databases

eggNOGiCOG5580.
HOGENOMiHOG000242852.
HOVERGENiHBG065806.
InParanoidiO95433.
OMAiPEVSHEN.
PhylomeDBiO95433.
TreeFamiTF313680.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTiSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMiSSF103111. SSF103111. 1 hit.

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: O95433-1) [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

MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ    50
NEEGKCEVTE VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK 100
GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEEG VKLLREAMGI 150
YISTLKTEFT QGMILPTMNG ESVDPVGQPA LKTEERKAKP APSKTQARPV 200
GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA TLEADRGGKF 250
HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL 300
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF 338
Length:338
Mass (Da):38,274
Last modified:May 1, 1999 - v1
Checksum:iE6B686DDD8D7D729
GO
Isoform 2 (identifier: O95433-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-338: HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF → SHCHSG

Note: No experimental confirmation available.

Show »
Length:288
Mass (Da):32,340
Checksum:i4ACB777F0ED29F4E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei283 – 33856HFATI…GARLF → SHCHSG in isoform 2.
VSP_055797Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 682EA → CL in AAF29000. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243310 mRNA. Translation: CAB45684.1.
AF164791 mRNA. Translation: AAF80755.1.
AK300766 mRNA. Translation: BAG62431.1.
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.
CCDSiCCDS9863.1.
PIRiJC7769.
RefSeqiNP_036243.1. NM_012111.2.
UniGeneiHs.204041.

Genome annotation databases

EnsembliENST00000216479; ENSP00000216479; ENSG00000100591.
ENST00000535854; ENSP00000440108; ENSG00000100591.
GeneIDi10598.
KEGGihsa:10598.
UCSCiuc001xtw.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243310 mRNA. Translation: CAB45684.1 .
AF164791 mRNA. Translation: AAF80755.1 .
AK300766 mRNA. Translation: BAG62431.1 .
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 .
CCDSi CCDS9863.1.
PIRi JC7769.
RefSeqi NP_036243.1. NM_012111.2.
UniGenei Hs.204041.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X53 NMR - A 204-335 [» ]
ProteinModelPortali O95433.
SMRi O95433. Positions 25-146, 204-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115846. 21 interactions.
IntActi O95433. 10 interactions.
MINTi MINT-5002315.
STRINGi 9606.ENSP00000216479.

PTM databases

PhosphoSitei O95433.

2D gel databases

REPRODUCTION-2DPAGE IPI00030706.

Proteomic databases

MaxQBi O95433.
PaxDbi O95433.
PeptideAtlasi O95433.
PRIDEi O95433.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216479 ; ENSP00000216479 ; ENSG00000100591 .
ENST00000535854 ; ENSP00000440108 ; ENSG00000100591 .
GeneIDi 10598.
KEGGi hsa:10598.
UCSCi uc001xtw.3. human.

Organism-specific databases

CTDi 10598.
GeneCardsi GC14P077924.
HGNCi HGNC:1189. AHSA1.
HPAi CAB006244.
HPA000903.
MIMi 608466. gene.
neXtProti NX_O95433.
PharmGKBi PA25515.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5580.
HOGENOMi HOG000242852.
HOVERGENi HBG065806.
InParanoidi O95433.
OMAi PEVSHEN.
PhylomeDBi O95433.
TreeFami TF313680.

Miscellaneous databases

ChiTaRSi AHSA1. human.
EvolutionaryTracei O95433.
GeneWikii AHSA1.
GenomeRNAii 10598.
NextBioi 40246.
PROi O95433.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95433.
Bgeei O95433.
CleanExi HS_AHSA1.
Genevestigatori O95433.

Family and domain databases

Gene3Di 3.30.530.20. 1 hit.
InterProi IPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view ]
Pfami PF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view ]
SMARTi SM01000. Aha1_N. 1 hit.
[Graphical view ]
SUPFAMi SSF103111. SSF103111. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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.
    , 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] (ISOFORMS 1 AND 2).
    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.
    , 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. 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] (ISOFORM 1).
    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.
    , 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 (ISOFORM 1).
    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. 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. 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.

Entry informationi

Entry nameiAHSA1_HUMAN
AccessioniPrimary (citable) accession number: O95433
Secondary accession number(s): B2R9L2
, B4DUR9, Q96IL6, Q9P060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 132 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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