O95433 (AHSA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol. 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Endoplasmic reticulum
Molecular function	Chaperone
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from sequence or structural similarity. Source: UniProtKB response to stress Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATPase activator activity Inferred from sequence or structural similarity. Source: UniProtKB chaperone binding Inferred from direct assay Ref.9. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GCH1	P30793	3	EBI-448610,EBI-958183
HSP90AA1	P07900	4	EBI-448610,EBI-296047

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 338

338

Activator of 90 kDa heat shock protein ATPase homolog 1

PRO_0000215820

Amino acid modifications

Modified residue

3

1

N6-acetyllysine Ref.13

Modified residue

212

1

N6-acetyllysine Ref.13

Experimental info

Sequence conflict

67 – 68

2

EA → CL in AAF29000. Ref.7

Secondary structure

1

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338

Helix Strand Turn

Details...

Beta strand

206 – 217

12

Helix

219 – 225

7

Helix

229 – 235

7

Turn

253 – 256

4

Beta strand

261 – 265

5

Turn

266 – 268

3

Beta strand

269 – 276

8

Beta strand

285 – 290

6

Beta strand

298 – 308

11

Helix

309 – 317

9

Turn

318 – 323

6

Helix

324 – 330

7

Sequences

	Sequence		Length	Mass (Da)
	O95433 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: E6B686DDD8D7D729	FASTA	338	38,274
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10931946] [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. , 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: 14702039] [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. , 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: 12508121] [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. , 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: 15489334] [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. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [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: 11554768] [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: 12504007] [Abstract] Cited for: INTERACTION WITH HSPCA, 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: 12604615] [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: 16696853] [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: 19240134] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-212, MASS SPECTROMETRY.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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.

IPI

IPI00030706.

PIR

JC7769.

RefSeq

NP_036243.1. NM_012111.2.

UniGene

Hs.204041.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X53	NMR	-	A	204-335	[»]

ProteinModelPortal

O95433.

SMR

O95433. Positions 23-165, 204-335.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95433. 8 interactions.

STRING

O95433.

PTM databases

PhosphoSite

O95433.

2D gel databases

REPRODUCTION-2DPAGE

IPI00030706.

Proteomic databases

PeptideAtlas

O95433.

PRIDE

O95433.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216479; ENSP00000216479; ENSG00000100591.

GeneID

10598.

KEGG

hsa:10598.

UCSC

uc001xtw.1. human.

Organism-specific databases

CTD

10598.

GeneCards

GC14P077924.

H-InvDB

HIX0011851.

HGNC

HGNC:1189. AHSA1.

HPA

CAB006244.
HPA000903.

MIM

608466. gene.

neXtProt

NX_O95433.

PharmGKB

PA25515.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06147.

GeneTree

ENSGT00390000006429.

HOGENOM

HBG407506.

HOVERGEN

HBG065806.

InParanoid

O95433.

OMA

EKNATPW.

OrthoDB

EOG4Q84XQ.

PhylomeDB

O95433.

Gene expression databases

ArrayExpress

O95433.

Bgee

O95433.

CleanEx

HS_AHSA1.

Genevestigator

O95433.

GermOnline

ENSG00000100591. Homo sapiens.

Family and domain databases

InterPro

IPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]

Gene3D

G3DSA:3.30.530.20. G3DSA:3.30.530.20. 1 hit.

Pfam

PF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]

SMART

SM01000. Aha1_N. 1 hit.
[Graphical view]

SUPFAM

SSF103111. AHSA1_N. 1 hit.

ProtoNet

Search...

Other

NextBio

40246.

SOURCE

Search...

Entry information

Entry name

AHSA1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.