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Q8BK64 (AHSA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:Ahsa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

Function

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

Subunit structure

Interacts with HSPCA/HSP90. Interacts with GCH1 By similarity. Interacts with SRPK1 By similarity.

Subcellular location

Cytoplasm › cytosol By similarity. Endoplasmic reticulum By similarity. Note: May transiently interact with the endoplasmic reticulum By similarity.

Induction

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

Sequence similarities

Belongs to the AHA1 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Endoplasmic reticulum
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from sequence or structural similarity. Source: UniProtKB

response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATPase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1
PRO_0000215821

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31N6-acetyllysine By similarity
Modified residue1931Phosphoserine By similarity
Modified residue2121N6-acetyllysine By similarity

Experimental info

Sequence conflict1921P → L in BAC36160. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BK64 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: C4F0F94FF44F9FB3

FASTA33838,117
        10         20         30         40         50         60 
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTEKL KTLFLAVRVE NEEGKCEVTE 

        70         80         90        100        110        120 
VNKLDGEASI NNRKGKLIFF YEWTIKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS 

       130        140        150        160        170        180 
VSLAKDEPDT NLVALMKEDG VKLLREAVGI YISTLKTEFT QGMILPTVNG ESVDPVGQPA 

       190        200        210        220        230        240 
LKTETCKAKS APSKSQAKPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA 

       250        260        270        280        290        300 
ALEADRGGKF HMVDGNVTGE FTDLVPEKHI AMKWRFKSWP EGHFATITLT FIDKNGETEL 

       310        320        330 
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[2]"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].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK076069 mRNA. Translation: BAC36160.1.
BC023857 mRNA. Translation: AAH23857.1.
BC025552 mRNA. Translation: AAH25552.1.
IPIIPI00153740.
RefSeqNP_666148.1. NM_146036.1.
UniGeneMm.22626.

3D structure databases

ProteinModelPortalQ8BK64.
SMRQ8BK64. Positions 25-126, 204-335.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000021425.

PTM databases

PhosphoSiteQ8BK64.

2D gel databases

REPRODUCTION-2DPAGEQ8BK64.

Proteomic databases

PaxDbQ8BK64.
PRIDEQ8BK64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021425; ENSMUSP00000021425; ENSMUSG00000021037.
GeneID217737.
KEGGmmu:217737.
UCSCuc007oit.1. mouse.

Organism-specific databases

CTD10598.
MGIMGI:2387603. Ahsa1.

Phylogenomic databases

eggNOGCOG5580.
GeneTreeENSGT00390000006429.
HOGENOMHOG000242852.
HOVERGENHBG065806.
InParanoidQ8BK64.
OMAKNCIDWA.
OrthoDBEOG4Q84XQ.

Gene expression databases

BgeeQ8BK64.
GenevestigatorQ8BK64.
GermOnlineENSMUSG00000021037. Mus musculus.

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. AHSA1_N. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAHSA1. mouse.
NextBio376016.
SOURCESearch...

Entry information

Entry nameAHSA1_MOUSE
AccessionPrimary (citable) accession number: Q8BK64
Secondary accession number(s): Q8R3E6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents