Q61699 (HS105_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock protein 105 kDa

Alternative name(s):
42 degrees C-HSP
Heat shock 110 kDa protein
Heat shock-related 100 kDa protein E7I
Short name=HSP-E7I

Gene names

Name:	Hsph1
Synonyms:	Hsp105, Hsp110, Kiaa0201

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	858 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities. Ref.12 Ref.13
Subunit structure	Interacts with HSPA8/HSC70. Ref.8 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: Strictly cytoplasmic in neurons. Ref.10
Tissue specificity	Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Within the brain, expression is restricted to neurons (at protein level). Overexpressed in cancer cells. Ref.10 Ref.15
Induction	By heat shock. Hsp105-alpha also induced by other stresses.
Post-translational modification	Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone mediated protein folding requiring cofactor Inferred from direct assay Ref.12. Source: MGI negative regulation of neuron apoptotic process Traceable author statement PubMed 12749852. Source: BHF-UCL positive regulation of MHC class I biosynthetic process Traceable author statement PubMed 12952910. Source: BHF-UCL positive regulation of NK T cell activation Traceable author statement PubMed 12952910. Source: BHF-UCL regulation of microtubule cytoskeleton organization Non-traceable author statement PubMed 12749852. Source: BHF-UCL response to unfolded protein Traceable author statement PubMed 9931472. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Traceable author statement PubMed 12952910. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alpha-tubulin binding Inferred from direct assay PubMed 12749852. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform HSP105-alpha (identifier: Q61699-1)

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.

Isoform HSP105-beta (identifier: Q61699-2)

The sequence of this isoform differs from the canonical sequence as follows:
     530-573: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 858	858	Heat shock protein 105 kDa		PRO_0000078285
Amino acid modifications
	Modified residue	509	1	Phosphoserine Ref.11
	Modified residue	558	1	Phosphoserine Ref.14
	Modified residue	810	1	Phosphoserine Ref.16 Ref.17 Ref.18
	Modified residue	816	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	530 – 573	44	Missing in isoform HSP105-beta.		VSP_002429
Experimental info
	Sequence conflict	2	1	S → L in BAC38797. Ref.4
	Sequence conflict	7 – 8	2	DV → EL in AAA99485. Ref.1
	Sequence conflict	7	1	D → N in BAC38797. Ref.4
	Sequence conflict	12	1	S → R in BAC38797. Ref.4
	Sequence conflict	16 – 19	4	AVAR → VGEG in BAC38797. Ref.4
	Sequence conflict	24	1	E → D in BAC38797. Ref.4
	Sequence conflict	28 – 29	2	NE → KD in BAC38797. Ref.4
	Sequence conflict	159	1	A → R in AAA99485. Ref.1
	Sequence conflict	159	1	A → R in BAA11036. Ref.2
	Sequence conflict	310	1	C → S in BAE38016. Ref.4
	Sequence conflict	320	1	P → L in BAA11036. Ref.2
	Sequence conflict	373	1	A → R in AAA99485. Ref.1
	Sequence conflict	518	1	P → FQ in AAA99485. Ref.1
	Sequence conflict	658	1	I → R in BAE27367. Ref.4
	Sequence conflict	744	1	I → N in AAA99485. Ref.1
	Sequence conflict	838	1	A → R in AAA99485. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform HSP105-alpha [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 0576A4C2C4715032	FASTA	858	96,407
	10 20 30 40 50 60 MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 70 80 90 100 110 120 NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM 130 140 150 160 170 180 LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 190 200 210 220 230 240 YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 250 260 270 280 290 300 VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK 310 320 330 340 350 360 MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK 370 380 390 400 410 420 DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF 430 440 450 460 470 480 SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV 490 500 510 520 530 540 KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG 550 560 570 580 590 600 TQPQVQTDGQ QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE 610 620 630 640 650 660 ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE 670 680 690 700 710 720 QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPKVLEEL 730 740 750 760 770 780 GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV 790 800 810 820 830 840 VRTHEIRAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH 850 QNGECHPNEK GSVNMDLD
	Isoform HSP105-beta [UniParc]. Checksum: F43090D86A608E42	FASTA	814	91,698
	10 20 30 40 50 60 MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 70 80 90 100 110 120 NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM 130 140 150 160 170 180 LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 190 200 210 220 230 240 YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 250 260 270 280 290 300 VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK 310 320 330 340 350 360 MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK 370 380 390 400 410 420 DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF 430 440 450 460 470 480 SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV 490 500 510 520 530 540 KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDA NEKKVDQPPE 550 560 570 580 590 600 AKKPKIKVVN VELPVEANLV WQLGRDLLNM YIETEGKMIM QDKLEKERND AKNAVEECVY 610 620 630 640 650 660 EFRDKLCGPY EKFICEQEHE KFLRLLTETE DWLYEEGEDQ AKQAYIDKLE ELMKMGTPVK 670 680 690 700 710 720 VRFQEAEERP KVLEELGQRL QHYAKIAADF RGKDEKYNHI DESEMKKVEK SVNEVMEWMN 730 740 750 760 770 780 NVMNAQAKRS LDQDPVVRTH EIRAKVKELN NVCEPVVTQP KPKIESPKLE RTPNGPNIDK 790 800 810 KEDLEGKNNL GAEAPHQNGE CHPNEKGSVN MDLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HPV16 E7 oncoprotein induces expression of a 110 kDa heat shock protein." Morozov A., Subjeck J., Raychaudhuri P. FEBS Lett. 371:214-218(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HSP105-ALPHA).
[2]	"Cloning and expression of murine high molecular mass heat shock proteins, HSP105." Yasuda K., Nakai A., Hatayama T., Nagata K. J. Biol. Chem. 270:29718-29723(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HSP105-ALPHA AND HSP105-BETA).
[3]	"Genomic cloning and promoter analysis of the mouse 105-kDa heat shock protein (HSP105) gene." Yasuda K., Ishihara K., Nakashima K., Hatayama T. Biochem. Biophys. Res. Commun. 256:75-80(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM HSP105-ALPHA). Strain: BALB/c.
[4]	"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. , 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] (ISOFORM HSP105-ALPHA). Strain: C57BL/6J. Tissue: Eye, Hippocampus and Liver.
[5]	"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 HSP105-ALPHA). Strain: NMRI. Tissue: Mammary gland.
[6]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-68; 74-82; 361-374 AND 462-471, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-858. Tissue: Pancreatic islet.
[8]	"Association of HSP105 with HSC70 in high molecular mass complexes in mouse FM3A cells." Hatayama T., Yasuda K., Yasuda K. Biochem. Biophys. Res. Commun. 248:395-401(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPA8.
[9]	"Phosphorylation of the 105-kDa heat shock proteins, HSP105alpha and HSP105beta, by casein kinase II." Ishihara K., Yasuda K., Hatayama T. Biochem. Biophys. Res. Commun. 270:927-931(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[10]	"The distribution and localization of hsp110 in brain." Hylander B.L., Chen X., Graf P.C.F., Subjeck J.R. Brain Res. 869:49-55(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[11]	"Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its function." Ishihara K., Yamagishi N., Hatayama T. Biochem. J. 371:917-925(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-509.
[12]	"Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP." Yamagishi N., Ishihara K., Saito Y., Hatayama T. FEBS Lett. 555:390-396(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity." Yamagishi N., Ishihara K., Hatayama T. J. Biol. Chem. 279:41727-41733(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPA8, FUNCTION.
[14]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, MASS SPECTROMETRY. Tissue: Embryonic brain.
[15]	"DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer and melanoma in mice through activation of both CD4 T cells and CD8 T cells." Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S., Komori H., Yoshitake Y., Motomura Y., Minohara M., Kubo T., Ishihara K., Hatayama T., Ogawa M., Nishimura Y. Cancer Sci. 96:695-705(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, MASS SPECTROMETRY. Tissue: Brain cortex.
[17]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, MASS SPECTROMETRY. Tissue: Macrophage.
[18]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L40406 mRNA. Translation: AAA99485.1. D67016 mRNA. Translation: BAA11035.1. D67017 mRNA. Translation: BAA11036.1. AB005282 Genomic DNA. Translation: BAA74540.1. AK083179 mRNA. Translation: BAC38797.1. AK146697 mRNA. Translation: BAE27367.1. AK165046 mRNA. Translation: BAE38016.1. BC018378 mRNA. Translation: AAH18378.1. AK172913 mRNA. Translation: BAD32191.1.
IPI	IPI00123802. IPI00224109.
PIR	S66666.
RefSeq	NP_038587.2. NM_013559.2.
UniGene	Mm.270681.
3D structure databases
ProteinModelPortal	Q61699.
SMR	Q61699. Positions 2-715.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32354N.
IntAct	Q61699. 3 interactions.
PTM databases
PhosphoSite	Q61699.
Proteomic databases
PaxDb	Q61699.
PRIDE	Q61699.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657. ENSMUST00000076410; ENSMUSP00000075746; ENSMUSG00000029657.
GeneID	15505.
KEGG	mmu:15505.
UCSC	uc009apx.1. mouse. uc009apz.1. mouse.
Organism-specific databases
CTD	10808.
MGI	MGI:105053. Hsph1.
Rouge	Search...
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00390000016919.
HOVERGEN	HBG047955.
InParanoid	Q61699.
KO	K09485.
OMA	NDEKYNH.
OrthoDB	EOG4KD6KC.
Gene expression databases
ArrayExpress	Q61699.
Bgee	Q61699.
CleanEx	MM_HSPH1.
Genevestigator	Q61699.
GermOnline	ENSMUSG00000029657. Mus musculus.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. False negative. PS00329. HSP70_2. False negative. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	288408.
SOURCE	Search...

Entry information

Entry name

HS105_MOUSE

Accession

Primary (citable) accession number: Q61699
Secondary accession number(s): Q3TNS2 , Q3UIY8, Q62578, Q62579, Q6A0A5, Q8C430, Q8VCW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program