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Protein

Heat shock protein 105 kDa

Gene

Hsph1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • chaperone mediated protein folding requiring cofactor Source: MGI
  • negative regulation of apoptotic signaling pathway Source: MGI
  • negative regulation of establishment of protein localization to mitochondrion Source: MGI
  • negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide Source: MGI
  • negative regulation of neuron apoptotic process Source: BHF-UCL
  • negative regulation of p38MAPK cascade Source: MGI
  • positive regulation of MHC class I biosynthetic process Source: BHF-UCL
  • positive regulation of NK T cell activation Source: BHF-UCL
  • positive regulation of protein tyrosine kinase activity Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • receptor-mediated endocytosis Source: Reactome
  • regulation of microtubule cytoskeleton organization Source: BHF-UCL
  • response to unfolded protein Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3000484. Scavenging by Class F Receptors.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Hsph1
Synonyms:Hsp105, Hsp110, Kiaa0201
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:105053. Hsph1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular region Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 858857Heat shock protein 105 kDaPRO_0000078285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei471 – 4711N6-acetyllysineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources1 Publication
Modified residuei510 – 5101PhosphoserineCombined sources
Modified residuei558 – 5581PhosphoserineCombined sources
Modified residuei562 – 5621PhosphothreonineBy similarity
Modified residuei810 – 8101PhosphoserineCombined sources
Modified residuei816 – 8161PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61699.
MaxQBiQ61699.
PaxDbiQ61699.
PRIDEiQ61699.

PTM databases

iPTMnetiQ61699.
PhosphoSiteiQ61699.
SwissPalmiQ61699.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

By heat shock. Hsp105-alpha also induced by other stresses.

Gene expression databases

BgeeiQ61699.
CleanExiMM_HSPH1.
ExpressionAtlasiQ61699. baseline and differential.
GenevisibleiQ61699. MM.

Interactioni

Subunit structurei

Interacts with HSPA8/HSC70.2 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi200448. 21 interactions.
DIPiDIP-32354N.
IntActiQ61699. 24 interactions.
MINTiMINT-4097981.
STRINGi10090.ENSMUSP00000074392.

Structurei

3D structure databases

ProteinModelPortaliQ61699.
SMRiQ61699. Positions 3-597, 612-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOVERGENiHBG047955.
InParanoidiQ61699.
KOiK09485.
OMAiANEHELP.
OrthoDBiEOG77M8N0.
PhylomeDBiQ61699.
TreeFamiTF105043.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS01036. HSP70_3. 1 hit.
[Graphical view]

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. AlignAdd to basket

Isoform HSP105-alpha (identifier: Q61699-1) [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

        10         20         30         40         50
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV
60 70 80 90 100
AAKNQQITHA NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG
110 120 130 140 150
IKVMYMDEEH FFSVEQITAM LLTKLKETAE NNLKKPVTDC VISVPSFFTD
160 170 180 190 200
AERRSVLDAA QIVGLNCLRL MNDMTAVALN YGIYKQDLPN AEEKPRVVVF
210 220 230 240 250
VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL VEHFCAEFKT
260 270 280 290 300
KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
310 320 330 340 350
MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV
360 370 380 390 400
KERIAKFFGK DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF
410 420 430 440 450
PISLVWNHDS EETEGVHEVF SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ
460 470 480 490 500
GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV KVRVNTHGIF TISTASMVEK
510 520 530 540 550
VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG TQPQVQTDGQ
560 570 580 590 600
QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
610 620 630 640 650
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL
660 670 680 690 700
CGPYEKFICE QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG
710 720 730 740 750
TPVKVRFQEA EERPKVLEEL GQRLQHYAKI AADFRGKDEK YNHIDESEMK
760 770 780 790 800
KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV VRTHEIRAKV KELNNVCEPV
810 820 830 840 850
VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH QNGECHPNEK

GSVNMDLD
Length:858
Mass (Da):96,407
Last modified:May 16, 2006 - v2
Checksum:i0576A4C2C4715032
GO
Isoform HSP105-beta (identifier: Q61699-2) [UniParc]FASTAAdd to basket

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

Show »
Length:814
Mass (Da):91,698
Checksum:iF43090D86A608E42
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → L in BAC38797 (PubMed:16141072).Curated
Sequence conflicti7 – 82DV → EL in AAA99485 (PubMed:7556594).Curated
Sequence conflicti7 – 71D → N in BAC38797 (PubMed:16141072).Curated
Sequence conflicti12 – 121S → R in BAC38797 (PubMed:16141072).Curated
Sequence conflicti16 – 194AVAR → VGEG in BAC38797 (PubMed:16141072).Curated
Sequence conflicti24 – 241E → D in BAC38797 (PubMed:16141072).Curated
Sequence conflicti28 – 292NE → KD in BAC38797 (PubMed:16141072).Curated
Sequence conflicti159 – 1591A → R in AAA99485 (PubMed:7556594).Curated
Sequence conflicti159 – 1591A → R in BAA11036 (PubMed:8530361).Curated
Sequence conflicti310 – 3101C → S in BAE38016 (PubMed:16141072).Curated
Sequence conflicti320 – 3201P → L in BAA11036 (PubMed:8530361).Curated
Sequence conflicti373 – 3731A → R in AAA99485 (PubMed:7556594).Curated
Sequence conflicti518 – 5181P → FQ in AAA99485 (PubMed:7556594).Curated
Sequence conflicti658 – 6581I → R in BAE27367 (PubMed:16141072).Curated
Sequence conflicti744 – 7441I → N in AAA99485 (PubMed:7556594).Curated
Sequence conflicti838 – 8381A → R in AAA99485 (PubMed:7556594).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei530 – 57344Missing in isoform HSP105-beta. 1 PublicationVSP_002429Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19885.1. [Q61699-1]
PIRiS66666.
RefSeqiNP_038587.2. NM_013559.2. [Q61699-1]
XP_006504977.1. XM_006504914.2. [Q61699-2]
UniGeneiMm.270681.

Genome annotation databases

EnsembliENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657. [Q61699-2]
ENSMUST00000201452; ENSMUSP00000144654; ENSMUSG00000029657. [Q61699-1]
ENSMUST00000202361; ENSMUSP00000144413; ENSMUSG00000029657. [Q61699-1]
GeneIDi15505.
KEGGimmu:15505.
UCSCiuc009apy.1. mouse. [Q61699-1]
uc009apz.1. mouse. [Q61699-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19885.1. [Q61699-1]
PIRiS66666.
RefSeqiNP_038587.2. NM_013559.2. [Q61699-1]
XP_006504977.1. XM_006504914.2. [Q61699-2]
UniGeneiMm.270681.

3D structure databases

ProteinModelPortaliQ61699.
SMRiQ61699. Positions 3-597, 612-715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200448. 21 interactions.
DIPiDIP-32354N.
IntActiQ61699. 24 interactions.
MINTiMINT-4097981.
STRINGi10090.ENSMUSP00000074392.

PTM databases

iPTMnetiQ61699.
PhosphoSiteiQ61699.
SwissPalmiQ61699.

Proteomic databases

EPDiQ61699.
MaxQBiQ61699.
PaxDbiQ61699.
PRIDEiQ61699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657. [Q61699-2]
ENSMUST00000201452; ENSMUSP00000144654; ENSMUSG00000029657. [Q61699-1]
ENSMUST00000202361; ENSMUSP00000144413; ENSMUSG00000029657. [Q61699-1]
GeneIDi15505.
KEGGimmu:15505.
UCSCiuc009apy.1. mouse. [Q61699-1]
uc009apz.1. mouse. [Q61699-2]

Organism-specific databases

CTDi10808.
MGIiMGI:105053. Hsph1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0103. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00390000016919.
HOVERGENiHBG047955.
InParanoidiQ61699.
KOiK09485.
OMAiANEHELP.
OrthoDBiEOG77M8N0.
PhylomeDBiQ61699.
TreeFamiTF105043.

Enzyme and pathway databases

ReactomeiR-MMU-3000484. Scavenging by Class F Receptors.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

PROiQ61699.
SOURCEiSearch...

Gene expression databases

BgeeiQ61699.
CleanExiMM_HSPH1.
ExpressionAtlasiQ61699. baseline and differential.
GenevisibleiQ61699. MM.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 2 hits.
PROSITEiPS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/cJ.
  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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  19. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHS105_MOUSE
AccessioniPrimary (citable) accession number: Q61699
Secondary accession number(s): Q3TNS2
, Q3UIY8, Q62578, Q62579, Q6A0A5, Q8C430, Q8VCW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: June 8, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.