| Tag | Content |
|---|
| CPLM ID | CPLM-014373 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Heat shock protein 105 kDa |
Protein Synonyms/Alias | 42 degrees C-HSP; Heat shock 110 kDa protein; Heat shock-related 100 kDa protein E7I; HSP-E7I |
Gene Name | Hsph1 |
Gene Synonyms/Alias | Hsp105; Hsp110; Kiaa0201 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 95 | SYDLVPMKNGGVGIK | ubiquitination | [1] | | 234 | FDPFLGGKNFDEKLV | ubiquitination | [1] | | 458 | GVPYPEAKIGRFVVQ | ubiquitination | [1] | | 471 | VQNVSAQKDGEKSRV | ubiquitination | [1] | | 665 | ICEQEHEKFLRLLTE | ubiquitination | [1] | | 750 | HIDESEMKKVEKSVN | ubiquitination | [1] | | 791 | HEIRAKVKELNNVCE | ubiquitination | [1] | | 812 | KPKIESPKLERTPNG | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | MOD_RES 509 509 Phosphoserine.
MOD_RES 558 558 Phosphoserine.
MOD_RES 810 810 Phosphoserine.
MOD_RES 816 816 Phosphothreonine (By similarity). |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 858 AA |
Protein Sequence | MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 60
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM 120
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 180
YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 240
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK 300
MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK 360
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF 420
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV 480
KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG 540
TQPQVQTDGQ QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE 600
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE 660
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPKVLEEL 720
GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV 780
VRTHEIRAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH 840
QNGECHPNEK GSVNMDLD 858 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005576; C:extracellular region; TAS:BHF-UCL. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:MGI. GO:0043524; P:negative regulation of neuron apoptotic process; TAS:BHF-UCL. GO:0045345; P:positive regulation of MHC class I biosynthetic process; TAS:BHF-UCL. GO:0051135; P:positive regulation of NK T cell activation; TAS:BHF-UCL. GO:0070507; P:regulation of microtubule cytoskeleton organization; NAS:BHF-UCL. GO:0006986; P:response to unfolded protein; TAS:BHF-UCL. |
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Pfam | |
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PROSITE | |
PRINTS | |