Details for: STIP1
Associated with
Other Information
Genular Protein ID: 3694072754
Symbol: STIP1_HUMAN
Name: Stress-induced-phosphoprotein 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 1569099
Title: Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1.
PubMed ID: 1569099
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 1286667
Title: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.
PubMed ID: 1286667
PubMed ID: 9195923
Title: Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
PubMed ID: 9195923
PubMed ID: 10508479
Title: Antigens recognized by autologous antibody in patients with renal-cell carcinoma.
PubMed ID: 10508479
DOI: 10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5
PubMed ID: 14532270
Title: A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.
PubMed ID: 14532270
PubMed ID: 15592455
Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.
PubMed ID: 15592455
DOI: 10.1038/nbt1046
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23349634
Title: A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
PubMed ID: 23349634
PubMed ID: 24880080
Title: SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation.
PubMed ID: 24880080
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 27353360
Title: The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
PubMed ID: 27353360
DOI: 10.1038/ncomms12037
PubMed ID: 29127155
Title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
PubMed ID: 29127155
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 10786835
Title: Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
PubMed ID: 10786835
Sequence Information:
- Length: 543
- Mass: 62639
- Checksum: 8E58ECA13825CB0E
- Sequence:
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.