CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008300
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hsc70-interacting protein 
Protein Synonyms/Alias
 Hip; Protein FAM10A1; Protein ST13 homolog 
Gene Name
 St13 
Gene Synonyms/Alias
 Fam10a1; Hip 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
152RLAILYAKRASVFVKacetylation[1]
185PDSAQPYKWRGKAHRacetylation[1]
359KVMNLISKLSAKFGGacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. 
Sequence Annotation
 REPEAT 113 146 TPR 1.
 REPEAT 147 180 TPR 2.
 REPEAT 181 214 TPR 3.
 DOMAIN 318 357 STI1.
 MOD_RES 345 345 Phosphoserine; by GRK5 (By similarity).  
Keyword
 Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 368 AA 
Protein Sequence
MDPRKVSELR AFVKMCRQDP SVLHTEEMRF LREWVESMGG KVPPATHKAK SEENTKEEKR 60
DKTTEDNIKT EEPSSEESDL EIDNEGVIEA DTDAPQEMGD ENAEITEAMM DEANEKKGAA 120
IDALNDGELQ KAIDLFTDAI KLNPRLAILY AKRASVFVKL QKPNAAIRDC DRAIEINPDS 180
AQPYKWRGKA HRLLGHWEEA ARDLALACKL DYDEDASAML REVQPRAQKI AEHRRKYERK 240
REEREIKERI ERVKKAREEH EKAQREEEAR RQSGSQFGSF PGGFPGGMPG NFPGGMPGMG 300
GAMPGMAGMP GLNEILSDPE VLAAMQDPEV MVAFQDVAQN PSNMSKYQNN PKVMNLISKL 360
SAKFGGHS 368 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0032564; F:dATP binding; IDA:RGD.
 GO:0030544; F:Hsp70 protein binding; IDA:RGD.
 GO:0042802; F:identical protein binding; IDA:RGD.
 GO:0032403; F:protein complex binding; IDA:RGD.
 GO:0019904; F:protein domain specific binding; IDA:RGD.
 GO:0051082; F:unfolded protein binding; IDA:RGD.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:RGD.
 GO:0061084; P:negative regulation of protein refolding; IDA:RGD.
 GO:0051260; P:protein homooligomerization; IDA:RGD. 
Interpro
 IPR006636; STI1_HS-bd.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR013105; TPR_2.
 IPR019734; TPR_repeat. 
Pfam
 PF00515; TPR_1
 PF07719; TPR_2 
SMART
 SM00727; STI1
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS