CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008299
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hsc70-interacting protein 
Protein Synonyms/Alias
 Hip; Aging-associated protein 2; Progesterone receptor-associated p48 protein; Protein FAM10A1; Putative tumor suppressor ST13; Renal carcinoma antigen NY-REN-33; Suppression of tumorigenicity 13 protein 
Gene Name
 ST13 
Gene Synonyms/Alias
 AAG2; FAM10A1; HIP; SNC6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14NELRAFVKMCKQDPSubiquitination[1, 2, 3, 4]
17RAFVKMCKQDPSVLHubiquitination[3]
41WVESMGGKVPPATQKubiquitination[1, 2, 4, 5]
48KVPPATQKAKSEENTubiquitination[2]
50PPATQKAKSEENTKEubiquitination[2]
56AKSEENTKEEKPDSKubiquitination[2, 5]
59EENTKEEKPDSKKVEubiquitination[2]
63KEEKPDSKKVEEDLKubiquitination[2]
118MDQANDKKVAAIEALubiquitination[2, 3, 6]
142DLFTDAIKLNPRLAIubiquitination[1, 3, 4, 6]
153RLAILYAKRASVFVKacetylation[7]
153RLAILYAKRASVFVKubiquitination[1, 2, 3, 4, 6]
160KRASVFVKLQKPNAAubiquitination[1, 3, 4, 5, 6]
163SVFVKLQKPNAAIRDubiquitination[1, 3, 4]
186PDSAQPYKWRGKAHRubiquitination[1, 2, 3, 4, 5, 6, 8, 9]
222EDASAMLKEVQPRAQubiquitination[2]
353SKYQSNPKVMNLISKubiquitination[2, 3, 5, 6, 9, 10, 11]
360KVMNLISKLSAKFGGubiquitination[2, 3, 5, 6, 9, 10, 11]
364LISKLSAKFGGQA**ubiquitination[2, 3, 5, 6, 8, 9, 10, 11, 12]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
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 (By similarity). 
Sequence Annotation
 REPEAT 114 147 TPR 1.
 REPEAT 148 181 TPR 2.
 REPEAT 182 215 TPR 3.
 DOMAIN 319 358 STI1.
 MOD_RES 346 346 Phosphoserine; by GRK5.  
Keyword
 3D-structure; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 369 AA 
Protein Sequence
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP 60
DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA 120
AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD 180
SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER 240
KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM 300
GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK 360
LSAKFGGQA 369 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0032564; F:dATP binding; IEA:Compara.
 GO:0030674; F:protein binding, bridging; TAS:ProtInc.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IEA:Compara.
 GO:0061084; P:negative regulation of protein refolding; IEA:Compara.
 GO:0006457; P:protein folding; TAS:ProtInc.
 GO:0051260; P:protein homooligomerization; IEA:Compara. 
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