CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001122
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Huntingtin-interacting protein 1-related protein 
Protein Synonyms/Alias
 HIP1-related protein; Huntingtin-interacting protein 12; HIP-12 
Gene Name
 HIP1R 
Gene Synonyms/Alias
 HIP12; KIAA0655 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MNSIKNVPARVLubiquitination[1, 2, 3, 4]
146TKISFHLKHPQFPAGacetylation[5]
146TKISFHLKHPQFPAGubiquitination[2, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3- phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. 
Sequence Annotation
 DOMAIN 23 151 ENTH.
 DOMAIN 771 1012 I/LWEQ.
 REGION 867 924 Important for actin binding.
 MOD_RES 1017 1017 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis; Membrane; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1068 AA 
Protein Sequence
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN TQEAPVKEKH ARRIILGTHH 60
EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN VLHDCQRYRS NIREIGDLWG 120
HLHDRYGQLV NVYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF 180
DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLLFKLHSC 240
LPADTLQGHR DRFHEQFHSL RNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK 300
PVVVIPEEAP EDEEPENLIE ISTGPPAGEP VVVADLFDQT FGPPNGSVKD DRDLQIESLK 360
REVEMLRSEL EKIKLEAQRY IAQLKSQVNA LEGELEEQRK QKQKALVDNE QLRHELAQLR 420
AAQLEGERSQ GLREEAERKA SATEARYNKL KEKHSELVHV HAELLRKNAD TAKQLTVTQQ 480
SQEEVARVKE QLAFQVEQVK RESELKLEEK SDQLEKLKRE LEAKAGELAR AQEALSHTEQ 540
SKSELSSRLD TLSAEKDALS GAVRQREADL LAAQSLVRET EAALSREQQR SSQEQGELQG 600
RLAERESQEQ GLRQRLLDEQ FAVLRGAAAE AAGILQDAVS KLDDPLHLRC TSSPDYLVSR 660
AQEALDAVST LEEGHAQYLT SLADASALVA ALTRFSHLAA DTIINGGATS HLAPTDPADR 720
LIDTCRECGA RALELMGQLQ DQQALRHMQA SLVRTPLQGI LQLGQELKPK SLDVRQEELG 780
AVVDKEMAAT SAAIEDAVRR IEDMMNQARH ASSGVKLEVN ERILNSCTDL MKAIRLLVTT 840
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVEAA DKVVLHTGKY 900
EELIVCSHEI AASTAQLVAA SKVKANKHSP HLSRLQECSR TVNERAANVV ASTKSGQEQI 960
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERMR LGELRKQHYV LAGASGSPGE 1020
EVAIRPSTAP RSVTTKKPPL AQKPSVAPRQ DHQLDKKDGI YPAQLVNY 1068 
Gene Ontology
 GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
 GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005905; C:coated pit; NAS:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB. 
Interpro
 IPR011417; ANTH_dom.
 IPR008942; ENTH_VHS.
 IPR013809; Epsin-like_N.
 IPR002558; ILWEQ_dom. 
Pfam
 PF07651; ANTH
 PF01608; I_LWEQ 
SMART
 SM00273; ENTH
 SM00307; ILWEQ 
PROSITE
 PS50942; ENTH
 PS50945; I_LWEQ 
PRINTS