CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021838
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Huntingtin-interacting protein 1-related protein 
Protein Synonyms/Alias
 HIP1-related protein 
Gene Name
 Hip1r 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
5***MNSIKNVPARVLubiquitination[1]
37TQAISISKAINSQEAubiquitination[1]
146TKISFHLKHPQFPAGubiquitination[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
 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 (By  
Keyword
 Actin-binding; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endocytosis; Membrane; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1068 AA 
Protein Sequence
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN SQEAPVKEKH ARRIILGTHH 60
EKGAFTFWSY AIGLPLSSSS ILSWKFCHVL HKVLRDGHPN VLHDYQRYRS NIREIGDLWG 120
HLRDQYGHLV NIYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF 180
DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLMFKLHSC 240
LPADTLQGHR DRFHEQFHSL KNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK 300
PVVVIPEEAP EEEEPENLIE ISSAPPAGEP VVVADLFDQT FGPPNGSMKD DRDLQIENLK 360
REVETLRAEL EKIKMEAQRY ISQLKGQVNG LEAELEEQRK QKQKALVDNE QLRHELAQLK 420
ALQLEGARNQ GLREEAERKA SATEARYSKL KEKHSELINT HAELLRKNAD TAKQLTVTQQ 480
SQEEVARVKE QLAFQMEQAK RESEMKMEEQ SDQLEKLKRE LAARAGELAR AQEALSRTEQ 540
SGSELSSRLD TLNAEKEALS GVVRQREAEL LAAQSLVREK EEALSQEQQR SSQEKGELRG 600
QLAEKESQEQ GLRQKLLDEQ LAVLRSAAAE AEAILQDAVS KLDDPLHLRC TSSPDYLVSR 660
AQAALDSVSG LEQGHTQYLA SSEDASALVA ALTRFSHLAA DTIVNGAATS HLAPTDPADR 720
LMDTCRECGA RALELVGQLQ DQTVLPRAQP SLMRAPLQGI LQLGQDLKPK SLDVRQEELG 780
AMVDKEMAAT SAAIEDAVRR IEDMMSQARH ESSGVKLEVN ERILNSCTDL MKAIRLLVMT 840
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVESA DKVVLHMGKY 900
EELIVCSHEI AASTAQLVAA SKVKANKNSP HLSRLQECSR TVNERAANVV ASTKSGQEQI 960
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERVR LGELRKQHYV LAGGMGTPSE 1020
EEPSRPSPAP RSGATKKPPL AQKPSIAPRT DNQLDKKDGV YPAQLVNY 1068 
Gene Ontology
 GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
 GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005905; C:coated pit; IDA:MGI.
 GO:0005856; C:cytoskeleton; IDA:MGI.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; IDA:MGI.
 GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
 GO:0006898; P:receptor-mediated endocytosis; ISS: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