CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000050
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Huntingtin-interacting protein 1 
Protein Synonyms/Alias
 HIP-1; Huntingtin-interacting protein I; HIP-I 
Gene Name
 HIP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9DRMASSMKQVPNPLPubiquitination[1, 2, 3, 4]
17QVPNPLPKVLSRRGVubiquitination[1]
144QLCSIYLKLLRTKMEubiquitination[2]
155TKMEYHTKNPRFPGNubiquitination[2, 4]
283SSNLQYFKRLIQIPQubiquitination[2]
395KAQLENMKTESQRVVubiquitination[4]
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] 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
Functional Description
 Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. 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. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors. 
Sequence Annotation
 DOMAIN 32 160 ENTH.
 DOMAIN 771 1012 I/LWEQ.
 REGION 410 491 pDED.
 REGION 867 924 Important for actin binding (By
 MOD_RES 154 154 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Actin-binding; Activator; Alternative splicing; Apoptosis; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Differentiation; Endocytosis; Membrane; Neurodegeneration; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1037 AA 
Protein Sequence
MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT QEVAVKEKHA 60
RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH KLLRDGHPNV LKDSLRYRNE 120
LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN 180
FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV 240
KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR 300
ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI FGSSFSSDPF 360
NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR VVLQLKGHVS ELEADLAEQQ 420
HLRQQAADDC EFLRAELDEL RRQREDTEKA QRSLSEIERK AQANEQRYSK LKEKYSELVQ 480
NHADLLRKNA EVTKQVSMAR QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ 540
ELATSQRELQ VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD 600
TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC AGSADHLLST 660
VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS DAIAHGATTC LRAPPEPADS 720
LTEACKQYGR ETLAYLASLE EEGSLENADS TAMRNCLSKI KAIGEELLPR GLDIKQEELG 780
DLVDKEMAAT SAAIETATAR IEEMLSKSRA GDTGVKLEVN ERILGCCTSL MQAIQVLIVA 840
SKDLQREIVE SGRGTASPKE FYAKNSRWTE GLISASKAVG WGATVMVDAA DLVVQGRGKF 900
EELMVCSHEI AASTAQLVAA SKVKADKDSP NLAQLQQASR GVNQATAGVV ASTISGKSQI 960
EETDNMDFSS MTLTQIKRQE MDSQVRVLEL ENELQKERQK LGELRKKHYE LAGVAEGWEE 1020
GTEASPPTLQ EVVTEKE 1037 
Gene Ontology
 GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
 GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO:0005794; C:Golgi apparatus; IDA:MGI.
 GO:0016020; C:membrane; TAS:ProtInc.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030276; F:clathrin binding; IDA:MGI.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
 GO:0097190; P:apoptotic signaling pathway; IDA:UniProtKB.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0048268; P:clathrin coat assembly; IDA:UniProtKB.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011417; ANTH_dom.
 IPR016024; ARM-type_fold.
 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