CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017643
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 EH domain-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
 EHBP1 
Gene Synonyms/Alias
 KIAA0903; NACSIN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
163CIFLREGKATDEDMQubiquitination[1]
763TSLSPTSKLGYSYSRubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
 May play a role in actin reorganization. Links clathrin- mediated endocytosis to the actin cytoskeleton. 
Sequence Annotation
 DOMAIN 443 545 CH.
 MOD_RES 171 171 Phosphoserine.
 MOD_RES 174 174 Phosphoserine.
 MOD_RES 177 177 Phosphoserine.
 MOD_RES 432 432 Phosphoserine.
 MOD_RES 436 436 Phosphoserine.
 MOD_RES 710 710 Phosphoserine.
 MOD_RES 964 964 Phosphoserine.
 MOD_RES 1019 1019 Phosphoserine (By similarity).
 MOD_RES 1058 1058 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1231 AA 
Protein Sequence
MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP 60
GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN 120
MKQYASPMPT QTDVKLKFKP LSKKVVSAAL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ 180
ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANMRSAK 240
SASSSEELIN KLNFLDEAEK DLATVNSNPF DDPDAAELNP FGDPDSEEPI TETASPRKTE 300
DSFYNNSYNP FKEVQTPQYL NPFDEPEAFV TIKDSPPQST KRKNIRPVDM SKYLYADSSK 360
TEEEELDESN PFYEPKSTPP PNNLVNPVQE LETERRVKRK APAPPVLSPK TGVLNENTVS 420
AGKDLSTSPK PSPIPSPVLG RKPNASQSLL VWCKEVTKNY RGVKITNFTT SWRNGLSFCA 480
ILHHFRPDLI DYKSLNPQDI KENNKKAYDG FASIGISRLL EPSDMVLLAI PDKLTVMTYL 540
YQIRAHFSGQ ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD LKREPELQQP 600
ISGAVDFLSQ DDSVFVNDSG VGESESEHQT PDDHLSPSTA SPYCRRTKSD TEPQKSQQSS 660
GRTSGSDDPG ICSNTDSTQA QVLLGKKRLL KAETLELSDL YVSDKKKDMS PPFICEETDE 720
QKLQTLDIGS NLEKEKLENS RSLECRSDPE SPIKKTSLSP TSKLGYSYSR DLDLAKKKHA 780
SLRQTESDPD ADRTTLNHAD HSSKIVQHRL LSRQEELKER ARVLLEQARR DAALKAGNKH 840
NTNTATPFCN RQLSDQQDEE RRRQLRERAR QLIAEARSGV KMSELPSYGE MAAEKLKERS 900
KASGDENDNI EIDTNEEIPE GFVVGGGDEL TNLENDLDTP EQNSKLVDLK LKKLLEVQPQ 960
VANSPSSAAQ KAVTESSEQD MKSGTEDLRT ERLQKTTERF RNPVVFSKDS TVRKTQLQSF 1020
SQYIENRPEM KRQRSIQEDT KKGNEEKAAI TETQRKPSED EVLNKGFKDT SQYVVGELAA 1080
LENEQKQIDT RAALVEKRLR YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE 1140
KEHDLERRYE LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVNKRD ALVRDLDAQE 1200
KQAEEEDEHL ERTLEQNKGK MAKKEEKCVL Q 1231 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 
Interpro
 IPR001715; CH-domain.
 IPR022735; DUF3585.
 IPR019448; NT-C2. 
Pfam
 PF00307; CH
 PF12130; DUF3585
 PF10358; NT-C2 
SMART
 SM00033; CH 
PROSITE
 PS50021; CH 
PRINTS