CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000236
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 FCH domain only protein 1 
Protein Synonyms/Alias
  
Gene Name
 FCHO1 
Gene Synonyms/Alias
 KIAA0290 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31KQGPISTKELADFIRubiquitination[1]
192ARADFEQKMLDSALRubiquitination[1]
262SKGTGREKPGPLDFEubiquitination[1]
814ATWNLEEKRLTWRLPubiquitination[1]
Reference
 [1] 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
Functional Description
 Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors. 
Sequence Annotation
 DOMAIN 2 83 FCH.
 DOMAIN 625 888 MHD.
 REGION 1 275 Mediates membrane-binding.
 REGION 267 442 Mediates interaction with the adaptor
 REGION 609 889 Mediates interaction with AGFG1, CALM,
 MOD_RES 182 182 Phosphotyrosine (By similarity).
 MOD_RES 184 184 Phosphoserine (By similarity).
 MOD_RES 616 616 Phosphoserine.  
Keyword
 Alternative splicing; Coated pit; Coiled coil; Complete proteome; Endocytosis; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 889 AA 
Protein Sequence
MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA MAKLSKLASN 60
GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL RYGEEQLKTH KKCKEEVVST 120
LDAVQVLSGV SQLLPKSREN YLNRCMDQER LRRESTSQKE MDKAETKTKK AAESLRRSVE 180
KYNSARADFE QKMLDSALRF QAMEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI 240
ENVSVEMLLR KFAESKGTGR EKPGPLDFEA YSAAALQEAM KRLRGAKAFR LPGLSRRERE 300
PEPPAAVDFL EPDSGTCPEV DEEGFTVRPD VTQNSTAEPS RFSSSDSDFD DEEPRKFYVH 360
IKPAPARAPA CSPEAAAAQL RATAGSLILP PGPGGTMKRH SSRDAAGKPQ RPRSAPRTSS 420
CAERLQSEEQ VSKNLFGPPL ESAFDHEDFT GSSSLGFTSS PSPFSSSSPE NVEDSGLDSP 480
SHAAPGPSPD SWVPRPGTPQ SPPSCRAPPP EARGIRAPPL PDSPQPLASS PGPWGLEALA 540
GGDLMPAPAD PTAREGLAAP PRRLRSRKVS CPLTRSNGDL SRSLSPSPLG SSAASTALER 600
PSFLSQTGHG VSRGPSPVVL GSQDALPIAT AFTEYVHAYF RGHSPSCLAR VTGELTMTFP 660
AGIVRVFSGT PPPPVLSFRL VHTTAIEHFQ PNADLLFSDP SQSDPETKDF WLNMAALTEA 720
LQRQAEQNPT ASYYNVVLLR YQFSRPGPQS VPLQLSAHWQ CGATLTQVSV EYGYRPGATA 780
VPTPLTNVQI LLPVGEPVTN VRLQPAATWN LEEKRLTWRL PDVSEAGGSG RLSASWEPLS 840
GPSTPSPVAA QFTSEGTTLS GVDLELVGSG YRMSLVKRRF ATGMYLVSC 889 
Gene Ontology
 GO:0005905; C:coated pit; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0035612; F:AP-2 adaptor complex binding; IDA:MGI.
 GO:0048268; P:clathrin coat assembly; IMP:UniProtKB.
 GO:0072583; P:clathrin-mediated endocytosis; IMP:UniProtKB. 
Interpro
 IPR001060; FCH_dom.
 IPR018808; Muniscin_C-term_mu_dom. 
Pfam
 PF00611; FCH
 PF10291; muHD 
SMART
 SM00055; FCH 
PROSITE
 PS50133; FCH
 PS51072; MHD 
PRINTS