CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001180
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pre-mRNA-processing factor 40 homolog A 
Protein Synonyms/Alias
 Fas ligand-associated factor 1; Formin-binding protein 11; Formin-binding protein 3; Huntingtin yeast partner A; Huntingtin-interacting protein 10; HIP-10; Huntingtin-interacting protein A; Renal carcinoma antigen NY-REN-6 
Gene Name
 PRPF40A 
Gene Synonyms/Alias
 FBP11; FLAF1; FNBP3; HIP10; HYPA; HSPC225 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
169EYKSDSGKPYYYNSQubiquitination[1]
393ASWEQAMKMIINDPRubiquitination[1]
691TLDAGNIKLAFNSLLubiquitination[2]
700AFNSLLEKAEAREREubiquitination[2]
749DIRERFVKEPAFEDIubiquitination[1]
917LSEGELEKRRRTLLEubiquitination[1]
Reference
 [1] 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]
 [2] 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
 Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. 
Sequence Annotation
 DOMAIN 140 173 WW 1.
 DOMAIN 181 214 WW 2.
 DOMAIN 393 447 FF 1.
 DOMAIN 460 514 FF 2.
 DOMAIN 527 587 FF 3.
 DOMAIN 607 667 FF 4.
 DOMAIN 672 727 FF 5.
 DOMAIN 742 799 FF 6.
 MOD_RES 36 36 Phosphoserine (By similarity).
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 196 196 N6-acetyllysine.
 MOD_RES 373 373 Phosphothreonine.
 MOD_RES 828 828 Phosphoserine (By similarity).
 MOD_RES 830 830 Phosphoserine (By similarity).
 MOD_RES 832 832 Phosphoserine (By similarity).
 MOD_RES 834 834 Phosphoserine (By similarity).
 MOD_RES 883 883 Phosphoserine.
 MOD_RES 885 885 Phosphoserine.
 MOD_RES 888 888 Phosphoserine.
 MOD_RES 932 932 Phosphothreonine.
 MOD_RES 933 933 Phosphoserine.
 MOD_RES 935 935 Phosphoserine.
 MOD_RES 938 938 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 957 AA 
Protein Sequence
MCSGSGRRRS SLSPTMRPGT GAERGGLMMG HPGMHYAPMG MHPMGQRANM PPVPHGMMPQ 60
MMPPMGGPPM GQMPGMMSSV MPGMMMSHMS QASMQPALPP GVNSMDVAAG TASGAKSMWT 120
EHKSPDGRTY YYNTETKQST WEKPDDLKTP AEQLLSKCPW KEYKSDSGKP YYYNSQTKES 180
RWAKPKELED LEGYQNTIVA GSLITKSNLH AMIKAEESSK QEECTTTSTA PVPTTEIPTT 240
MSTMAAAEAA AAVVAAAAAA AAAAAAANAN ASTSASNTVS GTVPVVPEPE VTSIVATVVD 300
NENTVTISTE EQAQLTSTPA IQDQSVEVSS NTGEETSKQE TVADFTPKKE EEESQPAKKT 360
YTWNTKEEAK QAFKELLKEK RVPSNASWEQ AMKMIINDPR YSALAKLSEK KQAFNAYKVQ 420
TEKEEKEEAR SKYKEAKESF QRFLENHEKM TSTTRYKKAE QMFGEMEVWN AISERDRLEI 480
YEDVLFFLSK KEKEQAKQLR KRNWEALKNI LDNMANVTYS TTWSEAQQYL MDNPTFAEDE 540
ELQNMDKEDA LICFEEHIRA LEKEEEEEKQ KSLLRERRRQ RKNRESFQIF LDELHEHGQL 600
HSMSSWMELY PTISSDIRFT NMLGQPGSTA LDLFKFYVED LKARYHDEKK IIKDILKDKG 660
FVVEVNTTFE DFVAIISSTK RSTTLDAGNI KLAFNSLLEK AEAREREREK EEARKMKRKE 720
SAFKSMLKQA APPIELDAVW EDIRERFVKE PAFEDITLES ERKRIFKDFM HVLEHECQHH 780
HSKNKKHSKK SKKHHRKRSR SRSGSDSDDD DSHSKKKRQR SESRSASEHS SSAESERSYK 840
KSKKHKKKSK KRRHKSDSPE SDAEREKDKK EKDRESEKDR TRQRSESKHK SPKKKTGKDS 900
GNWDTSGSEL SEGELEKRRR TLLEQLDDDQ 930 
Gene Ontology
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
Interpro
 IPR002713; FF_domain.
 IPR001202; WW_dom. 
Pfam
 PF01846; FF
 PF00397; WW 
SMART
 SM00441; FF
 SM00456; WW 
PROSITE
 PS51676; FF
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS