CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011688
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inverted formin-2 
Protein Synonyms/Alias
  
Gene Name
 Inf2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
706KFDVEVLKQLLKLLPubiquitination[1]
896ASIPEVQKQYAERLQubiquitination[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
 Severs actin filaments and accelerates their polymerization and depolymerization. 
Sequence Annotation
 DOMAIN 1 330 GBD/FH3.
 DOMAIN 421 564 FH1.
 DOMAIN 589 979 FH2.
 DOMAIN 1007 1022 WH2.
 MOD_RES 909 909 Phosphoserine.
 MOD_RES 1172 1172 Phosphoserine (By similarity).
 MOD_RES 1174 1174 Phosphoserine (By similarity).
 MOD_RES 1203 1203 Phosphothreonine (By similarity).
 MOD_RES 1216 1216 Phosphoserine.
 MOD_RES 1230 1230 Phosphothreonine (By similarity).  
Keyword
 Actin-binding; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1273 AA 
Protein Sequence
MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY SGLRKRLESS 60
DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CISCVRAVMN SQQGIEYILS 120
NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL TLDALDHYKM VCSQQYRFSV 180
IMSELSDSDN VPYVVTLLSV INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD 240
LLIQLEAFEE AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH 300
LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP SPLDKAHKSV 360
QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ SSSVDIAPQP VALEQCITAL 420
PLPTPPLSSS TPVLPPTPPP LPGPGATSPL PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP 480
PPLPGSGTIS PPPPPPPPPL PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP 540
PPPPLPRAGQ IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK 600
KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE PSAAPARKEP 660
KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF DVEVLKQLLK LLPEKHEIEN 720
LRAFTEERAK LSNADQFYVL LLDIPCYPLR VECMMLCEGT AIVLDMVRPK AQLVLTACES 780
LLTSQRLPVF CQLILKIGNF LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE 840
VEKSHPDLLQ LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE 900
RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR DLFTRALKEN 960
KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ EEVCVIDALL ADIRKGFQLR 1020
KTARGRGDTE ASGRVAPTDP PKATEPATAS NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA 1080
VTPSPQPSKE EDGPPALERR SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE 1140
FSSNKPPGVK SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG 1200
EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP SRNQEEFVPD 1260
SDDIKAKRLC VIQ 1273 
Gene Ontology
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0032535; P:regulation of cellular component size; IMP:MGI. 
Interpro
 IPR003104; Actin-bd_FH2/DRF_autoreg.
 IPR016024; ARM-type_fold.
 IPR010472; Drf_FH3.
 IPR010473; Drf_GTPase-bd.
 IPR015425; FH2_actin-bd.
 IPR014768; GTPase-bd/formin_homology_3.
 IPR003124; WH2_dom. 
Pfam
 PF06367; Drf_FH3
 PF06371; Drf_GBD
 PF02181; FH2
 PF02205; WH2 
SMART
 SM00498; FH2
 SM00246; WH2 
PROSITE
 PS51444; FH2
 PS51232; GBD_FH3
 PS51082; WH2 
PRINTS