CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019037
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fermitin family homolog 2 
Protein Synonyms/Alias
 Kindlin-2; Mitogen-inducible gene 2 protein; MIG-2; Pleckstrin homology domain-containing family C member 1; PH domain-containing family C member 1 
Gene Name
 FERMT2 
Gene Synonyms/Alias
 KIND2; MIG2; PLEKHC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107RLQLPNMKYVKVKVNubiquitination[1]
285SFFDLNPKYDAIRINubiquitination[1, 2]
582ARFQGGKKEELIGIAubiquitination[1]
605ASTGDAIKTWRFSNMubiquitination[3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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] 
Functional Description
 Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF4 and in Wnt signaling. 
Sequence Annotation
 DOMAIN 189 661 FERM.
 DOMAIN 380 476 PH.
 REGION 40 81 Interaction with membranes containing
 BINDING 383 383 Phosphatidylinositol phosphate.
 MOD_RES 159 159 Phosphoserine.
 MOD_RES 181 181 Phosphoserine.
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 351 351 Phosphoserine.
 MOD_RES 666 666 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Cell projection; Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 680 AA 
Protein Sequence
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE KLDVKKDWSD 60
HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR LQLPNMKYVK VKVNFSDRVF 120
KAVSDICKTF NIRHPEELSL LKKPRDPTKK KKKKLDDQSE DEALELEGPL ITPGSGSIYS 180
SPGLYSKTMT PTYDAHDGSP LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ 240
ALLDKAKINQ GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW 300
AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL SDLEITLEGG 360
KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK DTSISCYKSK EESSGTPAHQ 420
MNLRGCEVTP DVNISGQKFN IKLLIPVAEG MNEIWLRCDN EKQYAHWMAA CRLASKGKTM 480
ADSSYNLEVQ NILSFLKMQH LNPDPQLIPE QITTDITPEC LVSPRYLKKY KNKQITARIL 540
EAHQNVAQMS LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST 600
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI GGYIFLSTRA 660
KDQNESLDEE MFYKLTSGWV 680 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031234; C:extrinsic to internal side of plasma membrane; IDA:UniProtKB.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0031674; C:I band; IEA:UniProtKB-SubCell.
 GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0001725; C:stress fiber; IEA:Compara.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
 GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
 GO:0033622; P:integrin activation; IMP:UniProtKB.
 GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
 GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
 GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
 GO:0016055; P:Wnt receptor signaling pathway; IMP:UniProtKB. 
Interpro
 IPR019749; Band_41_domain.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR018979; FERM_N.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF00373; FERM_M
 PF09379; FERM_N
 PF00169; PH 
SMART
 SM00295; B41
 SM00233; PH 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3
 PS50003; PH_DOMAIN 
PRINTS