| Tag | Content |
|---|
| CPLM ID | CPLM-023838 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | FERM, RhoGEF and pleckstrin domain-containing protein 1 |
Protein Synonyms/Alias | Chondrocyte-derived ezrin-like protein; Pleckstrin homology domain-containing family C member 2; PH domain-containing family C member 2 |
Gene Name | FARP1 |
Gene Synonyms/Alias | CDEP; PLEKHC2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 456 | EEEEEVVKDRTQQSK | ubiquitination | [1] | | 572 | WFQSTVSKEDAMPEA | ubiquitination | [1] | | 1071 | RPHVLSHKESLVY** | ubiquitination | [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] |
Functional Description | Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). |
Sequence Annotation | DOMAIN 40 320 FERM.
DOMAIN 540 730 DH.
DOMAIN 759 856 PH 1.
DOMAIN 932 1029 PH 2.
MOD_RES 24 24 Phosphothreonine.
MOD_RES 340 340 Phosphoserine.
MOD_RES 427 427 Phosphoserine.
MOD_RES 510 510 Phosphoserine.
MOD_RES 514 514 Phosphoserine.
MOD_RES 872 872 Phosphoserine.
MOD_RES 889 889 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Developmental protein; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Synapse; Synaptosome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1045 AA |
Protein Sequence | MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA 60
PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF 120
PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL 180
AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI 240
NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD 300
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ 360
FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG 420
EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL 480
SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK 540
AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK 600
EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR 660
LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI 720
TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGRPG SFSLMRTPHL GQARRIPCAP 780
ERRPLLLVKE FIRLGSLSKL SGKGLQQRMF FLFNDVLLYT SRGLTASNQF KVHGQLPLYG 840
MTIEESEDEW GVPHCLTLRG QRQSIIVAAS SRSEMEKWVE DIQMAIDLAE KSSSPAPEFL 900
ASSPPDNKSP DEATAADQES EDDLSASRTS LERQAPHRGN TMVHVCWHRN TSVSMVDFSI 960
AVENQLSGNL LRKFKNSNGW QKLWVVFTNF CLFFYKSHQD NHPLASLPLL GYSLTIPSES 1020
ENIQKDYVFK LHFKSHVYYF RAESEYTFER WMEVIRSATS SASRPHVLSH KESLVY 1076 |
Gene Ontology | GO:0030054; C:cell junction; IEA:UniProtKB-KW. GO:0005856; C:cytoskeleton; TAS:ProtInc. GO:0005829; C:cytosol; ISS:UniProtKB. GO:0030425; C:dendrite; ISS:UniProtKB. GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. GO:0031234; C:extrinsic to internal side of plasma membrane; ISS:UniProtKB. GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. GO:0045202; C:synapse; IEA:UniProtKB-SubCell. GO:0005543; F:phospholipid binding; IEA:InterPro. GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB. GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB. GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB. GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. GO:0007416; P:synapse assembly; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |