CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Filamin A-interacting protein 1-like 
Protein Synonyms/Alias
 130 kDa GPBP-interacting protein; 90 kDa GPBP-interacting protein; Protein down-regulated in ovarian cancer 1; DOC-1 
Gene Name
 FILIP1L 
Gene Synonyms/Alias
 COL4A3BPIP; DOC1; GIP90 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
385RVLDMEGKDEELIKMacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor- associated vasculature. 
Sequence Annotation
 MOD_RES 791 791 Phosphoserine (By similarity).
 MOD_RES 1049 1049 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1135 AA 
Protein Sequence
MRSRGSDTEG SAQKKFPRHT KGHSFQGPKN MKHRQQDKDS PSESDVILPC PKAEKPHSGN 60
GHQAEDLSRD DLLFLLSILE GELQARDEVI GILKAEKMDL ALLEAQYGFV TPKKVLEALQ 120
RDAFQAKSTP WQEDIYEKPM NELDKVVEKH KESYRRILGQ LLVAEKSRRQ TILELEEEKR 180
KHKEYMEKSD EFICLLEQEC ERLKKLIDQE IKSQEEKEQE KEKRVTTLKE ELTKLKSFAL 240
MVVDEQQRLT AQLTLQRQKI QELTTNAKET HTKLALAEAR VQEEEQKATR LEKELQTQTT 300
KFHQDQDTIM AKLTNEDSQN RQLQQKLAAL SRQIDELEET NRSLRKAEEE LQDIKEKISK 360
GEYGNAGIMA EVEELRKRVL DMEGKDEELI KMEEQCRDLN KRLERETLQS KDFKLEVEKL 420
SKRIMALEKL EDAFNKSKQE CYSLKCNLEK ERMTTKQLSQ ELESLKVRIK ELEAIESRLE 480
KTEFTLKEDL TKLKTLTVMF VDERKTMSEK LKKTEDKLQA ASSQLQVEQN KVTTVTEKLI 540
EETKRALKSK TDVEEKMYSV TKERDDLKNK LKAEEEKGND LLSRVNMLKN RLQSLEAIEK 600
DFLKNKLNQD SGKSTTALHQ ENNKIKELSQ EVERLKLKLK DMKAIEDDLM KTEDEYETLE 660
RRYANERDKA QFLSKELEHV KMELAKYKLA EKTETSHEQW LFKRLQEEEA KSGHLSREVD 720
ALKEKIHEYM ATEDLICHLQ GDHSVLQKKL NQQENRNRDL GREIENLTKE LERYRHFSKS 780
LRPSLNGRRI SDPQVFSKEV QTEAVDNEPP DYKSLIPLER AVINGQLYEE SENQDEDPND 840
EGSVLSFKCS QSTPCPVNRK LWIPWMKSKE GHLQNGKMQT KPNANFVQPG DLVLSHTPGQ 900
PLHIKVTPDH VQNTATLEIT SPTTESPHSY TSTAVIPNCG TPKQRITILQ NASITPVKSK 960
TSTEDLMNLE QGMSPITMAT FARAQTPESC GSLTPERTMS PIQVLAVTGS ASSPEQGRSP 1020
EPTEISAKHA IFRVSPDRQS SWQFQRSNSN SSSVITTEDN KIHIHLGSPY MQAVASPVRP 1080
ASPSAPLQDN RTQGLINGAL NKTTNKVTSS ITITPTATPL PRQSQITVEP LLLPH 1135 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0016459; C:myosin complex; NAS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 
Interpro
 IPR019131; Cortactin-binding_p2_N. 
Pfam
 PF09727; CortBP2 
SMART
  
PROSITE
  
PRINTS