Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Filamin-A  

UniProtKB / Swiss-Prot ID :  FLNA_HUMAN

Gene Name (Synonyms) : 
FLNA, FLN, FLN1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. 

Protein Function :  Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface- localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. 

Protein Sequence MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTD...
Predicted Secondary Structure CCHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCHHCCCHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHH...
Protein Variant
LocationDescription
39A -> G (in PVNH4). VAR_022734
82E -> V (in PVNH1; dbSNP:rs28935169). VAR_015699
102M -> V (in PVNH1). VAR_031305
128A -> V (in PVNH4). VAR_031306
149S -> F (in PVNH1). VAR_031307
170Q -> P (in OPD2). VAR_015713
172L -> F (in OPD1). VAR_015714
196R -> G (in OPD2). VAR_015715
196R -> W (in OPD1). VAR_015716
200A -> S (in OPD2). VAR_015717
203D -> Y (in OPD1). VAR_031308
207P -> L (in OPD1; dbSNP:rs28935469). VAR_015700
210C -> F (in OPD2). VAR_058720
254E -> K (in OPD2; dbSNP:rs28935470). VAR_015701
273A -> P (in OPD2). VAR_015718
288G -> R (in CVDX). VAR_064156
320V -> A (in dbSNP:rs1064816). VAR_012831
370F -> L (in dbSNP:rs1064817). VAR_012832
528V -> M (in PVNH1). VAR_031309
552V -> A (in dbSNP:rs730319). VAR_012833
555T -> K (in OPD2). VAR_015719
637P -> Q (in CVDX). VAR_064157
656L -> F (in PVNH1). VAR_012834
711V -> D (in CVDX). VAR_064158
1012S -> L (in dbSNP:rs17091204). VAR_031310
1159D -> A (in FMD; does not inhibitinteraction with MIS18BP1;
1184D -> E (in MNS). VAR_015720
1186S -> L (in FMD). VAR_015721
1188A -> T (in MNS; does not inhibitinteraction with MIS18BP1;
1199S -> L (in MNS; does not inhibitinteraction with MIS18BP1;
1291P -> L (in FGS2). VAR_058721
1419A -> G (in dbSNP:rs35504556). VAR_032083
1620Missing (in FMD). VAR_015722
1635Missing (in otopalatodigital spectrumdisorder).
1645C -> F (in OPD2). VAR_015723
1724Missing (in TOD). VAR_064159
1728G -> C (in FMD). VAR_031312
1764A -> T (in PVNH1; dbSNP:rs57108893). VAR_012835
1803E -> K (probable disease-associatedmutation found in a patient with
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine---MSSSHS
---CCHHHH
52.42HPRD
Link-
2N-acetylserine.---MSSSHS
---CCHHHH
52.42UniProtKB
Link-
2Phosphoserine---MSSSHS
---CCHHHH
52.42HPRD
Link-
2Phosphoserine---MSSSHS
---CCHHHH
52.42Phosphositeplus
Link-
3Phosphoserine--MSSSHSR
--CCHHHHH
43.88HPRD
Link-
3Phosphoserine--MSSSHSR
--CCHHHHH
43.88Phosphositeplus
Link-
4Phosphoserine-MSSSHSRA
-CCHHHHHH
34.47HPRD
Link-
4Phosphoserine-MSSSHSRA
-CCHHHHHH
34.47Phosphositeplus
Link-
6PhosphoserineSSSHSRAGQ
CHHHHHHCC
26.27HPRD
Link-
6PhosphoserineSSSHSRAGQ
CHHHHHHCC
26.27Phosphositeplus
Link-
11PhosphoserineRAGQSAAGA
HHCCCCCCC
21.11HPRD
Link-
11PhosphoserineRAGQSAAGA
HHCCCCCCC
21.11Phosphositeplus
Link-
23PhosphothreonineGGVDTRDAE
CCCCCCCCC
28.21HPRD
Link-
23PhosphothreonineGGVDTRDAE
CCCCCCCCC
28.21Phosphositeplus
Link-
31PhosphothreonineEMPATEKDL
CCCCCCCCH
37.38HPRD
Link-
31PhosphothreonineEMPATEKDL
CCCCCCCCH
37.38Phosphositeplus
Link-
69PhosphothreonineANLQTDLSD
HHHHHHHHH
41.91Phosphositeplus
Link-
72PhosphoserineQTDLSDGLR
HHHHHHHHH
32.23Phosphositeplus
Link-
299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GNMVKKRAE
CCEECCCCE
26.27Phosphositeplus
Link-
299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GNMVKKRAE
CCEECCCCE
26.27Phosphositeplus
Link-
367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QHIAKSPFE
EECCCCCEE
59.04Phosphositeplus
Link-
373PhosphotyrosinePFEVYVDKS
CEEEEECCC
8.85HPRD
Link-
373PhosphotyrosinePFEVYVDKS
CEEEEECCC
8.85PhosphoELM
Link-
373PhosphotyrosinePFEVYVDKS
CEEEEECCC
8.85Phosphositeplus
Link-
373Phosphotyrosine.PFEVYVDKS
CEEEEECCC
8.85UniProtKB
Link-
444S-nitrosocysteineSTYRCSYQP
CEEEEEEEE
2.90dbSNO
Link-
504Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TADFKVYTK
EEEEEEEEE
34.57Phosphositeplus
Link-
504N6-acetyllysineTADFKVYTK
EEEEEEEEE
34.57HPRD
Link-
504N6-acetyllysineTADFKVYTK
EEEEEEEEE
34.57Phosphositeplus
Link-
504N6-acetyllysine.TADFKVYTK
EEEEEEEEE
34.57UniProtKB
Link-
506PhosphotyrosineDFKVYTKGA
EEEEEEEEC
11.88Phosphositeplus
Link-
508N6-acetyllysineKVYTKGAGS
EEEEEECCC
29.13HPRD
Link-
508N6-acetyllysineKVYTKGAGS
EEEEEECCC
29.13Phosphositeplus
Link-
508N6-acetyllysine.KVYTKGAGS
EEEEEECCC
29.13UniProtKB
Link-
564PhosphoserineNIGRSPFEV
CCCCCCEEE
28.82HPRD
Link-
700N6-acetyllysineTVDAKHGGK
EEEECCCCC
38.02HPRD
Link-
700N6-acetyllysineTVDAKHGGK
EEEECCCCC
38.02Phosphositeplus
Link-
700N6-acetyllysine.TVDAKHGGK
EEEECCCCC
38.02UniProtKB
Link-
717S-nitrosocysteineDNEGCPVEA
CCCCCEEEE
2.52dbSNO
Link-
717S-nitrosocysteineDNEGCPVEA
CCCCCEEEE
2.52HPRD
Link-
731PhosphotyrosineGNGTYSCSY
CCCEEEEEE
14.74Phosphositeplus
Link-
757PhosphoserineSIPNSPFRV
CCCCCCEEE
21.77HPRD
Link-
757PhosphoserineSIPNSPFRV
CCCCCCEEE
21.77Phosphositeplus
Link-
781N6-acetyllysinePGVAKTGLK
CCEEEECCE
40.49HPRD
Link-
781N6-acetyllysinePGVAKTGLK
CCEEEECCE
40.49Phosphositeplus
Link-
781N6-acetyllysine.PGVAKTGLK
CCEEEECCE
40.49UniProtKB
Link-
791PhosphotyrosineHEPTYFTVD
ECCEEEEEE
14.15Phosphositeplus
Link-
810S-nitrosocysteineIGIKCAPGV
CCCEEEEEE
5.37dbSNO
Link-
837Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TFTVKYTPR
CEEEEEEEC
40.11Phosphositeplus
Link-
837N6-acetyllysineTFTVKYTPR
CEEEEEEEC
40.11HPRD
Link-
837N6-acetyllysineTFTVKYTPR
CEEEEEEEC
40.11Phosphositeplus
Link-
837N6-acetyllysine.TFTVKYTPR
CEEEEEEEC
40.11UniProtKB
Link-
891N6-acetyllysineVELGKPTHF
HHCCCCEEE
60.41HPRD
Link-
891N6-acetyllysineVELGKPTHF
HHCCCCEEE
60.41Phosphositeplus
Link-
891N6-acetyllysine.VELGKPTHF
HHCCCCEEE
60.41UniProtKB
Link-
906Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AGKGKLDVQ
CCCCCEEEE
45.03Phosphositeplus
Link-
912PhosphoserineDVQFSGLTK
EEEEEEECC
18.79Phosphositeplus
Link-
915PhosphothreonineFSGLTKGDA
EEEECCCCC
36.18Phosphositeplus
Link-
916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGLTKGDAV
EEECCCCCE
60.89Phosphositeplus
Link-
966PhosphoserineSVAVSPSLD
EEEEECCCC
10.07HPRD
Link-
966PhosphoserineSVAVSPSLD
EEEEECCCC
10.07Phosphositeplus
Link-
973N6-acetyllysineLDLSKIKVS
CCCCCCEEE
54.57HPRD
Link-
973N6-acetyllysineLDLSKIKVS
CCCCCCEEE
54.57Phosphositeplus
Link-
994N6-acetyllysineEFTVKSKGA
EEEECCCCC
43.31HPRD
Link-
994N6-acetyllysineEFTVKSKGA
EEEECCCCC
43.31Phosphositeplus
Link-
994N6-acetyllysine.EFTVKSKGA
EEEECCCCC
43.31UniProtKB
Link-
1019Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AVPCKVEPG
EEEEEEECC
43.49Phosphositeplus
Link-
1047PhosphotyrosineVEVTYDGVP
EEEEECCEE
18.84HPRD
Link-
1047PhosphotyrosineVEVTYDGVP
EEEEECCEE
18.84PhosphoELM
Link-
1047PhosphotyrosineVEVTYDGVP
EEEEECCEE
18.84Phosphositeplus
Link-
1047Phosphotyrosine.VEVTYDGVP
EEEEECCEE
18.84UniProtKB
Link-
1048Caspase cleavage aspartic acidEVTYDGVPV
EEEECCEEE
42.10Phosphositeplus
Link-
1081PhosphoserineLQGGSAGSP
CHHCCCCCE
35.96HPRD
Link-
1081PhosphoserineLQGGSAGSP
CHHCCCCCE
35.96PhosphoELM
Link-
1081PhosphoserineLQGGSAGSP
CHHCCCCCE
35.96Phosphositeplus
Link-
1081PhosphoserineLQGGSAGSP
CHHCCCCCE
35.96SysPTM
Link-
1081Phosphoserine.LQGGSAGSP
CHHCCCCCE
35.96UniProtKB
Link-
1084PhosphoserineGSAGSPARF
CCCCCEEEE
18.33HPRD
Link-
1084PhosphoserineGSAGSPARF
CCCCCEEEE
18.33PhosphoELM
Link-
1084PhosphoserineGSAGSPARF
CCCCCEEEE
18.33Phosphositeplus
Link-
1084PhosphoserineGSAGSPARF
CCCCCEEEE
18.33SysPTM
Link-
1084Phosphoserine.GSAGSPARF
CCCCCEEEE
18.33UniProtKB
Link-
1089PhosphothreoninePARFTIDTK
EEEEEEEEE
16.64HPRD
Link-
1089Phosphothreonine.PARFTIDTK
EEEEEEEEE
16.64UniProtKB
Link-
1260S-nitrosocysteineSGVQCYGPG
CCEEEEECC
3.84dbSNO
Link-
1261PhosphotyrosineGVQCYGPGI
CEEEEECCC
14.84Phosphositeplus
Link-
1288PhosphothreonineALTQTGGPH
EEEECCCCE
38.58HPRD
Link-
1308PhosphotyrosineLTETYVQDR
EEEEEEEEC
7.00Phosphositeplus
Link-
1334PhosphothreonineSVDVTYDGS
EEEEEECCE
16.07HPRD
Link-
1334PhosphothreonineSVDVTYDGS
EEEEEECCE
16.07PhosphoELM
Link-
1334PhosphothreonineSVDVTYDGS
EEEEEECCE
16.07Phosphositeplus
Link-
1336Caspase cleavage aspartic acidDVTYDGSPV
EEEECCEEC
41.55Phosphositeplus
Link-
1338PhosphoserineTYDGSPVPS
EECCEECCC
21.59HPRD
Link-
1338PhosphoserineTYDGSPVPS
EECCEECCC
21.59PhosphoELM
Link-
1338PhosphoserineTYDGSPVPS
EECCEECCC
21.59Phosphositeplus
Link-
1338PhosphoserineTYDGSPVPS
EECCEECCC
21.59SysPTM
Link-
1338Phosphoserine.TYDGSPVPS
EECCEECCC
21.59UniProtKB
Link-
1343PhosphoserinePVPSSPFQV
ECCCCCEEE
24.54HPRD
Link-
1343PhosphoserinePVPSSPFQV
ECCCCCEEE
24.54PhosphoELM
Link-
1436PhosphoserineQVPGSPFKV
CCCCCEEEE
22.54HPRD
Link-
1436PhosphoserineQVPGSPFKV
CCCCCEEEE
22.54Phosphositeplus
Link-
1459PhosphoserineGPGLSPGMV
CCCCCEEEE
25.89HPRD
Link-
1459PhosphoserineGPGLSPGMV
CCCCCEEEE
25.89PhosphoELM
Link-
1459PhosphoserineGPGLSPGMV
CCCCCEEEE
25.89Phosphositeplus
Link-
1459PhosphoserineGPGLSPGMV
CCCCCEEEE
25.89SysPTM
Link-
1459Phosphoserine.GPGLSPGMV
CCCCCEEEE
25.89UniProtKB
Link-
1491Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VQGPKGLVE
EECCCCCCC
72.24Phosphositeplus
Link-
1504Caspase cleavage aspartic acidVDNADGTQT
EECCCCEEE
67.91Phosphositeplus
Link-
1504noneVDNADGTQT
EECCCCEEE
67.91HPRD
Link-
1525PhosphotyrosineISVLYGDEE
EEEEECCCC
22.00HPRD
Link-
1525PhosphotyrosineISVLYGDEE
EEEEECCCC
22.00SysPTM
Link-
1533PhosphoserineEVPRSPFKV
CCCCCCCEE
28.72HPRD
Link-
1533PhosphoserineEVPRSPFKV
CCCCCCCEE
28.72PhosphoELM
Link-
1533PhosphoserineEVPRSPFKV
CCCCCCCEE
28.72Phosphositeplus
Link-
1533PhosphoserineEVPRSPFKV
CCCCCCCEE
28.72SysPTM
Link-
1533Phosphoserine.EVPRSPFKV
CCCCCCCEE
28.72UniProtKB
Link-
1538N6-acetyllysinePFKVKVLPT
CCEEEEECC
38.35HPRD
Link-
1538N6-acetyllysinePFKVKVLPT
CCEEEEECC
38.35Phosphositeplus
Link-
1538N6-acetyllysine.PFKVKVLPT
CCEEEEECC
38.35UniProtKB
Link-
1604PhosphotyrosineHDGTYTVAY
CCCEEEEEE
12.54HPRD
Link-
1604PhosphotyrosineHDGTYTVAY
CCCEEEEEE
12.54PhosphoELM
Link-
1604PhosphotyrosineHDGTYTVAY
CCCEEEEEE
12.54Phosphositeplus
Link-
1604Phosphotyrosine.HDGTYTVAY
CCCEEEEEE
12.54UniProtKB
Link-
1630PhosphoserineEIPFSPYRV
CCCCCCEEE
18.70HPRD
Link-
1630PhosphoserineEIPFSPYRV
CCCCCCEEE
18.70PhosphoELM
Link-
1630PhosphoserineEIPFSPYRV
CCCCCCEEE
18.70Phosphositeplus
Link-
1630PhosphoserineEIPFSPYRV
CCCCCCEEE
18.70SysPTM
Link-
1630Phosphoserine.EIPFSPYRV
CCCCCCEEE
18.70UniProtKB
Link-
1734PhosphoserineHVPNSPFQV
ECCCCCEEE
22.48Phosphositeplus
Link-
1801Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FTIKKGEIT
CCCCCCEEE
58.90Phosphositeplus
Link-
1824Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITDNKDGTV
CCCCCCCEE
61.41Phosphositeplus
Link-
1932PhosphotyrosineLPGDYSILV
CCCCEEEEE
11.97Phosphositeplus
Link
1946PhosphoserineHVPGSPFTA
ECCCCCEEE
15.69Phosphositeplus
Link
1964Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MSHLKVGSA
HCEEECCCC
38.84Phosphositeplus
Link-
2032PhosphoserineQHVASSPIP
EECCCCCEE
35.24SysPTM
Link-
2033PhosphoserineHVASSPIPV
ECCCCCEEE
19.67SysPTM
Link-
2053PhosphoserineRVRVSGQGL
EEEEECCCH
18.16PhosphoELM
Link-
2053PhosphoserineRVRVSGQGL
EEEEECCCH
18.16Phosphositeplus
Link-
2053PhosphoserineRVRVSGQGL
EEEEECCCH
18.16SysPTM
Link-
2053Phosphoserine.RVRVSGQGL
EEEEECCCH
18.16UniProtKB
Link-
2128PhosphoserineHVPGSPFSV
ECCCCCEEE
19.39PhosphoELM
Link-
2128PhosphoserineHVPGSPFSV
ECCCCCEEE
19.39Phosphositeplus
Link-
2152PhosphoserineRRAPSVANV
CCCCEEEEC
32.64Phosphositeplus
Link-
2152PhosphoserineRRAPSVANV
CCCCEEEEC
32.64SysPTM
Link-
2152PhosphoserineRRAPSVANV
CCCCEEEEC
32.64SysPTM
Link-
2152Phosphoserine (RSK_group;PAK1)RRAPSVANV
CCCCEEEEC
32.64PhosphoELM
Link-
2152Phosphoserine.RRAPSVANV
CCCCEEEEC
32.64UniProtKB
Link-
2158PhosphoserineANVGSHCDL
EECCCCCCC
19.36PhosphoELM
Link-
2158PhosphoserineANVGSHCDL
EECCCCCCC
19.36Phosphositeplus
Link-
2158PhosphoserineANVGSHCDL
EECCCCCCC
19.36SysPTM
Link-
2158PhosphoserineANVGSHCDL
EECCCCCCC
19.36SysPTM
Link-
2158Phosphoserine.ANVGSHCDL
EECCCCCCC
19.36UniProtKB
Link-
2163PhosphoserineHCDLSLKIP
CCCCCEEEE
17.86SysPTM
Link-
2180PhosphoserineAQVTSPSGK
EEEECCCCC
20.43Phosphositeplus
Link-
2198PhosphotyrosineENHTYCIRF
CCCEEEEEE
4.37Phosphositeplus
Link-
2217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVKYKGQHV
EEEECCEEC
46.51Phosphositeplus
Link-
2284PhosphoserineKAEISFEDR
CCCCEEEEC
17.68Phosphositeplus
Link-
2284Phosphoserine.KAEISFEDR
CCCCEEEEC
17.68UniProtKB
Link-
2292PhosphoserineRKDGSCGVA
CCCCEEEEE
20.17Phosphositeplus
Link-
2305PhosphotyrosineEPGDYEVSV
CCCCEEEEE
24.93Phosphositeplus
Link-
2319PhosphoserineHIPDSPFVV
CCCCCCEEE
18.19HPRD
Link-
2319PhosphoserineHIPDSPFVV
CCCCCCEEE
18.19SysPTM
Link-
2327PhosphoserineVPVASPSGD
EEEECCCCC
21.60PhosphoELM
Link-
2327PhosphoserineVPVASPSGD
EEEECCCCC
21.60Phosphositeplus
Link-
2327Phosphoserine.VPVASPSGD
EEEECCCCC
21.60UniProtKB
Link-
2336PhosphothreonineARRLTVSSL
EEEEEECCC
19.27Phosphositeplus
Link-
2370PhosphoserineAKVHSPSGA
EEEECCCCC
24.61Phosphositeplus
Link-
2388PhosphotyrosineDQDKYAVRF
CCCCEEEEE
20.72PhosphoELM
Link-
2388PhosphotyrosineDQDKYAVRF
CCCCEEEEE
20.72Phosphositeplus
Link-
2388Phosphotyrosine.DQDKYAVRF
CCCCEEEEE
20.72UniProtKB
Link-
2414PhosphoserineHIPGSPFKI
ECCCCCCEE
23.08PhosphoELM
Link-
2414PhosphoserineHIPGSPFKI
ECCCCCCEE
23.08Phosphositeplus
Link-
2414PhosphoserineHIPGSPFKI
ECCCCCCEE
23.08SysPTM
Link-
2414Phosphoserine.HIPGSPFKI
ECCCCCCEE
23.08UniProtKB
Link-
2417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GSPFKIRVG
CCCCEEEEE
32.74Phosphositeplus
Link-
2510PhosphoserineHIGGSPFKA
CCCCCCEEE
23.19PhosphoELM
Link-
2510PhosphoserineHIGGSPFKA
CCCCCCEEE
23.19Phosphositeplus
Link-
2510PhosphoserineHIGGSPFKA
CCCCCCEEE
23.19SysPTM
Link-
2510Phosphoserine.HIGGSPFKA
CCCCCCEEE
23.19UniProtKB
Link-
2523PhosphoserinePRLVSNHSL
CCCCCCCCC
33.16Phosphositeplus
Link-
2523Phosphoserine (CaM-KII_group)PRLVSNHSL
CCCCCCCCC
33.16PhosphoELM
Link-
2543S-nitrosocysteineTKATCAPQH
CEEEECCCC
6.59dbSNO
Link-
2607N6-acetyllysineEILVKHVGS
EEEEEECCC
29.18Phosphositeplus
Link-
2607N6-acetyllysine.EILVKHVGS
EEEEEECCC
29.18UniProtKB
Link-
2614PhosphotyrosineGSRLYSVSY
CCCEEEEEE
13.10Phosphositeplus
Link-
2618PhosphotyrosineYSVSYLLKD
EEEEEEECC
17.56Phosphositeplus
Link-
2621N6-acetyllysineSYLLKDKGE
EEEECCCCC
55.59Phosphositeplus
Link-
2621N6-acetyllysine.SYLLKDKGE
EEEECCCCC
55.59UniProtKB
Link-
2642PhosphotyrosinePGSPYRVVV
CCCCEEEEE
20.10Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IKKB_HUMANphysical interactionMINT-48088MINT14743216
CCNB2_HUMANphysical interactionMINT-4653263MINT17408621
CCNB2_HUMANphysical interactionMINT-4653285MINT17408621
CCNB2_HUMANdirect interactionMINT-4653339MINT17408621
CCNB2_HUMANdirect interactionMINT-4653361MINT17408621
CCNB2_HUMANphosphorylation reactionMINT-4653401MINT17408621
HS90B_HUMANphysical interactionMINT-72661MINT16263121
DRD2_HUMANphysical interactionMINT-16723MINT11390380
DRD1_HUMANphysical interactionMINT-13854MINT11390380
ITB7_HUMANphysical interactionMINT-51374MINT15225631
PSN1_HUMANphysical interactionMINT-17725MINT9437013
PSN1_HUMANphysical interactionMINT-17726MINT9437013
SMAD3_HUMANphysical interactionMINT-61733MINT15231748
M3K1_HUMANphysical interactionMINT-48331MINT14743216
Q8WUM6_HUMANphysical interactionMINT-51375MINT15225631
TITIN_HUMANphysical interactionMINT-2882596MINT16902413
RIPK3_HUMANphysical interactionMINT-49136MINT14743216
CASR_HUMANphysical interactionDIP:10819EDIP11390379
DRD3_HUMANphysical interactionDIP:10820EDIP11320256
DRD2_HUMANphysical interactionDIP:10821EDIP11320256
PSN1_HUMANin vivo
yeast 2-hybrid
HPRD:02060HPRD9437013
CDC42_HUMANin vitroHPRD:02060HPRD10051605
DRD2_HUMANin vitro
yeast 2-hybrid
HPRD:02060HPRD11911837
DRD3_HUMANin vivo
yeast 2-hybrid
HPRD:02060HPRD11911837
LYAM2_HUMANin vitroHPRD:02060HPRD8609175
PGS2_HUMANin vitroHPRD:02060HPRD12106908
TF_HUMANin vitroHPRD:02060HPRD9490735
FURIN_HUMANin vivoHPRD:02060HPRD9412467
ITB1_HUMANin vivo
yeast 2-hybrid
HPRD:02060HPRD11807098
9722563
GRIK3_HUMANin vivoHPRD:02060HPRD11943148
GRIK1_HUMANin vivoHPRD:02060HPRD11943148
ITB7_HUMANin vitroHPRD:02060HPRD11781567
RHOA_HUMANin vivoHPRD:02060HPRD10051605
RALA_HUMANin vitro
in vivo
HPRD:02060HPRD10051605
VHL_HUMANyeast 2-hybridHPRD:02060HPRD8674032
12169691
GP1BA_HUMANin vivoHPRD:02060HPRD11700320
TLR10_HUMANyeast 2-hybridHPRD:02060HPRD16482509
SHBG_HUMANyeast 2-hybridHPRD:02060HPRD15862967
ARRB2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02060HPRD16611986
ARRB1_HUMANin vitro
in vivo
HPRD:02060HPRD16611986
KPCA_HUMANin vivo
yeast 2-hybrid
HPRD:02060HPRD12704190
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Disease Reference
Kegg disease
OMIM disease
300049Periventricular nodular heterotopia 1 (PVNH1)
300537Periventricular nodular heterotopia 4 (PVNH4)
311300Otopalatodigital syndrome 1 (OPD1)
304120Otopalatodigital syndrome 2 (OPD2)
305620Frontometaphyseal dysplasia (FMD)
309350Melnick-Needles syndrome (MNS)
300048Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (IPOX)
300321FG syndrome 2 (FGS2)
300244Terminal osseous dysplasia (TOD)
314400Cardiac valvular dysplasia X-linked (CVDX)
Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged.
300048
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504; LYS-508; LYS-700;LYS-781; LYS-837; LYS-891; LYS-994; LYS-1538; LYS-2607 AND LYS-2621,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1047, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459;SER-1533; SER-2152; SER-2284 AND SER-2327, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-373; TYR-1604 ANDTYR-2388, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459 ANDSER-2152, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459; SER-2152AND SER-2158, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084 ANDSER-1459, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1338;SER-1459; SER-1533; SER-1630; SER-2053; SER-2152; SER-2327; SER-2414AND SER-2510, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-2152, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures