LAM0_DROME - dbPTM
LAM0_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAM0_DROME
UniProt AC P08928
Protein Name Lamin Dm0
Gene Name Lam {ECO:0000312|FlyBase:FBgn0002525}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 622
Subcellular Localization Nucleus . Nucleus inner membrane . Nucleus envelope . Nucleus lamina . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm . Nuclear periphery (PubMed:7593280). At metaphase and anaphase, weakly expressed in the nuclear envelope and spindle poles (PubM
Protein Description Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. [PubMed: 3126192]
Protein Sequence MSSKSRRAGTATPQPGNTSTPRPPSAGPQPPPPSTHSQTASSPLSPTRHSRVAEKVELQNLNDRLATYIDRVRNLETENSRLTIEVQTTRDTVTRETTNIKNIFEAELLETRRLLDDTARDRARAEIDIKRLWEENEELKNKLDKKTKECTTAEGNVRMYESRANELNNKYNQANADRKKLNEDLNEALKELERLRKQFEETRKNLEQETLSRVDLENTIQSLREELSFKDQIHSQEINESRRIKQTEYSEIDGRLSSEYDAKLKQSLQELRAQYEEQMQINRDEIQSLYEDKIQRLQEAAARTSNSTHKSIEELRSTRVRIDALNANINELEQANADLNARIRDLERQLDNDRERHGQEIDLLEKELIRLREEMTQQLKEYQDLMDIKVSLDLEIAAYDKLLVGEEARLNITPATNTATVQSFSQSLRNSTRATPSRRTPSAAVKRKRAVVDESEDHSVADYYVSASAKGNVEIKEIDPEGKFVRLFNKGSEEVAIGGWQLQRLINEKGPSTTYKFHRSVRIEPNGVITVWSADTKASHEPPSSLVMKSQKWVSADNTRTILLNSEGEAVANLDRIKRIVSQHTSSSRLSRRRSVTAVDGNEQLYHQQGDPQQSNEKCAIM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSSKSRRAG
------CCCCCCCCC		46.61-
10PhosphorylationSKSRRAGTATPQPGN
CCCCCCCCCCCCCCC		26.7728490779
12PhosphorylationSRRAGTATPQPGNTS
CCCCCCCCCCCCCCC		23.4628490779
18PhosphorylationATPQPGNTSTPRPPS
CCCCCCCCCCCCCCC		39.6319429919
19PhosphorylationTPQPGNTSTPRPPSA
CCCCCCCCCCCCCCC		40.1819429919
20PhosphorylationPQPGNTSTPRPPSAG
CCCCCCCCCCCCCCC		22.6819429919
25PhosphorylationTSTPRPPSAGPQPPP
CCCCCCCCCCCCCCC		48.8419429919
34PhosphorylationGPQPPPPSTHSQTAS
CCCCCCCCCCCCCCC		44.5219429919
35PhosphorylationPQPPPPSTHSQTASS
CCCCCCCCCCCCCCC		31.1819429919
37PhosphorylationPPPPSTHSQTASSPL
CCCCCCCCCCCCCCC		29.3419429919
39PhosphorylationPPSTHSQTASSPLSP
CCCCCCCCCCCCCCC		31.3619429919
41PhosphorylationSTHSQTASSPLSPTR
CCCCCCCCCCCCCCC		35.5619429919
42PhosphorylationTHSQTASSPLSPTRH
CCCCCCCCCCCCCCH		27.6519429919
45PhosphorylationQTASSPLSPTRHSRV
CCCCCCCCCCCHHCH		27.8423607784
47PhosphorylationASSPLSPTRHSRVAE
CCCCCCCCCHHCHHH		37.323126192
50PhosphorylationPLSPTRHSRVAEKVE
CCCCCCHHCHHHHHH		25.769013881
55AcetylationRHSRVAEKVELQNLN
CHHCHHHHHHHCCHH		31.1321791702
170AcetylationRANELNNKYNQANAD
HHHHHHHHHHHHHHH		44.5021791702
222PhosphorylationDLENTIQSLREELSF
CHHHHHHHHHHHHCC		26.0829892262
235PhosphorylationSFKDQIHSQEINESR
CCCHHHHHHHHHHHH		31.0119429919
249PhosphorylationRRIKQTEYSEIDGRL
HCCEECCCHHCCCCC		18.263126192
250PhosphorylationRIKQTEYSEIDGRLS
CCEECCCHHCCCCCC		23.1125749252
257PhosphorylationSEIDGRLSSEYDAKL
HHCCCCCCHHHHHHH		21.5529892262
267PhosphorylationYDAKLKQSLQELRAQ
HHHHHHHHHHHHHHH		30.3619429919
293AcetylationIQSLYEDKIQRLQEA
HHHHHHHHHHHHHHH		28.8821791702
310AcetylationRTSNSTHKSIEELRS
HHCCCCCHHHHHHHH		53.9021791702
311PhosphorylationTSNSTHKSIEELRST
HCCCCCHHHHHHHHC		27.853126192
317PhosphorylationKSIEELRSTRVRIDA
HHHHHHHHCCHHHHH		32.9427626673
413PhosphorylationEEARLNITPATNTAT
CHHHCCCCCCCCHHH		13.0519060867
418PhosphorylationNITPATNTATVQSFS
CCCCCCCHHHHHHHH		21.2525749252
425PhosphorylationTATVQSFSQSLRNST
HHHHHHHHHHHHHCC		24.8923607784
427PhosphorylationTVQSFSQSLRNSTRA
HHHHHHHHHHHCCCC		28.2623607784
435PhosphorylationLRNSTRATPSRRTPS
HHHCCCCCCCCCCCC		20.6425749252
437PhosphorylationNSTRATPSRRTPSAA
HCCCCCCCCCCCCHH		30.0027626673
440PhosphorylationRATPSRRTPSAAVKR
CCCCCCCCCCHHHHH		22.0819429919
442PhosphorylationTPSRRTPSAAVKRKR
CCCCCCCCHHHHHCC		28.3922817900
455PhosphorylationKRAVVDESEDHSVAD
CCEEECCCCCCCHHH		43.8122817900
459PhosphorylationVDESEDHSVADYYVS
ECCCCCCCHHHEEEE		31.1822817900
476AcetylationAKGNVEIKEIDPEGK
CCCCEEEEEECCCCC		34.8021791702
483AcetylationKEIDPEGKFVRLFNK
EEECCCCCEEEEEEC		38.7421791702
509AcetylationLQRLINEKGPSTTYK
HHHHHHCCCCCCCEE		72.1821791702
516AcetylationKGPSTTYKFHRSVRI
CCCCCCEEEEECEEE		32.3821791702
582PhosphorylationDRIKRIVSQHTSSSR
HHHHHHHHHCCCCCH		17.5522817900
585PhosphorylationKRIVSQHTSSSRLSR
HHHHHHCCCCCHHHC		23.7519429919
586PhosphorylationRIVSQHTSSSRLSRR
HHHHHCCCCCHHHCC		24.9619429919
587PhosphorylationIVSQHTSSSRLSRRR
HHHHCCCCCHHHCCC		22.1919429919
588PhosphorylationVSQHTSSSRLSRRRS
HHHCCCCCHHHCCCC		36.6919429919
591PhosphorylationHTSSSRLSRRRSVTA
CCCCCHHHCCCCEEE		23.7219429919
595PhosphorylationSRLSRRRSVTAVDGN
CHHHCCCCEEEECCC		23.2421082442
597PhosphorylationLSRRRSVTAVDGNEQ
HHCCCCEEEECCCCC		23.3919429919
606PhosphorylationVDGNEQLYHQQGDPQ
ECCCCCCCCCCCCCC		9.4022668510
615PhosphorylationQQGDPQQSNEKCAIM
CCCCCCCCCCCCCCC		41.5323607784
619MethylationPQQSNEKCAIM----
CCCCCCCCCCC----		2.24-
619FarnesylationPQQSNEKCAIM----
CCCCCCCCCCC----		2.24-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
42SPhosphorylationKinaseCDK1P23572
GPS
42SPhosphorylationKinaseCDK-FAMILY-GPS
42SPhosphorylationKinaseCDK_GROUP-PhosphoELM
42SPhosphorylationKinaseCDK7-PhosphoELM
50SPhosphorylationKinasePKA-FAMILY-GPS
50SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAM0_DROME !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LAM0_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OTE_DROMEOtephysical
22036573
RFA1_DROMERpA-70physical
22036573
DYLT_DROMEDlc90Fphysical
22036573
HP1_DROMESu(var)205genetic
25417159
ECR_DROMEEcRgenetic
15996653
LAMC_DROMELamCgenetic
23827710
NEMO_DROMEkeygenetic
25417159
ERKA_DROMErlgenetic
23827710
NU153_DROMENup153physical
23827710
LAM0_DROMELamphysical
10350216
LAM0_DROMELamphysical
19855837
LAM0_DROMELamphysical
9632815
BICD_DROMEBicDphysical
10350216
WASH1_DROMEwashphysical
25754639
LAMC_DROMELamCphysical
19855837
OTE_DROMEOtephysical
9632815
TOPRS_DROMEToporsphysical
16209949
BRCA2_DROMEBrca2physical
25588834
JIL1_DROMEJIL-1physical
16254246
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAM0_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; THR-12; THR-20;SER-25; SER-34; THR-39; SER-41; SER-42; SER-45; THR-47; SER-235;TYR-249; SER-250; SER-311; THR-413; THR-435; SER-442; SER-455;SER-459; SER-595; THR-597 AND SER-615, AND MASS SPECTROMETRY.

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