LVA_DROME - dbPTM
LVA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LVA_DROME
UniProt AC Q8MSS1
Protein Name Protein lava lamp
Gene Name lva
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2779
Subcellular Localization Golgi apparatus . Cytoplasmic vesicle, autophagosome . Lva-alpha-spectrin and Lva-CLIP-190 complexes are found at the Golgi (PubMed:11076973). Upon autophagosome induction by starvation, also detected in small vesicle structures (PubMed:22493244).
Protein Description Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. [PubMed: 11076973 Under starvation conditions recruited by ema to developing autophagsosomes where it may function in autophagosome growth]
Protein Sequence MAEDSGALESSYDFSIVQPDDHEYGEADIRLAGSSNDLSSLQNVSASTTRGTKGKGRLDSLKENLYKQQERLTALKERALRKSQDERHKSSMSDSMESLKTLGQKLTVLKTRSGDSSTPLVSPTKDSDPGDVSLLQTSGSEKLLMLTQRTEQNRALLEQRKRDLAKSLLSVKSNIGHQTTAELGSSMTDLRHAASVSNPPVSRHRSALDLEAQGQEAVDESRVKLLRSRMKLTELKQGRQEQELNELRTELAKRAKLIERLELSGAELQRTLTQRNEELEQLRVVQAEEDSLKVQENSRLQGEVLVLRERLAELENVNDLLETTRCELQEELTTARERQRNLELEQEQEKASRSPQSEAAHTDAQVSAELAKQLQELTNQLADLQATNEELRQQVAAQAKLQVTDEIVSQRLEELEATIAAQLLELQEQKSAMAAQNEELAEKTTELNVLNVNLRLLEEKLAQSSRSKPLFLEDHSEDSAASKQMQEDLQQLKLKLDETNKANIKLKLKCKQAEKKLQKFQSQDGQQQLASLLADNEELQQRIAVLEDEKGQWQLANMQEDDRQPEQSTESNNPLQLETIRLLEEQKLELQQALEALLSSSSSAESIEIVERHHLECLGQRRPASEGDAQEQKQVHPPGPSHVSELTQTEQTEEEDSSGETLSQLRERLELFTQERGEVLDKLEQLSAENLQLQARLEESSSSLQLLQREREKDLISSTSTSSNLSQELSSMQRSSEVVATLDAGEGGPVLFEKCEKSLSKLNSELEAYRKANDRQAKFNVSKKLAKEAKNCHTQLSELLHKVKEASTAVETVTVVETVVAVTAPNGKALAEYEQLNAQNAELKAVISRLRQELDELRESYPETEAPLAIVGSDSQREDEILQLQSQLEDARSLQAEQRQQIEEQVDQIKELRQTEAEQLQLVARQSAEITQLQLQSEQFDQLLNSKEMSHEKQLEQQTRIRRELEARAESLEGELSILQTLVAEQKQQLIESVSESEHALNLKMLELQSAQEELRELRAKEDPDQLREALRVSKSLVAQQVRELTSSQETVDALNQQIQEYQGLEHAHKEEQFKNRELREKLKKYALNLKKRTQDNADLEQKVQELTSQLQEQQELVKQKEEVEREPIVDNHRVEQLQQQVSKLNEDLKAKIHLNLENRDALRQLKQQIQEQEQLIQERDAELQDANLVSKELRRERQEADQEVFQLGQENSRLREEISKLQEEIHNLGQRVNEEPTAVEDLRRQLEAKSKKFEKSKELIKLRNATIQSLQRELQQLQQDQDSEVEHVRNARAAHEQLRLEKDAEITALRQEILKLERSRAAGEGDDTITKTSHQLLESQSQQQAESLQVAERELQQLRVQLTAAQEQHALLAQQYASDKANFEMTIARLETLHEGIQAKLQEDASYIESLEAQNTELQARSAALEEQAASQANQQAASQDKVQILEQQLKEQREQEEQKRQQDQQLQERFYELGQREQAQSRQLELLTSEAEESRQQLAGLRTEYESLLAKHSQLTATAQAEREQMSSHSQEELAELRQQLDVKEADLHRQRQVYDAKLAAKATELDELECDLNSHVERAAAETRELCQQLERSQELVAQRTEELQRLNEEFQEVERERSTLSREVTLLRLQHDSAEQDVLELQELRMQAMQDKTEMDNLRTQIDALCANHSQELQALQQRIAELDTLGQNQTDDQVYIETENKRLAEQLSELQAQLARQQHQQQQQQHHHPAVQSQQHPPPASLFFGGDALAAPSPFDEIAQPLRVSSLAASAPPPISPPPTIEDLQRNVSDLEKHAQDLETKLLARNQNLAEQEERRLQLEQRLSEVERLLSERTQQLADIQTANEERDRLAALEKLIQPAAAPTLDMFFGGQAEETVPDAVSHHLDLGLPQTEPVVEPLIQPKKAYLCQPKQEIQEQTAQTIDWGVDEDPWASAANEAPQTDVEHLHTRIAQLELQLSNAEQQKTELQTKAAKLMKRLKEYKTKATTTATPTVTVDNDLDSTIIEELKHQLQLQESRLSKAEEISQQHALEKEKLAKRIDVLTAGNDRMAEMKERQDMDVQMYQARIRELQEKLSQLDQWGEPAATVSSSLDGDEAARIESLQQEIQQLRQQVSELEDERTRDQAELGALRQSSQGYDEAEDNQKLELQQLRQQESELEALRTRDQSELEALRQSCQGHDETVRIATLQQDNQQLELQQLRQAIIELETLRARDQTELEALRQSSQGHDEAARIAIEQRDNQQLELQQLRQQLIELEALRARDQAELEALRQSCQGQQLSVDMASRNDEQMAQLQEKESEIVHLKQRIEELMREDQTEKLVFEILTKNQELQLLRMQVKQLEEDKEDQQVSAAPPKDDGETVEKLKSLCQQLQQEKSDMEEELRVLNNHVLSSLELEDRMKQTLLQLDTKNIEITELRRSLEILQSQNLGQNSAAEQIPDLSAINQQWEQLVEQKCGEVASIWQEHLSQREAAFKAQLEEVTQQQQRELPQSQQSTQGEATSDIMQKMQKALETQEMEIVTLKEQLAIRSAEYARLAAQYDPFRLQNRGGASGGNPASTTVSAGGPPSLTANEPLPEYVLKADLDYALMMLHQRDMRVEEMIVELVQLLEERDHLQLKLSDTLRQLETERSRVSDEPSATASSSAASSSSPSKISSAGSNSELLGTTSAAGSDLKQKLAELQTVKHSKDKVIVDEREQRLQQMLQLQKDMAKQGSGSQSGAGAVAAVAAPTSAAPTAIGVDLSQSGLRSPSMMLMDWILGNNNKEEEAGHQTTG
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
34PhosphorylationADIRLAGSSNDLSSL
HCEEECCCCCCHHHC		21.9919429919
35PhosphorylationDIRLAGSSNDLSSLQ
CEEECCCCCCHHHCC		33.1819429919
39PhosphorylationAGSSNDLSSLQNVSA
CCCCCCHHHCCCCCC		31.6919429919
40PhosphorylationGSSNDLSSLQNVSAS
CCCCCHHHCCCCCCC		41.0719429919
60PhosphorylationKGKGRLDSLKENLYK
CCCCHHHHHHHHHHH		46.0322817900
83PhosphorylationKERALRKSQDERHKS
HHHHHHHCHHHHHHH		36.1122817900
93PhosphorylationERHKSSMSDSMESLK
HHHHHHHHHHHHHHH		28.6029892262
95PhosphorylationHKSSMSDSMESLKTL
HHHHHHHHHHHHHHH		19.6919429919
98PhosphorylationSMSDSMESLKTLGQK
HHHHHHHHHHHHHHH		26.9019429919
117PhosphorylationKTRSGDSSTPLVSPT
ECCCCCCCCCCCCCC		38.4929892262
118PhosphorylationTRSGDSSTPLVSPTK
CCCCCCCCCCCCCCC		25.2919429919
122PhosphorylationDSSTPLVSPTKDSDP
CCCCCCCCCCCCCCC		34.2419429919
124PhosphorylationSTPLVSPTKDSDPGD
CCCCCCCCCCCCCCC		39.7219429919
127PhosphorylationLVSPTKDSDPGDVSL
CCCCCCCCCCCCCEE		47.4622668510
133PhosphorylationDSDPGDVSLLQTSGS
CCCCCCCEEEECCCC		28.2718327897
137PhosphorylationGDVSLLQTSGSEKLL
CCCEEEECCCCCHHH		34.7219429919
138PhosphorylationDVSLLQTSGSEKLLM
CCEEEECCCCCHHHH		27.6219429919
140PhosphorylationSLLQTSGSEKLLMLT
EEEECCCCCHHHHHH		31.1819429919
167PhosphorylationRKRDLAKSLLSVKSN
HHHHHHHHHHHHHHC		29.0022817900
173PhosphorylationKSLLSVKSNIGHQTT
HHHHHHHHCCCCCHH		31.3721082442
185PhosphorylationQTTAELGSSMTDLRH
CHHHHHCCCCHHHHH		29.5719429919
186PhosphorylationTTAELGSSMTDLRHA
HHHHHCCCCHHHHHH		24.7319429919
188PhosphorylationAELGSSMTDLRHAAS
HHHCCCCHHHHHHHH		33.5519429919
195PhosphorylationTDLRHAASVSNPPVS
HHHHHHHHCCCCCCC		27.1921082442
202PhosphorylationSVSNPPVSRHRSALD
HCCCCCCCCCCCCCC		28.3021082442
206PhosphorylationPPVSRHRSALDLEAQ
CCCCCCCCCCCHHHH		27.3619429919
352PhosphorylationEQEQEKASRSPQSEA
HHHHHHHHCCCCHHH		44.3419429919
354PhosphorylationEQEKASRSPQSEAAH
HHHHHHCCCCHHHHH		25.4619429919
357PhosphorylationKASRSPQSEAAHTDA
HHHCCCCHHHHHHHH		32.3619429919
362PhosphorylationPQSEAAHTDAQVSAE
CCHHHHHHHHHHHHH		28.4419429919
625PhosphorylationLGQRRPASEGDAQEQ
HCCCCCCCCCCHHHH		44.8119429919
1284PhosphorylationQLQQDQDSEVEHVRN
HHHHCCCHHHHHHHH		37.6019429919
1770PhosphorylationIAQPLRVSSLAASAP
CCCCCCHHHHHHCCC		17.1319429919
1771PhosphorylationAQPLRVSSLAASAPP
CCCCCHHHHHHCCCC		21.1219429919
1775PhosphorylationRVSSLAASAPPPISP
CHHHHHHCCCCCCCC		35.3819429919
1781PhosphorylationASAPPPISPPPTIED
HCCCCCCCCCCCHHH		36.8119429919
1785PhosphorylationPPISPPPTIEDLQRN
CCCCCCCCHHHHHHC		42.6519429919
2106PhosphorylationDEAARIESLQQEIQQ
HHHHHHHHHHHHHHH		29.1622668510
2161PhosphorylationQQLRQQESELEALRT
HHHHHHHHHHHHHHH		43.0522817900
2180PhosphorylationELEALRQSCQGHDET
HHHHHHHHHCCCCCH		11.2818511481
2573PhosphorylationVSAGGPPSLTANEPL
CCCCCCCCCCCCCCC		41.3021082442
2575PhosphorylationAGGPPSLTANEPLPE
CCCCCCCCCCCCCCH		31.6021082442
2652PhosphorylationTASSSAASSSSPSKI
CCCCCCCCCCCCHHC		30.3919429919
2653PhosphorylationASSSAASSSSPSKIS
CCCCCCCCCCCHHCC		30.0619429919
2654PhosphorylationSSSAASSSSPSKISS
CCCCCCCCCCHHCCC		43.7119429919
2655PhosphorylationSSAASSSSPSKISSA
CCCCCCCCCHHCCCC		34.8319429919
2657PhosphorylationAASSSSPSKISSAGS
CCCCCCCHHCCCCCC		44.5619429919
2661PhosphorylationSSPSKISSAGSNSEL
CCCHHCCCCCCCCHH		39.8729892262
2664PhosphorylationSKISSAGSNSELLGT
HHCCCCCCCCHHCCC		36.5819060867
2754PhosphorylationLSQSGLRSPSMMLMD
CCCCCCCCHHHHHHH		26.7719429919
2756PhosphorylationQSGLRSPSMMLMDWI
CCCCCCHHHHHHHHH		20.3319429919
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

Oops, there are no upstream regulatory protein records of LVA_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LVA_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 LVA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOS_DROMESosphysical
14605208
SPTCB_DROMEbeta-Specphysical
11076973
CL190_DROMECLIP-190physical
11076973
SPTCA_DROMEalpha-Specphysical
11076973
DYHC_DROMEDhc64Cphysical
26216903
DCTN1_DROMEGlphysical
26216903
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LVA_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 SER-34; SER-35; SER-95;SER-98; SER-122; SER-133; SER-186; SER-352 AND SER-354, AND MASSSPECTROMETRY.

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