SPTCB_DROME - dbPTM
SPTCB_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTCB_DROME
UniProt AC Q00963
Protein Name Spectrin beta chain
Gene Name beta-Spec
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2291
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Description Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner..
Protein Sequence MTTDISIVRWDPSQGPGNEYIDEYEYDGGNSSSRLFERSRIKALAEERESVQKKTFTKWVNSHLCRVNCRIADLYVDMRDGKHLIKLLEVLSGERLPKPTKGKMRIHCLENVDKALQFLREQRVHLENIGSHDIVDGNASLNLGLIWTIILRFQIQDITIEEVDNKETKSAKDALLLWCQMKTAGYHNVNVRNFTTSWRDGLAFNAIIHKHRPDLVQFEKLSKTNAIHNLNNAFDVAEDKLGLAKLLDAEDVFVEHPDEKSIITYVVTYYHYFSKLKQETVQGKRIGKVVGIAMENDKMVHDYENFTSDLLKWIETTIQSLGEREFENSLAGVQGQLAQFSNYRTIEKPPKFVEKGNLEVLLFTLQSKMRANNQKPYTPKEGKMISDINKAWERLEKAEHERELALREELIRQEKLEQLAARFDRKASMRETWLSENQRLVSQDNFGFDLAAVEAAAKKHEAIETDIFAYEERVQAVVAVCDELESERYHDVKRILLRKDNVMRLWTYLLELLRARRMRLEISLQLQQNFQEMLYILDNMEEIKQLLMTDDYGKHLMGVEDLLQKHSLVEADINILGERVKVVVQNSQKFLSDDPESYKPCDPEIIVSRVQQLEDAYAELVRLAVERRSRLEESRKLWQFYWDTADEENWIKEKEQIVSTDEVGHDLTTVNLMLSKHKALESEITSHDPQLQNVAKVGSELITEGHFGADRIKDRLKEILNKWDHLLDLTKYRRQRLENAVEYFQLFADADDVDNWMLDTLRIVSSEDVGRDEANVQSLLKKHKDVADELKNYAEVIDALHKQAESLKLNEAEKANVDKRLEAIDNRYKELTELAKLRKQRLLDALSLYKLMSEADGVEQWIKEKTKMLDTMTPGKDIEDVEIMKHRFEGFDKEMNANASRVAVVNQLARQLLHVEHPNSDEILERQNHLNQEWSTLREKAEAKMDDLKSAHGVQTFYIECRETISWIEDKKRILTETDSLEMDLTGVMTLQRRLSGMDRDLAAIQAKLSSLEREANSIEDEHPEEAKIIRERIAQIELIWEQLTQMLKERDSKLEEAGDLHRFLRDLDHFQTWLTKTQTDVASEDTPTSLPEAEKLLNQHQSIREEIDNYTEDYKNMMEYGERLTSEGSTSDDPQYMFLRERLNALKDGWEELHQMWENRQVLLSQSLDQQLFNRDARQTEVLLSQQEHFLSKDDTPVNLEQAENQLKRHEAFLTTMEANDDKINTLLQVADTLVEKDHFDADKIGKRAENITGRRDDNRQRALDQHEKLKNQVKLHEFLQDLEELAEWVQEKYATSQDESYRSAKTIHSKWTRHQAFEAEIAANKERLFEAEKSAQELSKEKPEFKDVIEPKLKELAKQFDDLEVHTKEKGAMLFDANREVLVQQTCDDIDSYITDLEKQIVSGDTANDLTSVNILMQKQQVIQTQMAVKARQVEEIDKQTEYLQKTVPEEKIEPIVVKKTAVLERFEKIKAPLLERQKALEKKKEAFQFCRDVEDEKLWIDEKLPVANSPDYGNSLFNVHVLKKKNQSLATEIDNHEPRINAICNNGRKLIDEGHEDAKKFEALISDLTQKWQELKDAIENRRKHLLESEKVQQYFFDAQEAESWMSEQELYMMVEDRGKDEISAQNLMKKHENLEQSVEDYANTIRQLGEVARQFSGDDISSGDAVAVKQSQLDKLYAGLKDLAGERRARLNEALQLFMLSREVDDLEQWITDREVVAGSQELGQDFDHVTLLSERFNEFARDTEAVGGERVAKVNGIADNLIQAGHSDSATIAEWKDNLNESWQDLLELIETRTQMLAASRELHKFFHDCKDVLGRILEKQHGVSDELGRDAGSVSTLQRKHYNFLQDLITLYSQVQQIQEESAKLQDAYAGDKAKEITNREQEVLHAWDNLQAMCDARKQKLADTGDLFRFFNMVRILMIWMEDLVRQMNTSEKPRDVSGVELLMNNHQSLKAEIDTREDNFGACISLGKELLTRNHYASADIKDRLMTLSNSRNALLRRWEERWENLQLILEVYQFARDAAVAEAWLIAQEPYLLSSELGHTIDEVENLIKKHEAFEKSAAAQEERFSALERLTTFELKEMKRRQELAEEAERQRIKEEQEAKAASEAAEQAKREAERRDDVDVGASHDDSERGGTPGAGEGHEGYVTRKHEWDSTTKKASNRSWDKVYMAAKAGRISFYKDQKGYKSNPELTFRGEPSYDLQNAAIEIASDYTKKKHVLRVKLANGALFLLQAHDDTEMSQWVTSLKAQSDSTAVAASRSQTLPATSQKDEPKRRSFFTLKKK
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
159PhosphorylationRFQIQDITIEEVDNK
HHHCCCCCHHHCCCC		30.5325749252
996PhosphorylationMTLQRRLSGMDRDLA
HHHHHHHCCCCHHHH		30.2019429919
1512PhosphorylationEKLPVANSPDYGNSL
CCCCCCCCCCCCCCC		14.9227794539
1841PhosphorylationGRDAGSVSTLQRKHY
CCCCCCHHHHHHHHH		25.7119429919
1842PhosphorylationRDAGSVSTLQRKHYN
CCCCCHHHHHHHHHH		25.4219429919
2075PhosphorylationAAQEERFSALERLTT
HHHHHHHHHHHHHHH		37.8621082442
2138PhosphorylationVGASHDDSERGGTPG
CCCCCCCCCCCCCCC		34.9429892262
2143PhosphorylationDDSERGGTPGAGEGH
CCCCCCCCCCCCCCC		22.7519429919
2168PhosphorylationDSTTKKASNRSWDKV
CCCCCCCCCCCCHHH		41.4727794539
2174AcetylationASNRSWDKVYMAAKA
CCCCCCHHHHHHHHH		29.0721791702
2195PhosphorylationKDQKGYKSNPELTFR
ECCCCCCCCCCCEEC		49.4822817900
2266PhosphorylationDSTAVAASRSQTLPA
CCCCHHHHHCCCCCC		23.7927794539
2268PhosphorylationTAVAASRSQTLPATS
CCHHHHHCCCCCCCC		25.6428490779
2270PhosphorylationVAASRSQTLPATSQK
HHHHHCCCCCCCCCC		35.6422817900
2274PhosphorylationRSQTLPATSQKDEPK
HCCCCCCCCCCCCCC		29.7425749252
2284PhosphorylationKDEPKRRSFFTLKKK
CCCCCCCCCEEECCC		28.8425749252
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 SPTCB_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPTCB_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 SPTCB_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLIT_DROMEsligenetic
17215305
SPTCA_DROMEalpha-Specgenetic
17121810
DYHC_DROMEDhc64Cgenetic
20368622
DCTN1_DROMEGlgenetic
20368622
SPTCA_DROMEalpha-Specphysical
7971971
SPTCA_DROMEalpha-Specphysical
25381248
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPTCB_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-2195, AND MASSSPECTROMETRY.

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