TPR_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TPR_DROME
• UniProt AC: A1Z8P9
• Protein Name: Nucleoprotein TPR
• Gene Name: Mtor
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2346
• Subcellular Localization: Nucleus . Nucleus matrix . Nucleus lamina . Nucleus envelope . Nucleus membrane ; Peripheral membrane protein ; Nucleoplasmic side . Nucleus, nuclear pore complex . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Midbody . In
• Protein Description: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC. Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment. Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome. Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy. Preferentially binds to NARs of the male X chromosome. Acts also as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad2 and Mps1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression..
• Protein Sequence: MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNELRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIARVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAVKTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQLTEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSEELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENKKLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASEKNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSEQPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQKEQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEKETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDEEKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREHGEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLKSLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELLRSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRNNEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAITDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEEFKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKNRLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDEHEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKDINQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASIRPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTSSHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTATAPSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKRLRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDNEGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWKQAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSGSDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVSSEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNRFAQRTRNRRPIRRPPPNNFNNGGRFP

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
270	Acetylation	ATEEYVGKLKKELDA HHHHHHHHHHHHHHH		19608861
621	Phosphorylation	QKKLGQNTVDLDDSN HHHHCCCCCCCCCCC		22817900
627	Phosphorylation	NTVDLDDSNLEPNDS CCCCCCCCCCCCCCC		19429919
634	Phosphorylation	SNLEPNDSALDTSEQ CCCCCCCCCCCCCCC		19429919
711	Acetylation	ELTSSNCKLMNTTEF HHHHHCCCCCCCCHH		19608861
720	Acetylation	MNTTEFQKEQIELLH CCCCHHHHHHHHHHH		19608861
728	Acetylation	EQIELLHKNIGTYKQ HHHHHHHHHCCCCHH		19608861
749	Acetylation	ERTKNYEKTIIKHEQ HHHHCHHHHEECCHH		19608861
753	Acetylation	NYEKTIIKHEQTVHL CHHHHEECCHHHHHH		19608861
762	Acetylation	EQTVHLLKDEMMAAH HHHHHHHHHHHHHHH		19608861
1206	Acetylation	RNNEQLLKIIKFLRK CCHHHHHHHHHHHHH		19608861
1342	Acetylation	SLRTEAIKWRQRANA CHHHHHHHHHHHHHH		19608861
1625	Phosphorylation	QLTRQLGSQQSTKPS HHHHHHCCCCCCCCC		22817900
1628	Phosphorylation	RQLGSQQSTKPSTSS HHHCCCCCCCCCCCC		21082442
1646	Phosphorylation	KGNISESSPRTANVK HCCCCCCCCCCCCCC		22817900
1675	Phosphorylation	TPWRGGETPLASIRP CCCCCCCCCCCCEEE		21082442
1684	Phosphorylation	LASIRPISVQNSRTA CCCEEEEEECCCCEE		21082442
1688	Phosphorylation	RPISVQNSRTAAILP EEEEECCCCEEEECC		21082442
1704	Phosphorylation	SQQPPAGSSTSTSSS CCCCCCCCCCCCCCC		22817900
1874	Phosphorylation	VSSHSRHTPSSSNVT EECCCCCCCCCCCCE		21082442
1902	Phosphorylation	PRDIEGDSSTGTEEG CCCCCCCCCCCCHHH		19429919
1903	Phosphorylation	RDIEGDSSTGTEEGV CCCCCCCCCCCHHHH		19429919
1904	Phosphorylation	DIEGDSSTGTEEGVA CCCCCCCCCCHHHHH		19429919
2097	Phosphorylation	AARRNESSVEIVSSP HHHCCCCCEEEECCH		21082442
2102	Phosphorylation	ESSVEIVSSPQVSNF CCCEEEECCHHHHCC		21082442
2103	Phosphorylation	SSVEIVSSPQVSNFC CCEEEECCHHHHCCC		22817900
2118	Phosphorylation	EQPARLESAEVDGTA CCCCCCCCCEECCCC		29892262
2145	Phosphorylation	PSDTGAASASSPQKQ CCCCCCCCCCCHHHH		19429919
2147	Phosphorylation	DTGAASASSPQKQSE CCCCCCCCCHHHHHC		19429919
2148	Phosphorylation	TGAASASSPQKQSEA CCCCCCCCHHHHHCC		19429919
2260	Phosphorylation	EGREAEATSPSENTR CCCCCCCCCCCCCHH		19429919
2261	Phosphorylation	GREAEATSPSENTRF CCCCCCCCCCCCHHH		19429919
2263	Phosphorylation	EAEATSPSENTRFRT CCCCCCCCCCHHHHH		19429919
2288	Phosphorylation	HRAMRGGSPNSQNRP CCCCCCCCCCCCCCC		27626673
2291	Phosphorylation	MRGGSPNSQNRPQRI CCCCCCCCCCCCCEE		25749252
2305	Phosphorylation	IVWQRDTSPGNIQQN EEEECCCCCCCCCHH		30478224

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TPR_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TPR_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TPR_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSC_DROME	Psc	physical	18923078
RING1_DROME	Sce	physical	18923078
RB87F_DROME	Hrb87F	physical	25663367

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.