DKC1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DKC1_DROME
• UniProt AC: O44081
• Protein Name: H/ACA ribonucleoprotein complex subunit 4
• Gene Name: Nop60B
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 508
• Subcellular Localization: Nucleus, nucleolus .
• Protein Description: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for maintenance of the germline stem cell lineage during spermatogenesis..
• Protein Sequence: MADVEVRKEKKKKKIKEEPLDGDDIGTLQKQGNFQIKPSSKIAELDTSQWPLLLKNFDKLNIRSNHYTPLAHGSSPLNRDIKEYMKTGFINLDKPSNPSSHEVVAWIKKILKVEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQSAGKEYVAIFKLHGAVESVAKVRQGLEKLRGALFQRPPLISAVKRQLRVRTVYDSKLLDYDETRNMGVFWVSCEAGSYIRTMCVHLGLVLGVGGQMLELRRVRSGIQSERDGMVTMHDVLDAMWLYENHKDESMLRRVIKPLEGLLVNHKRIIMKDSSVNAVCYGAKITLPGVLRYEDGIEIDQEIVICTTKGEAICLAIALMTTATMASCDHGVVAKIKRVIMERDTYPRKWGLGPKASAKKALIAAGKLDKFGRPNENTPKEWLTGYVDYNAKKPAAQEVSPTNGSSEPSKRKLSTSSVEETAAAAVSEETPSKDKKKKKKKHKGDEEAPEAAEEEAEPVEKEKKKKKKKDKDRDRDEAQE

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
16	Acetylation	EKKKKKIKEEPLDGD HHHCCCCCCCCCCCC	65.98	21791702
74	Phosphorylation	YTPLAHGSSPLNRDI CCCCCCCCCCCCHHH	20.93	19429919
75	Phosphorylation	TPLAHGSSPLNRDIK CCCCCCCCCCCHHHH	37.69	19429919
395	Acetylation	KALIAAGKLDKFGRP HHHHHHCCHHHCCCC	49.11	21791702
428	Phosphorylation	KPAAQEVSPTNGSSE CCCCCCCCCCCCCCC	25.84	19429919
430	Phosphorylation	AAQEVSPTNGSSEPS CCCCCCCCCCCCCCC	44.71	19429919
433	Phosphorylation	EVSPTNGSSEPSKRK CCCCCCCCCCCCCCC	33.33	19429919
434	Phosphorylation	VSPTNGSSEPSKRKL CCCCCCCCCCCCCCC	55.73	19429919
437	Phosphorylation	TNGSSEPSKRKLSTS CCCCCCCCCCCCCCC	40.83	19429919
442	Phosphorylation	EPSKRKLSTSSVEET CCCCCCCCCCCHHHH	29.31	21082442
443	Phosphorylation	PSKRKLSTSSVEETA CCCCCCCCCCHHHHH	35.14	19429919
444	Phosphorylation	SKRKLSTSSVEETAA CCCCCCCCCHHHHHH	29.07	19429919
445	Phosphorylation	KRKLSTSSVEETAAA CCCCCCCCHHHHHHH	33.37	19429919
449	Phosphorylation	STSSVEETAAAAVSE CCCCHHHHHHHHHCC	14.21	19429919
455	Phosphorylation	ETAAAAVSEETPSKD HHHHHHHCCCCCCCC	25.62	19429919
458	Phosphorylation	AAAVSEETPSKDKKK HHHHCCCCCCCCHHH	28.89	19429919
460	Phosphorylation	AVSEETPSKDKKKKK HHCCCCCCCCHHHCH	61.99	22668510

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

Oops, there are no upstream regulatory protein records of DKC1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DKC1_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 DKC1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WNTG_DROME	wg	genetic	25811802

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-442; THR-443; SER-444;SER-445; THR-449; SER-455 AND THR-458, AND MASS SPECTROMETRY.
PubMed: 18327897