TSH_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TSH_DROME
• UniProt AC: P22265
• Protein Name: Protein teashirt
• Gene Name: tsh
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 954
• Subcellular Localization: Nucleus. Cytoplasm. Initially localized in the cytoplasm soon after the blastoderm stage, and becomes nuclear by stage 9.
• Protein Description: Homeotic protein that acts downstream of Arm in the Wg cascade during embryogenesis to determine segment identity throughout the entire trunk. Acts cooperatively with other trunk homeotic proteins to repress head homeotic genes and therefore repress head segmental identity. Necessary, in combination with Scr, for the formation of the prothoracic segment. Promotes eye development in the dorsal region of the eye disk and suppresses eye development in the ventral region in combination with Wg-signaling and several early dorso-ventral eye patterning genes. Required for proper development of proximal leg segments. Has differential functions along the dorso-ventral axs of the antennal and leg disks. May play a role in wing hinge development. Possible involvement in chromatin structure for modulation of transcription. Binds DNA and can act as both a transcriptional repressor and activator. Positively regulates its own expression as well as that of Dll. Negatively regulates the expression of mod. Required for Wg-mediated transcriptional repression of Ubx in the midgut. Also represses transcription of lab in the midgut and is necessary for the proper formation of anterior and central midgut structures. Tiptop (tio) and teashirt (tsh) have, on the whole, common activities. Tio and tsh repress each other's expression and tsh has a crucial role for trunk patterning that is in part masked by ectopic expression of tiptop. Both genes share a common activity required for the activation of Ser and svb and the maintenance of en and wg..
• Protein Sequence: MLHEALMLEIYRQALNAGALPTARPRSTESANSSERCPSHDSNSSEHGGGAGSGGVGHRLDAAALSTGVMPGEGPTTLHSSFPAVPQSLPSQPPSMEAYLHMVAAAAQQYGFPLAAAAAAGAGPRLPLPLANEAAAPFKLPPQASPTASSNNSEALDFRTNLYGRAESAEPPASEGEEEEFDDGANNPLDLSVGTRKRGHESEPQLGHIQVKKMFKSDSPPANSVASPSASQLLPGVNPYLAAVAAANIFRAGQFPDWNSKNDLVVDPLEKMSDIVKGGASGMGTKEKMHSSKATTPQAASQPPKSPVQPTPNQNSESGGGSGGGAAGSGAVTKARHNIWQSHWQNKGVASSVFRCVWCKQSFPTLEALTTHMKDSKHCGVNVPPFGNLPSNNPQPQHHHPTPPPPPQNHNLRKHSSGSASNHSPSANVKNAFQYRGDPPTPLPRKLVRGQNVWLGKGVEQAMQILKCMRCGESFRSLGEMTKHMQETQHYTNILSQEQSISIKSGNANANSDAKESHNSLSSEESRTLSAVLTCKVCDKAFNSLGDLSNHMAKNNHYAEPLLQSAGARKRPAPKKREKSLPVRKLLEMKGGSGTTQEDHSNEKTSVQGKPGLGPGGGDKNDAALFAERMRQYITGVKAPEEIAKVAAAQLLAKNKSPELVEQKNGGSAKAAGASSVLSAIEQMFTTSFDTPPRHASLPASSPSNSSTKNTSPVASSILKRLGIDETVDYNKPLIDTNDPYYQHYRYTSSERSGSECSAEARPRLDAPTPEKQQQGGGHDEESSKPAIKQEREAESKPVKMEIKSEFVDEPNEAEETSKMEAAVVNGSATNNNNNIVERSSPKTPSSAASPQTRLLPPRSPAESQRSVTPKSPASSHKSYDGSSEGTKKFPSDSLNALSSMFDSLGSSGAGANSRAKLAAAAAAGGSESPENLTAGGNSLAALRQFCVKKEKTA

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
27	Phosphorylation	LPTARPRSTESANSS CCCCCCCCCCCCCCC	38.93	27626673
168	Phosphorylation	NLYGRAESAEPPASE CCCCCCCCCCCCCCC	36.63	22668510
295	Phosphorylation	KMHSSKATTPQAASQ HHHCCCCCCCCHHCC	42.62	23607784
296	Phosphorylation	MHSSKATTPQAASQP HHCCCCCCCCHHCCC	20.47	23607784
301	Phosphorylation	ATTPQAASQPPKSPV CCCCCHHCCCCCCCC	46.35	23607784
306	Phosphorylation	AASQPPKSPVQPTPN HHCCCCCCCCCCCCC	35.76	23607784
311	Phosphorylation	PKSPVQPTPNQNSES CCCCCCCCCCCCCCC	20.13	23607784
316	Phosphorylation	QPTPNQNSESGGGSG CCCCCCCCCCCCCCC	24.31	23607784
318	Phosphorylation	TPNQNSESGGGSGGG CCCCCCCCCCCCCCC	42.43	23607784
477	Phosphorylation	RCGESFRSLGEMTKH HCCCHHHHHHHHHHH	38.42	22668510
482	Phosphorylation	FRSLGEMTKHMQETQ HHHHHHHHHHHHHHH	17.31	22668510
512	Phosphorylation	SGNANANSDAKESHN CCCCCCCCHHHHHHH	36.21	22668510
657	Phosphorylation	QLLAKNKSPELVEQK HHHHCCCCHHHHHHH	32.76	19429919
712	Phosphorylation	NSSTKNTSPVASSIL CCCCCCCCHHHHHHH	27.11	27794539
750	Phosphorylation	QHYRYTSSERSGSEC HHHCCCCCCCCCCCC	29.27	22817900
758	Phosphorylation	ERSGSECSAEARPRL CCCCCCCCCCCCCCC	25.70	18327897
853	Phosphorylation	SSAASPQTRLLPPRS CCCCCCCCCCCCCCC	27.03	27626673
860	Phosphorylation	TRLLPPRSPAESQRS CCCCCCCCHHHHCCC	33.95	22668510
867	Phosphorylation	SPAESQRSVTPKSPA CHHHHCCCCCCCCCC	23.78	19429919
869	Phosphorylation	AESQRSVTPKSPASS HHHCCCCCCCCCCCC	26.67	19429919
872	Phosphorylation	QRSVTPKSPASSHKS CCCCCCCCCCCCCCC	27.23	19429919
875	Phosphorylation	VTPKSPASSHKSYDG CCCCCCCCCCCCCCC	36.04	19429919

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TSH_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 TSH_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NHP2_DROME	NHP2	physical	14605208
TBB1_DROME	betaTub56D	physical	14605208
WNTG_DROME	wg	genetic	12183379
HTH_DROME	hth	genetic	12183379
SPEN_DROME	spen	genetic	10556062
TIPT_DROME	tio	genetic	15936749
TIPT_DROME	tio	genetic	23404107
ARM_DROME	arm	physical	9707400
PPT1_DROME	Ppt1	physical	25242320

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-750 AND SER-758, ANDMASS SPECTROMETRY.
PubMed: 18327897