IMA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IMA_DROME
• UniProt AC: P52295
• Protein Name: Importin subunit alpha
• Gene Name: Pen
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 522
• Subcellular Localization: Cytoplasm. Nucleus. Shuttles between the cytoplasm and nucleus in a cell cycle-dependent manner.
• Protein Description: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).; It is required for normal cell proliferation and may serve as an adapter molecule to form complexes with other proteins. May act as a tumor suppressor in hematopoietic cells. May play a role in the nuclear import of karyophilic proteins and some of these may be required for the normal transmission and function of proliferative signals in the cells..
• Protein Sequence: MSKADSNSRQGSYKANSINTQDSRMRRHEVTIELRKSKKEDQMFKRRNINDEDLTSPLKELNGQSPVQLSVDEIVAAMNSEDQERQFLGMQSARKMLSRERNPPIDLMIGHGIVPICIRFLQNTNNSMLQFEAAWALTNIASGTSDQTRCVIEHNAVPHFVALLQSKSMNLAEQAVWALGNIAGDGAAARDIVIHHNVIDGILPLINNETPLSFLRNIVWLMSNLCRNKNPSPPFDQVKRLLPVLSQLLLSQDIQVLADACWALSYVTDDDNTKIQAVVDSDAVPRLVKLLQMDEPSIIVPALRSVGNIVTGTDQQTDVVIASGGLPRLGLLLQHNKSNIVKEAAWTVSNITAGNQKQIQAVIQAGIFQQLRTVLEKGDFKAQKEAAWAVTNTTTSGTPEQIVDLIEKYKILKPFIDLLDTKDPRTIKVVQTGLSNLFALAEKLGGTENLCLMVEEMGGLDKLETLQQHENEEVYKKAYAIIDTYFSNGDDEAEQELAPQEVNGALEFNATQPKAPEGGYTF

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
12	Phosphorylation	DSNSRQGSYKANSIN CCCCCCCCCCCCCCC	18.34	27626673
17	Phosphorylation	QGSYKANSINTQDSR CCCCCCCCCCCCCHH	23.29	19429919
20	Phosphorylation	YKANSINTQDSRMRR CCCCCCCCCCHHHHH	31.89	21082442
23	Phosphorylation	NSINTQDSRMRRHEV CCCCCCCHHHHHHHH	20.40	25749252
31	Phosphorylation	RMRRHEVTIELRKSK HHHHHHHEEHHHHCH	13.02	22817900
37	Phosphorylation	VTIELRKSKKEDQMF HEEHHHHCHHHHHCH	42.39	22817900
55	Phosphorylation	NINDEDLTSPLKELN CCCHHHCCHHHHHHC	40.39	30478224
56	Phosphorylation	INDEDLTSPLKELNG CCHHHCCHHHHHHCC	35.22	19429919
65	Phosphorylation	LKELNGQSPVQLSVD HHHHCCCCCEECCHH	28.56	22817900
338	Phosphorylation	LLLQHNKSNIVKEAA HHHHCCCCHHHHHHH	36.79	22817900

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IMA_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 IMA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DEI_DROME	tx	physical	14605208
LAM0_DROME	Lam	physical	14605208
RS18_DROME	RpS18	physical	14605208
NU153_DROME	Nup153	physical	22036573
CCD1P_DROME	Cyp12d1-p	physical	22036573
IMB_DROME	Fs(2)Ket	physical	10882518

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-12; SER-56 AND SER-65,AND MASS SPECTROMETRY.
PubMed: 18327897

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.
PubMed: 17372656