dbPTM

IMA3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMA3_HUMAN
UniProt AC	O00629
Protein Name	Importin subunit alpha-3
Gene Name	KPNA4
Organism	Homo sapiens (Human).
Sequence Length	521
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS..
Protein Sequence	MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADNEKLDN ------CCCHHHHHH	25.85	22814378
6	Ubiquitination	--MADNEKLDNQRLK --CCCHHHHHHHHHH	60.95	24816145
16	Ubiquitination	NQRLKNFKNKGRDLE HHHHHHHHHCCCCHH	65.91	24816145
24	Phosphorylation	NKGRDLETMRRQRNE HCCCCHHHHHHHHCH	18.80	18212344
26	Methylation	GRDLETMRRQRNEVV CCCHHHHHHHHCHHH	38.38	115481375
37	Methylation	NEVVVELRKNKRDEH CHHHHHHHHCCCCHH	27.31	115481391
60	Phosphorylation	HEDICEDSDIDGDYR HHHHCCCCCCCCCCE	30.11	29255136
66	Phosphorylation	DSDIDGDYRVQNTSL CCCCCCCCEEECCCH	8.28	23927012
71	Phosphorylation	GDYRVQNTSLEAIVQ CCCEEECCCHHHHHH	4.26	30278072
72	Phosphorylation	DYRVQNTSLEAIVQN CCEEECCCHHHHHHC	26.82	28464451
81	Phosphorylation	EAIVQNASSDNQGIQ HHHHHCCCCCCCCCC	44.13	28176443
82	Phosphorylation	AIVQNASSDNQGIQL HHHHCCCCCCCCCCH	32.74	28464451
97	Ubiquitination	SAVQAARKLLSSDRN HHHHHHHHHHCCCCC	49.40	21890473
100	Phosphorylation	QAARKLLSSDRNPPI HHHHHHHCCCCCCCH	40.40	21712546
101	Phosphorylation	AARKLLSSDRNPPID HHHHHHCCCCCCCHH	40.33	21712546
103	Methylation	RKLLSSDRNPPIDDL HHHHCCCCCCCHHHH	60.55	-
113	Phosphorylation	PIDDLIKSGILPILV CHHHHHHCCCHHHHH	24.87	-
194	Phosphorylation	DGPQCRDYVISLGVV CCHHHHHHHHHHHCH	4.74	28450419
197	Phosphorylation	QCRDYVISLGVVKPL HHHHHHHHHHCHHHH	14.71	28450419
221	Phosphorylation	ITFLRNVTWVMVNLC EEHHHCCCEEEHHHH	19.98	21406692
302	Phosphorylation	HQEVKVQTAALRAVG CCHHHHHHHHHHHHC	19.51	24825855
386	Ubiquitination	KGDFGTQKEAAWAIS CCCCCCHHHHHHHHH	49.51	21890473
441	Sulfoxidation	GLSNILKMAEDEAET HHHHHHHHHHHHHHH	2.82	30846556
474	Phosphorylation	NHENEDIYKLAYEII CCCCHHHHHHHHHHH	16.57	25159151

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 IMA3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMA3_HUMAN !!

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 IMA3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGM2_HUMAN	TGM2	physical	10100610
IMB1_HUMAN	KPNB1	physical	10523667
RCC1_HUMAN	RCC1	physical	17855385
P53_HUMAN	TP53	physical	19927155
CUL4B_HUMAN	CUL4B	physical	19801544
EXO1_HUMAN	EXO1	physical	22222486
DAXX_HUMAN	DAXX	physical	17661348
A4_HUMAN	APP	physical	21832049
AICDA_HUMAN	AICDA	physical	19412186
NACC1_HUMAN	NACC1	physical	22665369
ACLY_HUMAN	ACLY	physical	22863883
PLAP_HUMAN	PLAA	physical	25416956
NUP50_HUMAN	NUP50	physical	25416956
MAT2B_HUMAN	MAT2B	physical	25416956
CYHR1_HUMAN	CYHR1	physical	25416956
ACTZ_HUMAN	ACTR1A	physical	26344197
ACTY_HUMAN	ACTR1B	physical	26344197
CALX_HUMAN	CANX	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
SEC63_HUMAN	SEC63	physical	26344197

Drug and Disease Associations

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

Regulatory Network of IMA3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-56 AND SER-60, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-56 AND SER-60, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.	17081983 [Abstract]