dbPTM

IMA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMA4_HUMAN
UniProt AC	O00505
Protein Name	Importin subunit alpha-4
Gene Name	KPNA3
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. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9..
Protein Sequence	MAENPSLENHRIKSFKNKGRDVETMRRHRNEVTVELRKNKRDEHLLKKRNVPQEESLEDSDVDADFKAQNVTLEAILQNATSDNPVVQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVKCLERDDNPSLQFEAAWALTNIASGTSAQTQAVVQSNAVPLFLRLLRSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVIVNLCRNKDPPPPMETVQEILPALCVLIYHTDINILVDTVWALSYLTDGGNEQIQMVIDSGVVPFLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDVLSHFPNLLSHPKEKINKEAVWFLSNITAGNQQQVQAVIDAGLIPMIIHQLAKGDFGTQKEAAWAISNLTISGRKDQVEYLVQQNVIPPFCNLLSVKDSQVVQVVLDGLKNILIMAGDEASTIAEIIEECGGLEKIEVLQQHENEDIYKLAFEIIDQYFSGDDIDEDPCLIPEATQGGTYNFDPTANLQTKEFNF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAENPSLEN ------CCCCCCCCC	28.47	19413330
6	Phosphorylation	--MAENPSLENHRIK --CCCCCCCCCCCHH	68.35	25159151
14	Phosphorylation	LENHRIKSFKNKGRD CCCCCHHHHHHCCCC	58.69	29496963
24	Phosphorylation	NKGRDVETMRRHRNE HCCCCHHHHHHHHCC	24.23	18212344
33	Phosphorylation	RRHRNEVTVELRKNK HHHHCCHHHHHHHCC	1.95	26437602
56	Phosphorylation	RNVPQEESLEDSDVD CCCCCHHHCCCCCCC	2.23	29255136
60	Phosphorylation	QEESLEDSDVDADFK CHHHCCCCCCCHHHH	17.74	19664994
72	Phosphorylation	DFKAQNVTLEAILQN HHHHHCCCHHHHHHC	31.59	26074081
81	Phosphorylation	EAILQNATSDNPVVQ HHHHHCCCCCCCCCH	45.86	28464451
82	Phosphorylation	AILQNATSDNPVVQL HHHHCCCCCCCCCHH	37.86	28464451
97	Ubiquitination	SAVQAARKLLSSDRN HHHHHHHHHHCCCCC	49.40	21890473
97	Ubiquitination	SAVQAARKLLSSDRN HHHHHHHHHHCCCCC	49.40	21890473
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 CHHHHHHCCHHHHHH	24.87	21712546
121	Ubiquitination	GILPILVKCLERDDN CHHHHHHHHHCCCCC	13.65	-
194	Phosphorylation	DGPQCRDYVISLGVV CCHHHHHHHHHHHCH	4.74	28450419
197	Phosphorylation	QCRDYVISLGVVKPL HHHHHHHHHHCHHHH	14.71	28450419
302	Phosphorylation	HQEVKVQTAALRAVG CCHHHHHHHHHHHHC	19.51	24825855
386	Ubiquitination	KGDFGTQKEAAWAIS CCCCCCHHHHHHHHH	49.51	21890473
386	Ubiquitination	KGDFGTQKEAAWAIS CCCCCCHHHHHHHHH	49.51	21890473
386	Ubiquitination	KGDFGTQKEAAWAIS CCCCCCHHHHHHHHH	49.51	21890473
421	Phosphorylation	PPFCNLLSVKDSQVV CCCCCEECCCCHHHH	28.77	24719451
423	Ubiquitination	FCNLLSVKDSQVVQV CCCEECCCCHHHHHH	41.95	-
425	Phosphorylation	NLLSVKDSQVVQVVL CEECCCCHHHHHHHH	9.80	21659604
474	Phosphorylation	QHENEDIYKLAFEII HCCCCCHHHHHHHHH	16.57	-
484	Phosphorylation	AFEIIDQYFSGDDID HHHHHHHHHCCCCCC	5.94	24275569
486	Phosphorylation	EIIDQYFSGDDIDED HHHHHHHCCCCCCCC	33.86	24275569
506	Phosphorylation	EATQGGTYNFDPTAN CCCCCCCCCCCCCCC	13.71	22817900

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 IMA4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMA4_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 IMA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FA50B_HUMAN	FAM50B	physical	16189514
IMB1_HUMAN	KPNB1	physical	10523667
RCC1_HUMAN	RCC1	physical	10744690
IMB1_HUMAN	KPNB1	physical	9435235
ZN131_HUMAN	ZNF131	physical	17306895
NACC1_HUMAN	NACC1	physical	22665369
MYOD1_HUMAN	MYOD1	physical	21988832
NF2L2_HUMAN	NFE2L2	physical	21988832
IMA7_HUMAN	KPNA6	physical	22863883
MCM6_HUMAN	MCM6	physical	22863883
MMS19_HUMAN	MMS19	physical	22863883
MTA1_HUMAN	MTA1	physical	25416956
DDX21_HUMAN	DDX21	physical	25416956
ZBT24_HUMAN	ZBTB24	physical	25416956
TSSC4_HUMAN	TSSC4	physical	25416956
NUP50_HUMAN	NUP50	physical	25416956
MAT2B_HUMAN	MAT2B	physical	25416956
ZCH10_HUMAN	ZCCHC10	physical	25416956
RPR1A_HUMAN	RPRD1A	physical	25416956
APOL6_HUMAN	APOL6	physical	25416956
SC5AB_HUMAN	SLC5A11	physical	25416956
TEX37_HUMAN	TEX37	physical	25416956
ACTZ_HUMAN	ACTR1A	physical	26344197
CALX_HUMAN	CANX	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
IPO8_HUMAN	IPO8	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
TMCO1_HUMAN	TMCO1	physical	26344197
RBBP4_HUMAN	RBBP4	physical	26491019

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 IMA4_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, 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-60, AND MASSSPECTROMETRY.	19690332 [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-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]