dbPTM

IMA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMA1_HUMAN
UniProt AC	P52292
Protein Name	Importin subunit alpha-1 {ECO:0000305}
Gene Name	KPNA2 {ECO:0000312\|HGNC:HGNC:6395}
Organism	Homo sapiens (Human).
Sequence Length	529
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..
Protein Sequence	MSTNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLLTAKDTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASLSLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTNENANT ------CCCCCCCCC	41.52	25159151
2	Acetylation	------MSTNENANT ------CCCCCCCCC	41.52	21406692
3	Phosphorylation	-----MSTNENANTP -----CCCCCCCCCH	28.84	25159151
9	Phosphorylation	STNENANTPAARLHR CCCCCCCCHHHHHHH	11.53	29255136
20	Ubiquitination	RLHRFKNKGKDSTEM HHHHHHHCCCCCHHH	49.41	-
22	Ubiquitination	HRFKNKGKDSTEMRR HHHHHCCCCCHHHHH	62.34	33845483
22	Acetylation	HRFKNKGKDSTEMRR HHHHHCCCCCHHHHH	62.34	10801418
24	Phosphorylation	FKNKGKDSTEMRRRR HHHCCCCCHHHHHHH	5.42	28102081
25	Phosphorylation	KNKGKDSTEMRRRRI HHCCCCCHHHHHHHH	27.23	20068231
40	Ubiquitination	EVNVELRKAKKDDQM HHHHHHHHHHHHHHH	50.63	29967540
43	Ubiquitination	VELRKAKKDDQMLKR HHHHHHHHHHHHHHH	47.66	24816145
49	Ubiquitination	KKDDQMLKRRNVSSF HHHHHHHHHCCCCCC	31.63	29967540
54	Phosphorylation	MLKRRNVSSFPDDAT HHHHCCCCCCCCCCC	52.60	22167270
55	Phosphorylation	LKRRNVSSFPDDATS HHHCCCCCCCCCCCC	68.69	22167270
61	Phosphorylation	SSFPDDATSPLQENR CCCCCCCCCCCHHHC	5.14	29255136
62	Phosphorylation	SFPDDATSPLQENRN CCCCCCCCCCHHHCC	3.23	19664994
73	Phosphorylation	ENRNNQGTVNWSVDD HHCCCCCCCCCCHHH	20.31	24732914
77	Phosphorylation	NQGTVNWSVDDIVKG CCCCCCCCHHHHHHC	3.67	24732914
83	Ubiquitination	WSVDDIVKGINSSNV CCHHHHHHCCCCCCH	3.27	21890473
83	Ubiquitination	WSVDDIVKGINSSNV CCHHHHHHCCCCCCH	3.27	21890473
83	Sumoylation	WSVDDIVKGINSSNV CCHHHHHHCCCCCCH	3.27	-
83	Ubiquitination	WSVDDIVKGINSSNV CCHHHHHHCCCCCCH	3.27	21890473
83	Ubiquitination	WSVDDIVKGINSSNV CCHHHHHHCCCCCCH	3.27	21906983
87	Phosphorylation	DIVKGINSSNVENQL HHHHCCCCCCHHHHH	2.54	27050516
88	Phosphorylation	IVKGINSSNVENQLQ HHHCCCCCCHHHHHH	3.79	25159151
102	Ubiquitination	QATQAARKLLSREKQ HHHHHHHHHHHCCCC	23.73	23503661
105	Phosphorylation	QAARKLLSREKQPPI HHHHHHHHCCCCCCC	42.66	15342649
108	Sumoylation	RKLLSREKQPPIDNI HHHHHCCCCCCCHHH	57.84	-
108	Sumoylation	RKLLSREKQPPIDNI HHHHHCCCCCCCHHH	57.84	-
108	Ubiquitination	RKLLSREKQPPIDNI HHHHHCCCCCCCHHH	57.84	21906983
108	Acetylation	RKLLSREKQPPIDNI HHHHHCCCCCCCHHH	57.84	25953088
123	Ubiquitination	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	21890473
123	Ubiquitination	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	21890473
123	Acetylation	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	26051181
123	Sumoylation	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	-
123	Ubiquitination	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	21963094
123	Ubiquitination	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	21890473
123	Sumoylation	IRAGLIPKFVSFLGR HHCCCHHHHHHHHCC	33.45	-
126	Phosphorylation	GLIPKFVSFLGRTDC CCHHHHHHHHCCCCC	26.98	21406692
131	Phosphorylation	FVSFLGRTDCSPIQF HHHHHCCCCCCCCCC	4.44	21712546
145	Phosphorylation	FESAWALTNIASGTS CHHHHHHHCCCCCCC	10.09	21712546
151	Phosphorylation	LTNIASGTSEQTKAV HHCCCCCCCCHHHHH	1.80	21712546
156	Ubiquitination	SGTSEQTKAVVDGGA CCCCCHHHHHHCCCH	34.41	16196087
202	Ubiquitination	VFRDLVIKYGAVDPL HHHHHHHHCCCCCHH	1.72	33845483
203	Phosphorylation	FRDLVIKYGAVDPLL HHHHHHHCCCCCHHH	2.80	-
225	Phosphorylation	MSSLACGYLRNLTWT HHHHHHHHHHHHHHH	29.10	-
230	Phosphorylation	CGYLRNLTWTLSNLC HHHHHHHHHHHHHHH	20.49	21712546
232	Phosphorylation	YLRNLTWTLSNLCRN HHHHHHHHHHHHHCC	8.57	21712546
234	Phosphorylation	RNLTWTLSNLCRNKN HHHHHHHHHHHCCCC	6.78	21712546
240	Ubiquitination	LSNLCRNKNPAPPID HHHHHCCCCCCCCCH	6.70	21890473
240	Ubiquitination	LSNLCRNKNPAPPID HHHHHCCCCCCCCCH	6.70	21890473
240	Ubiquitination	LSNLCRNKNPAPPID HHHHHCCCCCCCCCH	6.70	21890473
240	Ubiquitination	LSNLCRNKNPAPPID HHHHHCCCCCCCCCH	6.70	21963094
240	Sumoylation	LSNLCRNKNPAPPID HHHHHCCCCCCCCCH	6.70	-
255	Phosphorylation	AVEQILPTLVRLLHH HHHHHHHHHHHHHCC	3.17	-
291	Ubiquitination	ERIGMVVKTGVVPQL CEEEEEEECCHHHHH	12.05	21890473
291	Acetylation	ERIGMVVKTGVVPQL CEEEEEEECCHHHHH	12.05	25953088
291	Ubiquitination	ERIGMVVKTGVVPQL CEEEEEEECCHHHHH	12.05	21890473
291	Ubiquitination	ERIGMVVKTGVVPQL CEEEEEEECCHHHHH	12.05	21890473
291	Ubiquitination	ERIGMVVKTGVVPQL CEEEEEEECCHHHHH	12.05	23000965
300	Ubiquitination	GVVPQLVKLLGASEL CHHHHHHHHHCCCCC	37.65	20639865
305	Phosphorylation	LVKLLGASELPIVTP HHHHHCCCCCCCCHH	1.76	27050516
311	Phosphorylation	ASELPIVTPALRAIG CCCCCCCHHHHHHHH	38.74	20068231
348	Ubiquitination	PSLLTNPKTNIQKEA HHHHCCCCCCHHHHH	51.45	23000965
348	Sumoylation	PSLLTNPKTNIQKEA HHHHCCCCCCHHHHH	51.45	-
349	Phosphorylation	SLLTNPKTNIQKEAT HHHCCCCCCHHHHHE	39.70	19651622
353	Ubiquitination	NPKTNIQKEATWTMS CCCCCHHHHHEEEEC	45.92	21890473
353	Ubiquitination	NPKTNIQKEATWTMS CCCCCHHHHHEEEEC	45.92	23000965
353	Ubiquitination	NPKTNIQKEATWTMS CCCCCHHHHHEEEEC	45.92	21890473
353	Acetylation	NPKTNIQKEATWTMS CCCCCHHHHHEEEEC	45.92	23236377
353	Ubiquitination	NPKTNIQKEATWTMS CCCCCHHHHHEEEEC	45.92	21890473
358	Phosphorylation	IQKEATWTMSNITAG HHHHHEEEECHHCCC	11.74	19651622
360	Phosphorylation	KEATWTMSNITAGRQ HHHEEEECHHCCCCH	12.10	21712546
363	Phosphorylation	TWTMSNITAGRQDQI EEEECHHCCCCHHHH	18.14	19651622
388	Ubiquitination	FLVSVLSKADFKTQK HHHHHHHHCCCCCHH	2.34	33845483
392	Ubiquitination	VLSKADFKTQKEAVW HHHHCCCCCHHHHEE	10.85	21906983
392	Acetylation	VLSKADFKTQKEAVW HHHHCCCCCHHHHEE	10.85	25953088
395	Ubiquitination	KADFKTQKEAVWAVT HCCCCCHHHHEEEEE	25.73	22817900
435	Ubiquitination	LLTAKDTKIILVILD HCCCCCCCEEHHHHH	3.97	33845483
459	Ubiquitination	EKLGETEKLSIMIEE HHHCCCHHHHHHHHH	45.72	21963094
483	Phosphorylation	LQNHENESVYKASLS HHCCCCHHHHHHHHH	9.54	20873877
485	Phosphorylation	NHENESVYKASLSLI CCCCHHHHHHHHHHH	48.33	23917254
486	Ubiquitination	HENESVYKASLSLIE CCCHHHHHHHHHHHH	34.61	21890473
486	Ubiquitination	HENESVYKASLSLIE CCCHHHHHHHHHHHH	34.61	21890473
486	Ubiquitination	HENESVYKASLSLIE CCCHHHHHHHHHHHH	34.61	21890473
486	Neddylation	HENESVYKASLSLIE CCCHHHHHHHHHHHH	34.61	32015554
486	Ubiquitination	HENESVYKASLSLIE CCCHHHHHHHHHHHH	34.61	22053931
488	Phosphorylation	NESVYKASLSLIEKY CHHHHHHHHHHHHHH	66.89	29255136
490	Phosphorylation	SVYKASLSLIEKYFS HHHHHHHHHHHHHHC	35.16	30266825
494	Sumoylation	ASLSLIEKYFSVEEE HHHHHHHHHHCCCCC	35.94	-
512	Phosphorylation	NVVPETTSEGYTFQV CCCCCCCCCCEEEEE	34.78	-

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
9	T	Phosphorylation	Kinase	CDK1	P06493	PSP
54	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
62	S	Phosphorylation	Kinase	CDK1	P06493	PSP
105	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
105	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
105	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMA1_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 IMA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SGK1_HUMAN	SGK1	physical	12631736
ITK_HUMAN	ITK	physical	11581171
IMB1_HUMAN	KPNB1	physical	10523667
ARL4A_HUMAN	ARL4A	physical	10980193
PLAG1_HUMAN	PLAG1	physical	11882654
GTR2_HUMAN	SLC2A2	physical	11988093
TF65_HUMAN	RELA	physical	12504098
41_HUMAN	EPB41	physical	10359596
IMB1_HUMAN	KPNB1	physical	9323134
XPO2_HUMAN	CSE1L	physical	9323134
SPI1_SCHPO	spi1	physical	9323134
CTBL1_HUMAN	CTNNBL1	physical	21385873
CUL4B_HUMAN	CUL4B	physical	19801544
MAGH1_HUMAN	MAGEH1	physical	15383276
HAP1_HUMAN	HAP1	physical	15383276
KAISO_HUMAN	ZBTB33	physical	15564377
KAISO_MOUSE	Zbtb33	physical	15564377
ZN131_HUMAN	ZNF131	physical	17306895
CHK2_HUMAN	CHEK2	physical	12909615
A4_HUMAN	APP	physical	21832049
AICDA_HUMAN	AICDA	physical	19412186
ZBT7B_HUMAN	ZBTB7B	physical	21988832
RILP_HUMAN	RILP	physical	21988832
K1C18_HUMAN	KRT18	physical	21988832
RGL2_HUMAN	RGL2	physical	21988832
K2C8_HUMAN	KRT8	physical	21988832
LAMB2_HUMAN	LAMB2	physical	21988832
MYC_HUMAN	MYC	physical	21988832
RBP2_HUMAN	RANBP2	physical	21988832
TF65_HUMAN	RELA	physical	21988832
TRAF1_HUMAN	TRAF1	physical	21988832
SART3_HUMAN	SART3	physical	21988832
MVP_HUMAN	MVP	physical	21988832
TANK_HUMAN	TANK	physical	21988832
SPY1_HUMAN	SPRY1	physical	21988832
MORC3_HUMAN	MORC3	physical	21988832
ZC12A_HUMAN	ZC3H12A	physical	21988832
T22D4_HUMAN	TSC22D4	physical	21988832
ACLY_HUMAN	ACLY	physical	22863883
CSN4_HUMAN	COPS4	physical	22863883
HS90B_HUMAN	HSP90AB1	physical	22863883
IMA3_HUMAN	KPNA4	physical	22863883
ANM1_HUMAN	PRMT1	physical	22863883
MDFI_HUMAN	MDFI	physical	25416956
MLH1_HUMAN	MLH1	physical	25416956
TAD2A_HUMAN	TADA2A	physical	25416956
MAGD1_HUMAN	MAGED1	physical	25416956
HM20A_HUMAN	HMG20A	physical	25416956
NUP50_HUMAN	NUP50	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
NUP62_HUMAN	NUP62	physical	25416956
SRTD3_HUMAN	SERTAD3	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
NMNA1_HUMAN	NMNAT1	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
NUTM1_HUMAN	NUTM1	physical	25416956
IN80E_HUMAN	INO80E	physical	25416956
TBPL2_HUMAN	TBPL2	physical	15234975
RAC1_HUMAN	RAC1	physical	19961560
ACO13_HUMAN	ACOT13	physical	26344197
IMA5_HUMAN	KPNA1	physical	26344197
IMA4_HUMAN	KPNA3	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
IMA7_HUMAN	KPNA6	physical	26344197
PHB2_HUMAN	PHB2	physical	26052702
CDCA2_HUMAN	CDCA2	physical	28514442
NU153_HUMAN	NUP153	physical	28514442
NUP50_HUMAN	NUP50	physical	28514442
IMB1_HUMAN	KPNB1	physical	28514442
RB39B_HUMAN	RAB39B	physical	28514442
RGPD5_HUMAN	RGPD5	physical	28514442

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 IMA1_HUMAN

Related Literatures of Post-Translational Modification