IMA7_HUMAN - dbPTM
IMA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMA7_HUMAN
UniProt AC O60684
Protein Name Importin subunit alpha-7
Gene Name KPNA6
Organism Homo sapiens (Human).
Sequence Length 536
Subcellular Localization
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 METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPRVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSVCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSPKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEGKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
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 Orthologous
Protein Cluster
1Acetylation-------METMASPG
-------CCCCCCCC		9.7422814378
3Phosphorylation-----METMASPGKD
-----CCCCCCCCCC		19.4223401153
6Phosphorylation--METMASPGKDNYR
--CCCCCCCCCCCCC		24.3029255136
9UbiquitinationETMASPGKDNYRMKS
CCCCCCCCCCCCCHH		46.3024816145
9AcetylationETMASPGKDNYRMKS
CCCCCCCCCCCCCHH		46.3025953088
12PhosphorylationASPGKDNYRMKSYKN
CCCCCCCCCCHHHCC		23.4026074081
15UbiquitinationGKDNYRMKSYKNNAL
CCCCCCCHHHCCCCC		41.4523503661
16PhosphorylationKDNYRMKSYKNNALN
CCCCCCHHHCCCCCC		31.8128857561
17PhosphorylationDNYRMKSYKNNALNP
CCCCCHHHCCCCCCH		16.5329214152
18UbiquitinationNYRMKSYKNNALNPE
CCCCHHHCCCCCCHH		51.3127667366
18AcetylationNYRMKSYKNNALNPE
CCCCHHHCCCCCCHH		51.318259057
23UbiquitinationSYKNNALNPEEMRRR
HHCCCCCCHHHHHHH		39.2621890473
27SulfoxidationNALNPEEMRRRREEE
CCCCHHHHHHHHHHH		3.7321406390
39UbiquitinationEEEGIQLRKQKREQQ
HHHHHHHHHHHHHHH		24.0024816145
45UbiquitinationLRKQKREQQLFKRRN
HHHHHHHHHHHHHHC		49.6723503661
48UbiquitinationQKREQQLFKRRNVEL
HHHHHHHHHHHCHHH		5.1321890473
49UbiquitinationKREQQLFKRRNVELI
HHHHHHHHHHCHHHH		60.0727667366
54UbiquitinationLFKRRNVELINEEAA
HHHHHCHHHHHHHHH		47.7021890473
79UbiquitinationVSSTTGESVITREMV
HCCCCCCCCHHHHHH		21.8421890473
91PhosphorylationEMVEMLFSDDSDLQL
HHHHHHCCCCCCHHH		36.22-
100PhosphorylationDSDLQLATTQKFRKL
CCCHHHHHHHHHHHH		38.05-
101PhosphorylationSDLQLATTQKFRKLL
CCHHHHHHHHHHHHH		24.93-
106UbiquitinationATTQKFRKLLSKEPS
HHHHHHHHHHCCCCC		57.8423503661
109PhosphorylationQKFRKLLSKEPSPPI
HHHHHHHCCCCCCCH		45.4728857561
110UbiquitinationKFRKLLSKEPSPPID
HHHHHHCCCCCCCHH		73.8721906983
113PhosphorylationKLLSKEPSPPIDEVI
HHHCCCCCCCHHHHH		44.3830266825
115UbiquitinationLSKEPSPPIDEVINT
HCCCCCCCHHHHHCC		51.5021890473
122PhosphorylationPIDEVINTPRVVDRF
CHHHHHCCHHHHHHH		11.0121815630
128MethylationNTPRVVDRFVEFLKR
CCHHHHHHHHHHHHH		26.38115481399
134AcetylationDRFVEFLKRNENCTL
HHHHHHHHHCCCCEE		59.5025953088
134UbiquitinationDRFVEFLKRNENCTL
HHHHHHHHHCCCCEE		59.5023000965
136UbiquitinationFVEFLKRNENCTLQF
HHHHHHHCCCCEEEH		43.1523503661
139UbiquitinationFLKRNENCTLQFEAA
HHHHCCCCEEEHHHH		3.0721890473
140UbiquitinationLKRNENCTLQFEAAW
HHHCCCCEEEHHHHH		34.8721963094
164UbiquitinationSQQTKIVIEAGAVPI
CCCCEEEEECCCHHH		3.2321890473
204PhosphorylationDSSVCRDYVLNCSIL
CCHHHHHHHHCHHHH		6.3620068231
209PhosphorylationRDYVLNCSILNPLLT
HHHHHCHHHHHHHHH		29.1020068231
216PhosphorylationSILNPLLTLLTKSTR
HHHHHHHHHHCCCCC		27.6620068231
219PhosphorylationNPLLTLLTKSTRLTM
HHHHHHHCCCCCHHH		26.5120068231
235PhosphorylationRNAVWALSNLCRGKN
HHHHHHHHHHHCCCC		21.7321712546
238GlutathionylationVWALSNLCRGKNPPP
HHHHHHHHCCCCCCH		6.7022555962
241UbiquitinationLSNLCRGKNPPPEFA
HHHHHCCCCCCHHHH		47.1032142685
249UbiquitinationNPPPEFAKVSPCLPV
CCCHHHHCCCCCHHH		48.87-
253GlutathionylationEFAKVSPCLPVLSRL
HHHCCCCCHHHHHHH		5.3722555962
293PhosphorylationKIQAVIDSGVCRRLV
HHHHHHHHHHHHHHH		23.2332142685
296GlutathionylationAVIDSGVCRRLVELL
HHHHHHHHHHHHHHH		2.0922555962
308PhosphorylationELLMHNDYKVASPAL
HHHHCCCHHHHCHHH		16.81-
349UbiquitinationLHLLSSPKESIRKEA
HHHHHCCCHHHHHHH		67.0723000965
354MalonylationSPKESIRKEACWTIS
CCCHHHHHHHCEEEC		48.2526320211
354UbiquitinationSPKESIRKEACWTIS
CCCHHHHHHHCEEEC		48.2521890473
359PhosphorylationIRKEACWTISNITAG
HHHHHCEEECCCCCC		17.89-
361PhosphorylationKEACWTISNITAGNR
HHHCEEECCCCCCCH		18.1421712546
379UbiquitinationQAVIDANIFPVLIEI
HHHHHCCHHHHHHHH		4.4123000965
384UbiquitinationANIFPVLIEILQKAE
CCHHHHHHHHHHHCC		2.9321890473
396MalonylationKAEFRTRKEAAWAIT
HCCCCCHHHHHHHHH		51.6026320211
396UbiquitinationKAEFRTRKEAAWAIT
HCCCCCHHHHHHHHH		51.6022817900
401UbiquitinationTRKEAAWAITNATSG
CHHHHHHHHHCCCCC		8.2621890473
426UbiquitinationSLGCIKPLCDLLTVM
HCCCHHHHHHHHHHC		2.7722817900
457AcetylationRLGEQEGKRSGSGVN
HHHHHCCCCCCCCCC		42.5125953088
457UbiquitinationRLGEQEGKRSGSGVN
HHHHHCCCCCCCCCC		42.5132142685
459PhosphorylationGEQEGKRSGSGVNPY
HHHCCCCCCCCCCCC		40.5729632367
461PhosphorylationQEGKRSGSGVNPYCG
HCCCCCCCCCCCCCH		40.5929632367
466PhosphorylationSGSGVNPYCGLIEEA
CCCCCCCCCHHHHHH		8.2429632367
474PhosphorylationCGLIEEAYGLDKIEF
CHHHHHHHCCCHHHH		22.85-
478UbiquitinationEEAYGLDKIEFLQSH
HHHHCCCHHHHHHCC		49.5329967540
491PhosphorylationSHENQEIYQKAFDLI
CCCCHHHHHHHHHHH		11.83-
509PhosphorylationFGVEDDDSSLAPQVD
HCCCCCCCCCCCCCC		33.9622468782
510PhosphorylationGVEDDDSSLAPQVDE
CCCCCCCCCCCCCCH		35.2322468782
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 IMA7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMA7_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 IMA7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMB1_HUMANKPNB1physical
10523667
KEAP1_HUMANKEAP1physical
21383067
ZN131_HUMANZNF131physical
17306895
IMB1_HUMANKPNB1physical
22939629
SKP2_HUMANSKP2physical
22770219
IMA1_HUMANKPNA2physical
22863883
KAP2_HUMANPRKAR2Aphysical
22863883
TTC1_HUMANTTC1physical
22863883
EXOS4_HUMANEXOSC4physical
26344197
HDAC1_HUMANHDAC1physical
26344197
IPO5_HUMANIPO5physical
26344197
MO4L1_HUMANMORF4L1physical
26344197
MO4L2_HUMANMORF4L2physical
26344197
NOP56_HUMANNOP56physical
26344197
ANM1_HUMANPRMT1physical
26344197
PRS7_HUMANPSMC2physical
26344197
RAN_HUMANRANphysical
26344197
RNBP6_HUMANRANBP6physical
26344197
RL11_HUMANRPL11physical
26344197
PHB2_HUMANPHB2physical
26052702
MDM2_HUMANMDM2physical
28196907
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 IMA7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-3 AND SER-6, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-3 AND SER-6, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.

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