IMA5_HUMAN - dbPTM
IMA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMA5_HUMAN
UniProt AC P52294
Protein Name Importin subunit alpha-5
Gene Name KPNA1
Organism Homo sapiens (Human).
Sequence Length 538
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..
Protein Sequence MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLNQQQYIFQQCEAPMEGFQL
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-------MTTPGKEN
-------CCCCCCCC		8.2222814378
2Acetylation------MTTPGKENF
------CCCCCCCCC		25.1622814378
2Phosphorylation------MTTPGKENF
------CCCCCCCCC		25.1629255136
3Phosphorylation-----MTTPGKENFR
-----CCCCCCCCCC		32.6529255136
6Acetylation--MTTPGKENFRLKS
--CCCCCCCCCCCCC		46.3023749302
6Ubiquitination--MTTPGKENFRLKS
--CCCCCCCCCCCCC		46.30-
13PhosphorylationKENFRLKSYKNKSLN
CCCCCCCCCCCCCCC		31.8126074081
14PhosphorylationENFRLKSYKNKSLNP
CCCCCCCCCCCCCCH		17.0526074081
18PhosphorylationLKSYKNKSLNPDEMR
CCCCCCCCCCHHHHH		23.2026437602
46UbiquitinationKREEQLFKRRNVATA
HHHHHHHHHHCCCCC		60.0721890473
462-HydroxyisobutyrylationKREEQLFKRRNVATA
HHHHHHHHHHCCCCC		60.07-
63PhosphorylationETEEEVMSDGGFHEA
HCHHHHHHCCCCCHH		20.9115489334
93PhosphorylationDMIEMIFSKSPEQQL
HHHHHHHCCCHHHHH		43.6324719451
95PhosphorylationIEMIFSKSPEQQLSA
HHHHHCCCHHHHHHH		38.5921815630
105UbiquitinationQQLSATQKFRKLLSK
HHHHHHHHHHHHHCC		35.4321890473
105AcetylationQQLSATQKFRKLLSK
HHHHHHHHHHHHHCC		35.4326051181
112UbiquitinationKFRKLLSKEPNPPID
HHHHHHCCCCCCCHH		63.46-
124PhosphorylationPIDEVISTPGVVARF
CHHHHHCCHHHHHHH		38.98-
136UbiquitinationARFVEFLKRKENCTL
HHHHHHHHHHCCCEE		35.1421890473
1362-HydroxyisobutyrylationARFVEFLKRKENCTL
HHHHHHHHHHCCCEE		35.14-
136AcetylationARFVEFLKRKENCTL
HHHHHHHHHHCCCEE		35.1426051181
221PhosphorylationPPLLQLFSKQNRLTM
HHHHHHHHHCCCCHH		20.3524719451
222UbiquitinationPLLQLFSKQNRLTMT
HHHHHHHHCCCCHHH		45.08-
237PhosphorylationRNAVWALSNLCRGKS
HHHHHHHHHHHCCCC		1.5721712546
244PhosphorylationSNLCRGKSPPPEFAK
HHHHCCCCCCHHHHC		45.9530266825
310PhosphorylationELLMHNDYKVVSPAL
HHHHCCCHHHHCHHH		4.14-
311UbiquitinationLLMHNDYKVVSPALR
HHHCCCHHHHCHHHH		5.05-
355UbiquitinationSSPKESIKKEACWTI
HCCCHHHHHHHCEEE		38.93-
356UbiquitinationSPKESIKKEACWTIS
CCCHHHHHHHCEEEC		9.3621890473
361PhosphorylationIKKEACWTISNITAG
HHHHHCEEECCCCCC		18.36-
363PhosphorylationKEACWTISNITAGNR
HHHCEEECCCCCCCH		1.8621712546
375PhosphorylationGNRAQIQTVIDANIF
CCHHHHEEHHHCCHH		4.67-
396PhosphorylationLQTAEFRTRKEAAWA
HHHHCHHCHHHHHHH		51.60-
398UbiquitinationTAEFRTRKEAAWAIT
HHCHHCHHHHHHHHH		16.022190698
405PhosphorylationKEAAWAITNATSGGS
HHHHHHHHCCCCCCC		8.4220068231
408PhosphorylationAWAITNATSGGSAEQ
HHHHHCCCCCCCHHH		39.3720068231
409PhosphorylationWAITNATSGGSAEQI
HHHHCCCCCCCHHHH		37.5520068231
412PhosphorylationTNATSGGSAEQIKYL
HCCCCCCCHHHHHHH		59.4820068231
459UbiquitinationRLGEQEAKRNGTGIN
HHCHHHHHHCCCCCC		48.03-
459AcetylationRLGEQEAKRNGTGIN
HHCHHHHHHCCCCCC		48.0325953088
476PhosphorylationCALIEEAYGLDKIEF
HHHHHHHHCCCHHHH		3.8425884760
493PhosphorylationSHENQEIYQKAFDLI
CCCCHHHHHHHHHHH		33.77-
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
18SPhosphorylationKinaseCHEK1O14757
GPS
-KUbiquitinationE3 ubiquitin ligaseRAG1P15918
PMID:19118899
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMA5_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 IMA5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBR5_HUMANUBR5physical
12011095
RAG1_HUMANRAG1physical
8052633
IMB1_HUMANKPNB1physical
10523667
MTG8_HUMANRUNX1T1physical
10951564
CTBL1_HUMANCTNNBL1physical
21385873
CUL4B_HUMANCUL4Bphysical
19801544
HSP74_HUMANHSPA4physical
10964507
STAT1_HUMANSTAT1physical
10964507
IMB1_HUMANKPNB1physical
11032817
NOSIP_HUMANNOSIPphysical
16135813
DCAF8_HUMANDCAF8physical
22500989
IMB1_HUMANKPNB1physical
22939629
AICDA_HUMANAICDAphysical
19412186
SKP2_HUMANSKP2physical
22770219
ORC4_HUMANORC4physical
21988832
GABPA_HUMANGABPAphysical
22863883
TRM61_HUMANTRMT61Aphysical
22863883
TAF9_HUMANTAF9physical
25416956
AN32B_HUMANANP32Bphysical
25416956
NUP50_HUMANNUP50physical
25416956
CLK4_HUMANCLK4physical
25416956
FACD2_HUMANFANCD2physical
26344197
MO4L1_HUMANMORF4L1physical
26344197
MO4L2_HUMANMORF4L2physical
26344197
RAN_HUMANRANphysical
26344197
TCP4_HUMANSUB1physical
26344197
LMNB1_HUMANLMNB1physical
26496610
TRI27_HUMANTRIM27physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
SMRD2_HUMANSMARCD2physical
26496610
VPS72_HUMANVPS72physical
26496610
UBP1_HUMANUSP1physical
26496610
UBP7_HUMANUSP7physical
26496610
RUVB1_HUMANRUVBL1physical
26496610
MCES_HUMANRNMTphysical
26496610
MTA2_HUMANMTA2physical
26496610
NCOR1_HUMANNCOR1physical
26496610
TSSC4_HUMANTSSC4physical
26496610
TADA3_HUMANTADA3physical
26496610
NUP50_HUMANNUP50physical
26496610
RUVB2_HUMANRUVBL2physical
26496610
ADNP_HUMANADNPphysical
26496610
SF3B1_HUMANSF3B1physical
26496610
PHAX_HUMANPHAXphysical
26496610
MBD3_HUMANMBD3physical
26496610
P66A_HUMANGATAD2Aphysical
26496610
SP20H_HUMANSUPT20Hphysical
26496610
CARF_HUMANCDKN2AIPphysical
26496610
P66B_HUMANGATAD2Bphysical
26496610
MTA3_HUMANMTA3physical
26496610
AN32E_HUMANANP32Ephysical
26496610
K2013_HUMANKIAA2013physical
26496610
CL045_HUMANC12orf45physical
26496610
ARID2_HUMANARID2physical
26496610
RBBP4_HUMANRBBP4physical
26491019
IMB1_HUMANKPNB1physical
26491019
PHB2_HUMANPHB2physical
26052702
KPYM_HUMANPKMphysical
23178880
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 IMA5_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.

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