IPO4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IPO4_HUMAN
• UniProt AC: Q8TEX9
• Protein Name: Importin-4
• Gene Name: IPO4
• Organism: Homo sapiens (Human).
• Sequence Length: 1081
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin 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 the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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 (By similarity). Mediates the nuclear import of RPS3A. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS..
• Protein Sequence: MESAGLEQLLRELLLPDTERIRRATEQLQIVLRAPAALPALCDLLASAADPQIRQFAAVLTRRRLNTRWRRLAAEQRESLKSLILTALQRETEHCVSLSLAQLSATIFRKEGLEAWPQLLQLLQHSTHSPHSPEREMGLLLLSVVVTSRPEAFQPHHRELLRLLNETLGEVGSPGLLFYSLRTLTTMAPYLSTEDVPLARMLVPKLIMAMQTLIPIDEAKACEALEALDELLESEVPVITPYLSEVLTFCLEVARNVALGNAIRIRILCCLTFLVKVKSKALLKNRLLPPLLHTLFPIVAAEPPPGQLDPEDQDSEEEELEIELMGETPKHFAVQVVDMLALHLPPEKLCPQLMPMLEEALRSESPYQRKAGLLVLAVLSDGAGDHIRQRLLPPLLQIVCKGLEDPSQVVRNAALFALGQFSENLQPHISSYSREVMPLLLAYLKSVPLGHTHHLAKACYALENFVENLGPKVQPYLPELMECMLQLLRNPSSPRAKELAVSALGAIATAAQASLLPYFPAIMEHLREFLLTGREDLQPVQIQSLETLGVLARAVGEPMRPLAEECCQLGLGLCDQVDDPDLRRCTYSLFAALSGLMGEGLAPHLEQITTLMLLSLRSTEGIVPQYDGSSSFLLFDDESDGEEEEELMDEDVEEEDDSEISGYSVENAFFDEKEDTCAAVGEISVNTSVAFLPYMESVFEEVFKLLECPHLNVRKAAHEALGQFCCALHKACQSCPSEPNTAALQAALARVVPSYMQAVNRERERQVVMAVLEALTGVLRSCGTLTLKPPGRLAELCGVLKAVLQRKTACQDTDEEEEEEDDDQAEYDAMLLEHAGEAIPALAAAAGGDSFAPFFAGFLPLLVCKTKQGCTVAEKSFAVGTLAETIQGLGAASAQFVSRLLPVLLSTAQEADPEVRSNAIFGMGVLAEHGGHPAQEHFPKLLGLLFPLLARERHDRVRDNICGALARLLMASPTRKPEPQVLAALLHALPLKEDLEEWVTIGRLFSFLYQSSPDQVIDVAPELLRICSLILADNKIPPDTKAALLLLLTFLAKQHTDSFQAALGSLPVDKAQELQAVLGLS

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
1	Sulfoxidation	-------MESAGLEQ -------CCCCHHHH	40.72	28183972
1	Acetylation	-------MESAGLEQ -------CCCCHHHH	40.72	22223895
18	Phosphorylation	RELLLPDTERIRRAT HHHCCCCHHHHHHHH	25.81	-
42	S-nitrosylation	PAALPALCDLLASAA CCHHHHHHHHHHHCC	3.63	19483679
42	Glutathionylation	PAALPALCDLLASAA CCHHHHHHHHHHHCC	3.63	22555962
42	S-nitrosocysteine	PAALPALCDLLASAA CCHHHHHHHHHHHCC	3.63	-
79	Phosphorylation	LAAEQRESLKSLILT HHHHHHHHHHHHHHH	43.20	20873877
81 (in isoform 2)	Ubiquitination	-	53.12	21906983
81 (in isoform 1)	Ubiquitination	-	53.12	21906983
81	Ubiquitination	AEQRESLKSLILTAL HHHHHHHHHHHHHHH	53.12	21906983
82	Phosphorylation	EQRESLKSLILTALQ HHHHHHHHHHHHHHH	26.40	20873877
86	Phosphorylation	SLKSLILTALQRETE HHHHHHHHHHHHHHH	20.51	20873877
148	Phosphorylation	LLSVVVTSRPEAFQP HHHHHHCCCCHHCCH	33.94	24719451
173	Phosphorylation	ETLGEVGSPGLLFYS HHHCCCCCHHHHHHH	22.44	-
180	Phosphorylation	SPGLLFYSLRTLTTM CHHHHHHHHHHHHHC	12.21	24719451
187	Sulfoxidation	SLRTLTTMAPYLSTE HHHHHHHCCCCCCCC	2.73	28183972
315	Phosphorylation	LDPEDQDSEEEELEI CCCCCCCCHHHHHHH	41.07	28464451
370	Ubiquitination	SESPYQRKAGLLVLA CCCHHHHHHCCHHHH	31.14	-
370 (in isoform 2)	Ubiquitination	-	31.14	-
401	Ubiquitination	PLLQIVCKGLEDPSQ HHHHHHHCCCCCHHH	56.49	-
401 (in isoform 2)	Ubiquitination	-	56.49	-
445	Ubiquitination	PLLLAYLKSVPLGHT HHHHHHHHCCCCCCH	36.41	-
445 (in isoform 2)	Ubiquitination	-	36.41	-
452	Phosphorylation	KSVPLGHTHHLAKAC HCCCCCCHHHHHHHH	14.81	29457462
457	Ubiquitination	GHTHHLAKACYALEN CCHHHHHHHHHHHHH	45.40	-
457 (in isoform 2)	Ubiquitination	-	45.40	-
544	Phosphorylation	LQPVQIQSLETLGVL CCCEECCHHHHHHHH	29.78	25693802
547	Phosphorylation	VQIQSLETLGVLARA EECCHHHHHHHHHHH	33.82	25693802
586	Phosphorylation	DPDLRRCTYSLFAAL CCCHHHHHHHHHHHH	17.84	-
708	S-nitrosylation	EVFKLLECPHLNVRK HHHHHHCCCCCCHHH	2.31	19483679
708	S-nitrosocysteine	EVFKLLECPHLNVRK HHHHHHCCCCCCHHH	2.31	-
715 (in isoform 2)	Ubiquitination	-	45.72	-
715	Ubiquitination	CPHLNVRKAAHEALG CCCCCHHHHHHHHHH	45.72	-
730 (in isoform 2)	Ubiquitination	-	52.27	-
730	Ubiquitination	QFCCALHKACQSCPS HHHHHHHHHHHCCCC	52.27	-
754	Phosphorylation	ALARVVPSYMQAVNR HHHHHHHHHHHHHCH	22.94	-
755	Phosphorylation	LARVVPSYMQAVNRE HHHHHHHHHHHHCHH	6.28	-
769	Sulfoxidation	ERERQVVMAVLEALT HHHHHHHHHHHHHHH	1.93	28183972
788 (in isoform 2)	Ubiquitination	-	43.88	-
788	Acetylation	SCGTLTLKPPGRLAE HCCCEECCCCCHHHH	43.88	27452117
788	Ubiquitination	SCGTLTLKPPGRLAE HCCCEECCCCCHHHH	43.88	-
801 (in isoform 2)	Ubiquitination	-	33.76	21906983
801	Acetylation	AELCGVLKAVLQRKT HHHHHHHHHHHHHHC	33.76	26051181
801	Ubiquitination	AELCGVLKAVLQRKT HHHHHHHHHHHHHHC	33.76	2190698
801 (in isoform 1)	Ubiquitination	-	33.76	21906983
813	Phosphorylation	RKTACQDTDEEEEEE HHCCCCCCCHHHHCC	21.30	27362937
827	Phosphorylation	EDDDQAEYDAMLLEH CCCCHHHHHHHHHHH	16.42	22468782
865	Ubiquitination	FLPLLVCKTKQGCTV HHHHEEECCCCCCCH	51.80	-
867	Ubiquitination	PLLVCKTKQGCTVAE HHEEECCCCCCCHHH	30.13	-
875	Ubiquitination	QGCTVAEKSFAVGTL CCCCHHHHHHHHHHH	40.93	-
875 (in isoform 2)	Ubiquitination	-	40.93	-
972	Phosphorylation	LARLLMASPTRKPEP HHHHHHCCCCCCCCH	16.91	24732914
974	Phosphorylation	RLLMASPTRKPEPQV HHHHCCCCCCCCHHH	49.15	24732914
1028	Phosphorylation	PELLRICSLILADNK HHHHHHHHHHHCCCC	18.97	-
1081	Phosphorylation	LQAVLGLS------- HHHHHCCC-------	36.06	30576142

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IPO4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IPO4_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IPO4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASF1B_HUMAN	ASF1B	physical	20953179
HAT1_HUMAN	HAT1	physical	20953179
CEBPD_HUMAN	CEBPD	physical	20805509
FACD2_HUMAN	FANCD2	physical	20805509
NXF1_HUMAN	NXF1	physical	21965294
A4_HUMAN	APP	physical	21832049
IPO5_HUMAN	IPO5	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
TR112_HUMAN	TRMT112	physical	22863883
ATPB_HUMAN	ATP5B	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
TERA_HUMAN	VCP	physical	26344197
STOM_HUMAN	STOM	physical	27173435

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.

Related Literatures of Post-Translational Modification

Acetylation

"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, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND MASSSPECTROMETRY.
PubMed: 16964243