Overview
| Uniprot ID | Q8TEX9 |
| Protein Name | Importin-4 |
| Gene Name | IPO4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 867 |
PLLVCKTKQGCTVAE |
Function
Nuclear transport receptor that mediates nuclear import of proteins, such as histones, RPS3A, TNP2 and VDR (PubMed:11823430, PubMed:16207705, PubMed:17682055, PubMed:21454524, PubMed:30177573). Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430, PubMed:16207705). 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 (PubMed:11823430, PubMed:16207705). 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 (PubMed:11823430). 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 (PubMed:11823430). Mediates the nuclear import of the histone H3-H4 dimer when in complex with ASF1 (ASF1A or ASF1B) (PubMed:21454524, PubMed:29408485, PubMed:36103578). Also mediates the nuclear import of monomeric histones H3.1 and H4 (PubMed:30177573). Mediates the ligand-independent nuclear import of vitamin D receptor (VDR) (PubMed:16207705). In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS (PubMed:12610148)
Protein Sequence
10
MESAGLEQLL
20
RELLLPDTER
30
IRRATEQLQI
40
VLRAPAALPA
50
LCDLLASAAD
60
PQIRQFAAVL
70
TRRRLNTRWR
80
RLAAEQRESL
90
KSLILTALQR
100
ETEHCVSLSL
110
AQLSATIFRK
120
EGLEAWPQLL
130
QLLQHSTHSP
140
HSPEREMGLL
150
LLSVVVTSRP
160
EAFQPHHREL
170
LRLLNETLGE
180
VGSPGLLFYS
190
LRTLTTMAPY
200
LSTEDVPLAR
210
MLVPKLIMAM
220
QTLIPIDEAK
230
ACEALEALDE
240
LLESEVPVIT
250
PYLSEVLTFC
260
LEVARNVALG
270
NAIRIRILCC
280
LTFLVKVKSK
290
ALLKNRLLPP
300
LLHTLFPIVA
310
AEPPPGQLDP
320
EDQDSEEEEL
330
EIELMGETPK
340
HFAVQVVDML
350
ALHLPPEKLC
360
PQLMPMLEEA
370
LRSESPYQRK
380
AGLLVLAVLS
390
DGAGDHIRQR
400
LLPPLLQIVC
410
KGLEDPSQVV
420
RNAALFALGQ
430
FSENLQPHIS
440
SYSREVMPLL
450
LAYLKSVPLG
460
HTHHLAKACY
470
ALENFVENLG
480
PKVQPYLPEL
490
MECMLQLLRN
500
PSSPRAKELA
510
VSALGAIATA
520
AQASLLPYFP
530
AIMEHLREFL
540
LTGREDLQPV
550
QIQSLETLGV
560
LARAVGEPMR
570
PLAEECCQLG
580
LGLCDQVDDP
590
DLRRCTYSLF
600
AALSGLMGEG
610
LAPHLEQITT
620
LMLLSLRSTE
630
GIVPQYDGSS
640
SFLLFDDESD
650
GEEEEELMDE
660
DVEEEDDSEI
670
SGYSVENAFF
680
DEKEDTCAAV
690
GEISVNTSVA
700
FLPYMESVFE
710
EVFKLLECPH
720
LNVRKAAHEA
730
LGQFCCALHK
740
ACQSCPSEPN
750
TAALQAALAR
760
VVPSYMQAVN
770
RERERQVVMA
780
VLEALTGVLR
790
SCGTLTLKPP
800
GRLAELCGVL
810
KAVLQRKTAC
820
QDTDEEEEEE
830
DDDQAEYDAM
840
LLEHAGEAIP
850
ALAAAAGGDS
860
FAPFFAGFLP
870
LLVCKTKQGC
880
TVAEKSFAVG
890
TLAETIQGLG
900
AASAQFVSRL
910
LPVLLSTAQE
920
ADPEVRSNAI
930
FGMGVLAEHG
940
GHPAQEHFPK
950
LLGLLFPLLA
960
RERHDRVRDN
970
ICGALARLLM
980
ASPTRKPEPQ
990
VLAALLHALP
1000
LKEDLEEWVT
1010
IGRLFSFLYQ
1020
SSPDQVIDVA
1030
PELLRICSLI
1040
LADNKIPPDT
1050
KAALLLLLTF
1060
LAKQHTDSFQ
1070
AALGSLPVDK
1080
AQELQAVLGL
S
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0032991 |
protein-containing complex |
| Molecular Function |
GO:0061608 |
nuclear import signal receptor activity |
| Molecular Function |
GO:0008139 |
nuclear localization sequence binding |
| Molecular Function |
GO:0031267 |
small GTPase binding |
| Biological Process |
GO:0006606 |
protein import into nucleus |
| Biological Process |
GO:0034504 |
protein localization to nucleus |
Reference
[1] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.