Search Results
Overview
| Uniprot ID | A0A287BFZ2 |
|---|---|
| Protein Name | Protein 4.1 |
| Gene Name | EPB41L2 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 232 | CDLEKRAKGQVLFDK |
| 270 | KNWVDPAKEIKRQLR |
| 373 | EKVAELYKTHRGLSP |
| 451 | KRSNFYIKVRPAELE |
| 479 | RAAKRLWKVCVEHHT |
| 500 | PEPPPKAKFLTLGSK |
| 507 | KFLTLGSKFRYSGRT |
| 594 | RDVRSLAKAPPVQYI |
| 935 | QRTEISTKEVPIVQT |
| 989 | THITKTVKGGISETR |
Function
Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase
Protein Sequence
10
MTTEVGSASE
20
VKKESDQLGA
30
DATKEKPKEV
40
AENQQNQSSD
50
PEEEKGSQSS
60
PPAESQSSSR
70
PQKKERDPSG
80
SRGISRFIPP
90
WLKKQKSYTL
100
VVAKDGGDKK
110
EPTQAVVEEQ
120
ILAKEESLPE
130
EGKQAKGDAA
140
EMALQKQQQI
150
KVDVKEEKPP
160
VSSLEMQPVE
170
EVSKEREEEK
180
GKEIQEDTLD
190
EAAKRETKEV
200
QTNELKAEKA
210
SQKATKKTKT
220
VQCKVTLLDG
230
TEYSCDLEKR
240
AKGQVLFDKV
250
CEHLNLLEKD
260
YFGLVFQENP
270
EQKNWVDPAK
280
EIKRQLRNLP
290
WLFTFNVKFY
300
PPDPSQLTED
310
ITRYFLCLQL
320
RQDIASGRLP
330
CSLMTHALLG
340
SYTLQAELGD
350
YDPEEHDSND
360
LSDFQFAPTQ
370
TKELEEKVAE
380
LYKTHRGLSP
390
AQADSQFLEN
400
AKRLSMYGVD
410
LHHAKDSEGV
420
DIKLGVCANG
430
LLIYKDRLRI
440
NRFAWPKILK
450
ISYKRSNFYI
460
KVRPAELEQF
470
ESTIGFKLPN
480
HRAAKRLWKV
490
CVEHHTFYRL
500
VSPEPPPKAK
510
FLTLGSKFRY
520
SGRTQAQTRQ
530
ASTLIDRPAP
540
HFERTSSKRV
550
SRSLDGAPVG
560
VVDQSLMKDF
570
AGPAGEVSAY
580
GPGVVSPAVV
590
QDGDGRRDVR
600
SLAKAPPVQY
610
IEGKKNSLRV
620
EGDNIYVRHS
630
NLMLEDLDKA
640
QEEILKHQAS
650
ISELKRNFME
660
STPEPRPNEW
670
EKRRITPLSL
680
QTQGSKGDRL
690
FKDIFSMKEK
700
HQMAATRTVE
710
EKAQEADKKR
720
APESEGPCAG
730
ASDAVKSSHE
740
TLNVVEEKKQ
750
AEVGKDERVI
760
TEEVNGKALA
770
PGRGPGEMRK
780
VEPGTQKDST
790
SLSSESSPSS
800
ESEDEDVGEY
810
RPHHQVTEGT
820
IREEQEEEEE
830
VEEAPGPAAK
840
VVEREDPVPA
850
TRPVTHAGAN
860
VSTVETVIQE
870
NVVAPQIPTE
880
KSVNEGVKQD
890
VREDPEDEPQ
900
KVNGEVSHVD
910
IDVLPQVICC
920
SEPPVVKTEM
930
VTISDASQRT
940
EISTKEVPIV
950
QTETKTITYE
960
SPQIDGGAGG
970
DSGTLLTAQT
980
ITSESVSTTT
990
TTHITKTVKG
1000
GISETRIEKR
1010
IVITGDADID
1020
HDQALAQAIR
1030
EAREQHPDMS
1040
VTRVVVHKET
ELEEGDE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005938 | cell cortex |
| Cellular Component | GO:0030054 | cell junction |
| Cellular Component | GO:0008180 | COP9 signalosome |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0042731 | PH domain binding |
| Molecular Function | GO:0030507 | spectrin binding |
| Molecular Function | GO:0005198 | structural molecule activity |
| Biological Process | GO:0031032 | actomyosin structure organization |
| Biological Process | GO:0030866 | cortical actin cytoskeleton organization |
| Biological Process | GO:1904778 | positive regulation of protein localization to cell cortex |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.