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Overview

Uniprot IDP11171
Protein NameProtein 4.1
Gene NameEPB41
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
499 TDTIPKSKFLALGSK
808 TQITKTVKGGISETR

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 (PubMed:23870127)

Protein Sequence

10 MTTEKSLVTE 20 AENSQHQQKE 30 EGEEAINSGQ 40 QEPQQEESCQ 50 TAAEGDNWCE 60 QKLKASNGDT 70 PTHEDLTKNK 80 ERTSESRGLS 90 RLFSSFLKRP 100 KSQVSEEEGK 110 EVESDKEKGE 120 GGQKEIEFGT 130 SLDEEIILKA 140 PIAAPEPELK 150 TDPSLDLHSL 160 SSAETQPAQE 170 ELREDPDFEI 180 KEGEGLEECS 190 KIEVKEESPQ 200 SKAETELKAS 210 QKPIRKHRNM 220 HCKVSLLDDT 230 VYECVVEKHA 240 KGQDLLKRVC 250 EHLNLLEEDY 260 FGLAIWDNAT 270 SKTWLDSAKE 280 IKKQVRGVPW 290 NFTFNVKFYP 300 PDPAQLTEDI 310 TRYYLCLQLR 320 QDIVAGRLPC 330 SFATLALLGS 340 YTIQSELGDY 350 DPELHGVDYV 360 SDFKLAPNQT 370 KELEEKVMEL 380 HKSYRSMTPA 390 QADLEFLENA 400 KKLSMYGVDL 410 HKAKDLEGVD 420 IILGVCSSGL 430 LVYKDKLRIN 440 RFPWPKVLKI 450 SYKRSSFFIK 460 IRPGEQEQYE 470 STIGFKLPSY 480 RAAKKLWKVC 490 VEHHTFFRLT 500 STDTIPKSKF 510 LALGSKFRYS 520 GRTQAQTRQA 530 SALIDRPAPH 540 FERTASKRAS 550 RSLDGAAAVD 560 SADRSPRPTS 570 APAITQGQVA 580 EGGVLDASAK 590 KTVVPKAQKE 600 TVKAEVKKED 610 EPPEQAEPEP 620 TEAWKVEKTH 630 IEVTVPTSNG 640 DQTQKLAEKT 650 EDLIRMRKKK 660 RERLDGENIY 670 IRHSNLMLED 680 LDKSQEEIKK 690 HHASISELKK 700 NFMESVPEPR 710 PSEWDKRLST 720 HSPFRTLNIN 730 GQIPTGEGPP 740 LVKTQTVTIS 750 DNANAVKSEI 760 PTKDVPIVHT 770 ETKTITYEAA 780 QTDDNSGDLD 790 PGVLLTAQTI 800 TSETPSSTTT 810 TQITKTVKGG 820 ISETRIEKRI 830 VITGDADIDH 840 DQVLVQAIKE 850 AKEQHPDMSV 860 TKVVVHQETE IADE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0005938 cell cortex
Cellular Component GO:0030863 cortical cytoskeleton
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0045171 intercellular bridge
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0014731 spectrin-associated cytoskeleton
Molecular Function GO:0005545 1-phosphatidylinositol binding
Molecular Function GO:0003779 actin binding
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0051219 phosphoprotein binding
Molecular Function GO:0030507 spectrin binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0031032 actomyosin structure organization
Biological Process GO:0051301 cell division
Biological Process GO:0030866 cortical actin cytoskeleton organization
Biological Process GO:1904778 positive regulation of protein localization to cell cortex
Biological Process GO:0051924 regulation of calcium ion transport
Biological Process GO:1904478 regulation of intestinal absorption
Biological Process GO:0034405 response to fluid shear stress

Reference

[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.