E41L5_HUMAN - dbPTM
E41L5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E41L5_HUMAN
UniProt AC Q9HCM4
Protein Name Band 4.1-like protein 5
Gene Name EPB41L5
Organism Homo sapiens (Human).
Sequence Length 733
Subcellular Localization Cytoplasm. Cell junction, adherens junction. Associated with the plasma membrane. Colocalizes with CTNNB1, an adherens junction marker (By similarity)..
Protein Description May contribute to the correct positioning of tight junctions during the establishment of polarity in epithelial cells..
Protein Sequence MLSFFRRTLGRRSMRKHAEKERLREAQRAATHIPAAGDSKSIITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLDCPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGDTKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHHAFFRLRGPVQKSSHRSGFIRLGSRFRYSGKTEYQTTKTNKARRSTSFERRPSKRYSRRTLQMKACATKPEELSVHNNVSTQSNGSQQAWGMRSALPVSPSISSAPVPVEIENLPQSPGTDQHDRKCIPLNIDLLNSPDLLEATIGDVIGASDTMETSQALNDVNVATRLPGLGEPEVEYETLKDTSEKLKQLEMENSPLLSPRSNIDVNINSQEEVVKLTEKCLNNVIESPGLNVMRVPPDFKSNILKAQVEAVHKVTKEDSLLSHKNANVQDAATNSAVLNENNVPLPKESLETLMLITPADSGSVLKEATDELDALLASLTENLIDHTVAPQVSSTSMITPRWIVPQSGAMSNGLAGCEMLLTGKEGHGNKDGISLISPPAPFLVDAVTSSGPILAEEAVLKQKCLLTTEL
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
3Phosphorylation-----MLSFFRRTLG
-----CHHHHHHHHC
22.5024719451
31PhosphorylationREAQRAATHIPAAGD
HHHHHHHHCCCCCCC
21.2528102081
39PhosphorylationHIPAAGDSKSIITCR
CCCCCCCCCEEEEEE
27.6428464451
40 (in isoform 3)Ubiquitination-50.8721890473
40 (in isoform 2)Ubiquitination-50.8721890473
40 (in isoform 1)Ubiquitination-50.8721890473
40UbiquitinationIPAAGDSKSIITCRV
CCCCCCCCEEEEEEE
50.8722817900
40 (in isoform 4)Ubiquitination-50.8721890473
41PhosphorylationPAAGDSKSIITCRVS
CCCCCCCEEEEEEEE
24.1524117733
44PhosphorylationGDSKSIITCRVSLLD
CCCCEEEEEEEEECC
7.8125072903
151UbiquitinationKQDILSGKLDCPFDT
HHHHHCCCCCCCHHH
37.4629901268
223UbiquitinationAETNYLNKAKWLEMY
HHHHHHHHHHHHHHH
49.0729901268
230PhosphorylationKAKWLEMYGVDMHVV
HHHHHHHHCCEEEEE
12.4820736484
276PhosphorylationPKITRLDFKKNKLTL
CCCEEEECCCCEEEE
16.7632645325
278UbiquitinationITRLDFKKNKLTLVV
CEEEECCCCEEEEEE
60.3523000965
347PhosphorylationRLGSRFRYSGKTEYQ
EECCEEEECCCEEEE
21.0428796482
348PhosphorylationLGSRFRYSGKTEYQT
ECCEEEECCCEEEEE
29.5623927012
350UbiquitinationSRFRYSGKTEYQTTK
CEEEECCCEEEEECC
32.0423000965
351PhosphorylationRFRYSGKTEYQTTKT
EEEECCCEEEEECCC
43.3728796482
353PhosphorylationRYSGKTEYQTTKTNK
EECCCEEEEECCCCH
19.1828796482
355PhosphorylationSGKTEYQTTKTNKAR
CCCEEEEECCCCHHH
29.3828796482
356PhosphorylationGKTEYQTTKTNKARR
CCEEEEECCCCHHHC
21.9828796482
364PhosphorylationKTNKARRSTSFERRP
CCCHHHCCCCCCCCC
23.8926699800
365PhosphorylationTNKARRSTSFERRPS
CCHHHCCCCCCCCCC
35.3125954137
366PhosphorylationNKARRSTSFERRPSK
CHHHCCCCCCCCCCC
26.7630576142
372PhosphorylationTSFERRPSKRYSRRT
CCCCCCCCCCCCCCC
28.1423882029
376PhosphorylationRRPSKRYSRRTLQMK
CCCCCCCCCCCEEEH
21.2224719451
387PhosphorylationLQMKACATKPEELSV
EEEHHHCCCHHHEEC
47.1928348404
393PhosphorylationATKPEELSVHNNVST
CCCHHHEECCCCCCC
25.3028348404
399PhosphorylationLSVHNNVSTQSNGSQ
EECCCCCCCCCCCCC
23.8928348404
400PhosphorylationSVHNNVSTQSNGSQQ
ECCCCCCCCCCCCCC
31.5628348404
402PhosphorylationHNNVSTQSNGSQQAW
CCCCCCCCCCCCCCC
43.1628348404
405PhosphorylationVSTQSNGSQQAWGMR
CCCCCCCCCCCCCCC
24.3028348404
413PhosphorylationQQAWGMRSALPVSPS
CCCCCCCCCCCCCCC
25.8428102081
418 (in isoform 2)Phosphorylation-15.8119276368
418PhosphorylationMRSALPVSPSISSAP
CCCCCCCCCCCCCCC
15.8125159151
420PhosphorylationSALPVSPSISSAPVP
CCCCCCCCCCCCCCC
27.8325159151
422PhosphorylationLPVSPSISSAPVPVE
CCCCCCCCCCCCCEE
25.4530266825
423PhosphorylationPVSPSISSAPVPVEI
CCCCCCCCCCCCEEE
34.6230266825
431UbiquitinationAPVPVEIENLPQSPG
CCCCEEEECCCCCCC
38.9323000965
436UbiquitinationEIENLPQSPGTDQHD
EEECCCCCCCCCHHC
24.2923000965
436 (in isoform 2)Phosphorylation-24.2922210691
436PhosphorylationEIENLPQSPGTDQHD
EEECCCCCCCCCHHC
24.2930266825
438UbiquitinationENLPQSPGTDQHDRK
ECCCCCCCCCHHCCC
47.3621890473
439PhosphorylationNLPQSPGTDQHDRKC
CCCCCCCCCHHCCCE
35.5530266825
439 (in isoform 2)Phosphorylation-35.5522210691
466UbiquitinationLLEATIGDVIGASDT
HHHHHHHHHHCCCCH
25.6323000965
470UbiquitinationTIGDVIGASDTMETS
HHHHHHCCCCHHHHH
7.9723000965
476 (in isoform 2)Phosphorylation-18.4728442448
477 (in isoform 2)Phosphorylation-10.5128442448
491UbiquitinationNVATRLPGLGEPEVE
CHHHCCCCCCCCCCC
51.4021890473
496UbiquitinationLPGLGEPEVEYETLK
CCCCCCCCCCCEECC
43.6122817900
499PhosphorylationLGEPEVEYETLKDTS
CCCCCCCCEECCCHH
21.2725884760
501PhosphorylationEPEVEYETLKDTSEK
CCCCCCEECCCHHHH
37.9026471730
503UbiquitinationEVEYETLKDTSEKLK
CCCCEECCCHHHHHH
67.3923000965
503 (in isoform 3)Ubiquitination-67.39-
504UbiquitinationVEYETLKDTSEKLKQ
CCCEECCCHHHHHHH
59.5923000965
507UbiquitinationETLKDTSEKLKQLEM
EECCCHHHHHHHHHH
65.5823000965
508 (in isoform 4)Ubiquitination-61.8321890473
508 (in isoform 3)Ubiquitination-61.8321890473
508UbiquitinationTLKDTSEKLKQLEME
ECCCHHHHHHHHHHH
61.8323000965
508 (in isoform 1)Ubiquitination-61.8321890473
510 (in isoform 1)Ubiquitination-65.0021890473
510 (in isoform 4)Ubiquitination-65.0021890473
510UbiquitinationKDTSEKLKQLEMENS
CCHHHHHHHHHHHCC
65.0023000965
510 (in isoform 3)Ubiquitination-65.0021890473
515UbiquitinationKLKQLEMENSPLLSP
HHHHHHHHCCCCCCC
45.2223000965
517PhosphorylationKQLEMENSPLLSPRS
HHHHHHCCCCCCCCC
12.0130266825
521PhosphorylationMENSPLLSPRSNIDV
HHCCCCCCCCCCCCC
26.4226055452
524PhosphorylationSPLLSPRSNIDVNIN
CCCCCCCCCCCCCCC
41.3330266825
532PhosphorylationNIDVNINSQEEVVKL
CCCCCCCCHHHHHHH
34.8630266825
538UbiquitinationNSQEEVVKLTEKCLN
CCHHHHHHHHHHHHH
55.6723000965
542UbiquitinationEVVKLTEKCLNNVIE
HHHHHHHHHHHHHHH
38.4923000965
550PhosphorylationCLNNVIESPGLNVMR
HHHHHHHCCCCCEEE
17.1030266825
563 (in isoform 4)Ubiquitination-50.3921890473
563 (in isoform 1)Ubiquitination-50.3921890473
563 (in isoform 3)Ubiquitination-50.3921890473
563UbiquitinationMRVPPDFKSNILKAQ
EECCCCHHHHHHHHH
50.3922817900
568UbiquitinationDFKSNILKAQVEAVH
CHHHHHHHHHHHHHH
32.7322817900
576UbiquitinationAQVEAVHKVTKEDSL
HHHHHHHHCCCHHHH
45.0323000965
579 (in isoform 3)Ubiquitination-63.61-
579UbiquitinationEAVHKVTKEDSLLSH
HHHHHCCCHHHHHCC
63.6123000965
582PhosphorylationHKVTKEDSLLSHKNA
HHCCCHHHHHCCCCC
32.0928857561
585PhosphorylationTKEDSLLSHKNANVQ
CCHHHHHCCCCCCHH
37.3925002506
587UbiquitinationEDSLLSHKNANVQDA
HHHHHCCCCCCHHHH
55.1423000965
587 (in isoform 3)Ubiquitination-55.14-
610UbiquitinationENNVPLPKESLETLM
CCCCCCCHHHHCCEE
68.5630230243
620PhosphorylationLETLMLITPADSGSV
HCCEEEECCCCCCHH
14.4128270605
624PhosphorylationMLITPADSGSVLKEA
EEECCCCCCHHHHHH
34.7628270605
626PhosphorylationITPADSGSVLKEATD
ECCCCCCHHHHHHHH
28.3828270605
632PhosphorylationGSVLKEATDELDALL
CHHHHHHHHHHHHHH
30.97-
677 (in isoform 4)Phosphorylation-4.3022617229
700PhosphorylationKDGISLISPPAPFLV
CCCEEEECCCCCCCC
30.0829496963

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

Oops, there are no upstream regulatory protein records of E41L5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E41L5_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 E41L5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CHD9_HUMANCHD9physical
28514442
URFB1_HUMANUHRF1BP1physical
28514442
SET1A_HUMANSETD1Aphysical
28514442
CXXC1_HUMANCXXC1physical
28514442
CWC22_HUMANCWC22physical
28514442
NAF1_HUMANNAF1physical
28514442
BD1L1_HUMANBOD1L1physical
28514442
HECD1_HUMANHECTD1physical
28514442
H2B1O_HUMANHIST1H2BOphysical
28514442
AF9_HUMANMLLT3physical
28514442
BRD2_HUMANBRD2physical
28514442
DCAF5_HUMANDCAF5physical
28514442
FHL2_HUMANFHL2physical
28514442
DCAF8_HUMANDCAF8physical
28514442
NAGK_HUMANNAGKphysical
28514442
FNTA_HUMANFNTAphysical
28514442
CWC27_HUMANCWC27physical
28514442
VANG1_HUMANVANGL1physical
28514442
AFF4_HUMANAFF4physical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
AP3B1_HUMANAP3B1physical
28514442
ASH2L_HUMANASH2Lphysical
28514442
MIB1_HUMANMIB1physical
27510968

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 E41L5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND MASSSPECTROMETRY.

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