E41LB_HUMAN - dbPTM
E41LB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E41LB_HUMAN
UniProt AC Q9H329
Protein Name Band 4.1-like protein 4B
Gene Name EPB41L4B
Organism Homo sapiens (Human).
Sequence Length 900
Subcellular Localization Cytoplasm . Cell junction, tight junction . Accumulates along apical cell-cell boundaries and is also detected in the cytoplasm in a punctate manner.
Protein Description Up-regulates the activity of the Rho guanine nucleotide exchange factor ARHGEF18 (By similarity). Involved in the regulation of the circumferential actomyosin belt in epithelial cells. [PubMed: 22006950 Promotes cellular adhesion, migration and motility in vitro and may play a role in wound healing]
Protein Sequence MLRFLRRTFGRRSMQRYARGAAGRGAAGLGDERDGGPRGGPAAAASSSALPAAPGGSVFPAGGGPLLTGGAAVHISAAGAAKATLYCRVFLLDGTEVSVDLPKHAKGQDLFDQIVYHLDLVETDYFGLQFLDSAQVAHWLDHAKPIKKQMKIGPAYALHFRVKYYSSEPNNLREEFTRYLFVLQLRHDILSGKLKCPYETAVELAALCLQAELGECELPEHTPELVSEFRFIPNQTEAMEFDIFQRWKECRGKSPAQAELSYLNKAKWLEMYGVDMHVVRGRDGCEYSLGLTPTGILIFEGANKIGLFFWPKITKMDFKKSKLTLVVVEDDDQGREQEHTFVFRLDSARTCKHLWKCAVEHHAFFRLRTPGNSKSNRSDFIRLGSRFRFSGRTEYQATHGSRLRRTSTFERKPSKRYPSRRHSTFKASNPVIAAQLCSKTNPEVHNYQPQYHPNIHPSQPRWHPHSPNVSYPLPSPVLSSSDRLPFGIEENGGTPFLTAASGRHHHQHQHQHQHQHHSNYSLSLTLENKEGPLRSPNSSSKSLTKLSPGTPALFSEAAAHLKKLELETVKAAGPWPPLHININKAEEKKVSEKTLQTPLLPSPVADHVKCNILKAQLENASRVNIQGGKEESPFVNINKKSSLQDASVRSPIPIRVETAQPAVEKPEIKPPRVRKLTRQYSFDEDDLPPDLAEAVGVTTSTTTNTTTAATQVSVPLPSPKVQNVSSPHKSEGKGLLSPGAKSPSDRGGAFTLEPGDLLMDFTEATPLAEPASNPHCAHSRCSPPLSLPMKEETTGVCMYPPIKTRLIKTFPVDTMNPFPDTFTTGPQFTADFRDSKLQCCPGPTSPLIPAATLRPLTETVSTVQTIYTTRKPVSLAASAETLRQELEREKMMKRLLMTEL
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
19MethylationRSMQRYARGAAGRGA
HHHHHHHCCCCCCCC
26.75-
24MethylationYARGAAGRGAAGLGD
HHCCCCCCCCCCCCC
27.18-
164PhosphorylationALHFRVKYYSSEPNN
EEEEEEEECCCCCCC
13.01-
254PhosphorylationWKECRGKSPAQAELS
HHHHCCCCHHHHHHH
28.4325159151
265 (in isoform 2)Ubiquitination-49.0721890473
265 (in isoform 1)Ubiquitination-49.0721890473
265UbiquitinationAELSYLNKAKWLEMY
HHHHHHHHHHHHHHH
49.0721890473
272PhosphorylationKAKWLEMYGVDMHVV
HHHHHHHHCCEEEEE
12.4822817900
369PhosphorylationHAFFRLRTPGNSKSN
CEEEEECCCCCCCCC
39.8926657352
378PhosphorylationGNSKSNRSDFIRLGS
CCCCCCHHHCEECCC
40.9223403867
390PhosphorylationLGSRFRFSGRTEYQA
CCCCEEECCCCEEEE
24.1020873877
393PhosphorylationRFRFSGRTEYQATHG
CEEECCCCEEEECCC
42.4424719451
395PhosphorylationRFSGRTEYQATHGSR
EECCCCEEEECCCCC
11.6628796482
398PhosphorylationGRTEYQATHGSRLRR
CCCEEEECCCCCCCC
15.9627794612
401PhosphorylationEYQATHGSRLRRTST
EEEECCCCCCCCCCC
22.1225849741
406PhosphorylationHGSRLRRTSTFERKP
CCCCCCCCCCCCCCC
26.1923312004
407PhosphorylationGSRLRRTSTFERKPS
CCCCCCCCCCCCCCC
29.3228102081
408PhosphorylationSRLRRTSTFERKPSK
CCCCCCCCCCCCCCC
28.9823312004
414PhosphorylationSTFERKPSKRYPSRR
CCCCCCCCCCCCCCC
32.57-
423PhosphorylationRYPSRRHSTFKASNP
CCCCCCCCCCCCCCH
33.4620873877
424PhosphorylationYPSRRHSTFKASNPV
CCCCCCCCCCCCCHH
24.0320873877
426MethylationSRRHSTFKASNPVIA
CCCCCCCCCCCHHHH
51.50-
428PhosphorylationRHSTFKASNPVIAAQ
CCCCCCCCCHHHHHH
42.1128985074
440PhosphorylationAAQLCSKTNPEVHNY
HHHHHCCCCHHHHCC
39.4521945579
447PhosphorylationTNPEVHNYQPQYHPN
CCHHHHCCCCCCCCC
13.4921945579
451PhosphorylationVHNYQPQYHPNIHPS
HHCCCCCCCCCCCCC
26.4021945579
466 (in isoform 2)Phosphorylation-23.7126657352
466PhosphorylationQPRWHPHSPNVSYPL
CCCCCCCCCCCCCCC
23.7122798277
472 (in isoform 2)Phosphorylation-30.2327794612
479PhosphorylationPLPSPVLSSSDRLPF
CCCCCCCCCCCCCCC
28.2017389395
480PhosphorylationLPSPVLSSSDRLPFG
CCCCCCCCCCCCCCC
31.9022798277
483 (in isoform 2)Phosphorylation-46.3224719451
485 (in isoform 2)Phosphorylation-26.7225849741
489 (in isoform 2)Phosphorylation-45.8728796482
493 (in isoform 2)Phosphorylation-41.6225884760
510 (in isoform 2)Phosphorylation-25.60-
539PhosphorylationPLRSPNSSSKSLTKL
CCCCCCCCCCCCCCC
48.7224719451
568PhosphorylationLKKLELETVKAAGPW
HHHCCCEEHHHCCCC
39.6724114839
591PhosphorylationKAEEKKVSEKTLQTP
HHHHHCCCCCCCCCC
42.11-
594PhosphorylationEKKVSEKTLQTPLLP
HHCCCCCCCCCCCCC
21.75-
597PhosphorylationVSEKTLQTPLLPSPV
CCCCCCCCCCCCCCC
21.01-
602PhosphorylationLQTPLLPSPVADHVK
CCCCCCCCCCCCHHH
31.7924076635
718PhosphorylationQVSVPLPSPKVQNVS
EEECCCCCCCCCCCC
45.0624719451
737PhosphorylationSEGKGLLSPGAKSPS
CCCCCCCCCCCCCCC
26.7425307156
794PhosphorylationLPMKEETTGVCMYPP
CCCCCCCCCEECCCC
30.78-
804PhosphorylationCMYPPIKTRLIKTFP
ECCCCCCEEEEEEEC
31.28-

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 E41LB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E41LB_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 E41LB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAMC3_HUMANLAMC3physical
21988832

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 E41LB_HUMAN

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Related Literatures of Post-Translational Modification

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