ESRP1_HUMAN - dbPTM
ESRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESRP1_HUMAN
UniProt AC Q6NXG1
Protein Name Epithelial splicing regulatory protein 1
Gene Name ESRP1
Organism Homo sapiens (Human).
Sequence Length 681
Subcellular Localization Nucleus .
Protein Description mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2..
Protein Sequence MTASPDYLVVLFGITAGATGAKLGSDEKELILLFWKVVDLANKKVGQLHEVLVRPDQLELTEDCKEETKIDVESLSSASQLDQALRQFNQSVSNELNIGVGTSFCLCTDGQLHVRQILHPEASKKNVLLPECFYSFFDLRKEFKKCCPGSPDIDKLDVATMTEYLNFEKSSSVSRYGASQVEDMGNIILAMISEPYNHRFSDPERVNYKFESGTCSKMELIDDNTVVRARGLPWQSSDQDIARFFKGLNIAKGGAALCLNAQGRRNGEALVRFVSEEHRDLALQRHKHHMGTRYIEVYKATGEDFLKIAGGTSNEVAQFLSKENQVIVRMRGLPFTATAEEVVAFFGQHCPITGGKEGILFVTYPDGRPTGDAFVLFACEEYAQNALRKHKDLLGKRYIELFRSTAAEVQQVLNRFSSAPLIPLPTPPIIPVLPQQFVPPTNVRDCIRLRGLPYAATIEDILDFLGEFATDIRTHGVHMVLNHQGRPSGDAFIQMKSADRAFMAAQKCHKKNMKDRYVEVFQCSAEEMNFVLMGGTLNRNGLSPPPCKLPCLSPPSYTFPAPAAVIPTEAAIYQPSVILNPRALQPSTAYYPAGTQLFMNYTAYYPSPPGSPNSLGYFPTAANLSGVPPQPGTVVRMQGLAYNTGVKEILNFFQGYQYATEDGLIHTNDQARTLPKEWVCI
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
2Phosphorylation------MTASPDYLV
------CCCCCCEEE
35.5224043423
4Phosphorylation----MTASPDYLVVL
----CCCCCCEEEEE
14.7824043423
7Phosphorylation-MTASPDYLVVLFGI
-CCCCCCEEEEEEEE
12.5524043423
15PhosphorylationLVVLFGITAGATGAK
EEEEEEECCCCCCCC
21.2924043423
19PhosphorylationFGITAGATGAKLGSD
EEECCCCCCCCCCCC
36.4324043423
150PhosphorylationFKKCCPGSPDIDKLD
HHHHCCCCCCHHHCC
12.4430206219
162PhosphorylationKLDVATMTEYLNFEK
HCCHHHHHHHHCCCC
19.6823663014
164PhosphorylationDVATMTEYLNFEKSS
CHHHHHHHHCCCCCC
9.5923663014
170PhosphorylationEYLNFEKSSSVSRYG
HHHCCCCCCCCHHCC
22.2023663014
171PhosphorylationYLNFEKSSSVSRYGA
HHCCCCCCCCHHCCC
45.9123663014
172PhosphorylationLNFEKSSSVSRYGAS
HCCCCCCCCHHCCCH
31.0723663014
174PhosphorylationFEKSSSVSRYGASQV
CCCCCCCHHCCCHHH
23.0223663014
225PhosphorylationMELIDDNTVVRARGL
EEEECCCCEEECCCC
27.63-
236PhosphorylationARGLPWQSSDQDIAR
CCCCCCCCCHHHHHH
31.8224719451
237PhosphorylationRGLPWQSSDQDIARF
CCCCCCCCHHHHHHH
24.9626657352
298PhosphorylationGTRYIEVYKATGEDF
CCCEEEEEEHHHCCH
5.11-
307 (in isoform 2)Ubiquitination-30.4221906983
307 (in isoform 4)Ubiquitination-30.4221906983
307 (in isoform 3)Ubiquitination-30.4221906983
307 (in isoform 1)Ubiquitination-30.4221906983
307UbiquitinationATGEDFLKIAGGTSN
HHHCCHHHHCCCCHH
30.4221906983
313PhosphorylationLKIAGGTSNEVAQFL
HHHCCCCHHHHHHHH
33.9825003641
322 (in isoform 4)Ubiquitination-63.9321906983
322 (in isoform 3)Ubiquitination-63.9321906983
322 (in isoform 1)Ubiquitination-63.9321906983
322 (in isoform 2)Ubiquitination-63.9321906983
322UbiquitinationEVAQFLSKENQVIVR
HHHHHHCCCCCEEEE
63.932190698
426PhosphorylationAPLIPLPTPPIIPVL
CCCCCCCCCCCCCCC
49.7524719451
543PhosphorylationTLNRNGLSPPPCKLP
CCCCCCCCCCCCCCC
36.4419664995
543 (in isoform 3)Phosphorylation-36.4428348404
543 (in isoform 5)Phosphorylation-36.4428348404
549 (in isoform 3)Phosphorylation-4.6328348404
549 (in isoform 5)Phosphorylation-4.6328348404
552 (in isoform 5)Phosphorylation-8.9928348404
552 (in isoform 3)Phosphorylation-8.9928348404
553PhosphorylationPCKLPCLSPPSYTFP
CCCCCCCCCCCCCCC
41.2924719451
553 (in isoform 3)Phosphorylation-41.2928348404
553 (in isoform 5)Phosphorylation-41.2928348404
554 (in isoform 3)Phosphorylation-14.6528348404
554 (in isoform 5)Phosphorylation-14.6528348404
556PhosphorylationLPCLSPPSYTFPAPA
CCCCCCCCCCCCCCC
39.9428348404
558PhosphorylationCLSPPSYTFPAPAAV
CCCCCCCCCCCCCEE
27.7228348404
568PhosphorylationAPAAVIPTEAAIYQP
CCCEEECCCCHHCCC
27.42-
573PhosphorylationIPTEAAIYQPSVILN
ECCCCHHCCCEEEEC
15.05-
576PhosphorylationEAAIYQPSVILNPRA
CCHHCCCEEEECCCC
13.28-
582MethylationPSVILNPRALQPSTA
CEEEECCCCCCCCCC
47.0224129315
636MethylationPQPGTVVRMQGLAYN
CCCCCEEEEEEEEEC
13.8458854923

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 ESRP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ESRP1_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 ESRP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RGPD8_HUMANRGPD8physical
28514442
RGPD5_HUMANRGPD5physical
28514442
RBPMS_HUMANRBPMSphysical
28514442
RGPD3_HUMANRGPD3physical
28514442
RBPS2_HUMANRBPMS2physical
28514442
ATX2_HUMANATXN2physical
28514442
THUM3_HUMANTHUMPD3physical
28514442
ZN703_HUMANZNF703physical
28514442
ELAV2_HUMANELAVL2physical
28514442
GPTC8_HUMANGPATCH8physical
28514442

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 ESRP1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP