MIP_HUMAN - dbPTM
MIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIP_HUMAN
UniProt AC P30301
Protein Name Lens fiber major intrinsic protein
Gene Name MIP
Organism Homo sapiens (Human).
Sequence Length 263
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell junction, gap junction .
Protein Description Water channel. [PubMed: 24120416 Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity Plays a role in cell-to-cell adhesion and facilitates gap junction coupling]
Protein Sequence MWELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVAMAFGLALATLVQSVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYMAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHPAVSVGQATTVEIFLTLQFVLCIFATYDERRNGQLGSVALAVGFSLALGHLFGMYYTGAGMNPARSFAPAILTGNFTNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSISERLSVLKGAKPDVSNGQPEVTGEPVELNTQAL
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
31PhosphorylationVFFGLGSSLRWAPGP
HHHCCCCCCCCCCCH
21.8324719451
229PhosphorylationLLFPRLKSISERLSV
HHHHHHHHHHHHHHH
35.622176601
231PhosphorylationFPRLKSISERLSVLK
HHHHHHHHHHHHHHH
24.6118081321
235PhosphorylationKSISERLSVLKGAKP
HHHHHHHHHHHCCCC
31.4618081321
245PhosphorylationKGAKPDVSNGQPEVT
HCCCCCCCCCCCCCC
42.49-
246Deamidated asparagineGAKPDVSNGQPEVTG
CCCCCCCCCCCCCCC
53.63-
246DeamidationGAKPDVSNGQPEVTG
CCCCCCCCCCCCCCC
53.6310634618
259Deamidated asparagineTGEPVELNTQAL---
CCCCEECCCCCC---
19.35-
259DeamidationTGEPVELNTQAL---
CCCCEECCCCCC---
19.3510634618

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
229SPhosphorylationKinasePKA-FAMILY-GPS
229SPhosphorylationKinasePKA_GROUP-PhosphoELM
231SPhosphorylationKinasePKA-FAMILY-GPS
231SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIP_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 MIP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRYAA_HUMANCRYAAphysical
18004741
CRYAB_HUMANCRYABphysical
18004741
CRBB2_HUMANCRYBB2physical
18004741
CRGC_HUMANCRYGCphysical
18004741

Drug and Disease Associations
Kegg Disease
H01202 Cataract
OMIM Disease
615274Cataract 15, multiple types (CTRCT15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MIP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Deamidation
ReferencePubMed
"Characterization of human lens major intrinsic protein structure.";
Schey K.L., Little M., Fowler J.G., Crouch R.K.;
Invest. Ophthalmol. Vis. Sci. 41:175-182(2000).
Cited for: PHOSPHORYLATION AT SER-235, DEAMIDATION AT ASN-246 AND ASN-259, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Characterization of human lens major intrinsic protein structure.";
Schey K.L., Little M., Fowler J.G., Crouch R.K.;
Invest. Ophthalmol. Vis. Sci. 41:175-182(2000).
Cited for: PHOSPHORYLATION AT SER-235, DEAMIDATION AT ASN-246 AND ASN-259, ANDMASS SPECTROMETRY.

TOP