MIEN1_HUMAN - dbPTM
MIEN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIEN1_HUMAN
UniProt AC Q9BRT3
Protein Name Migration and invasion enhancer 1
Gene Name MIEN1
Organism Homo sapiens (Human).
Sequence Length 115
Subcellular Localization Cytoplasm, cytosol. Cell membrane
Lipid-anchor
Cytoplasmic side. Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions.
Protein Description Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process..
Protein Sequence MSGEPGQTSVAPPPEEVEPGSGVRIVVEYCEPCGFEATYLELASAVKEQYPGIEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRRASNGETLEKITNSRPPCVIL
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
2Acetylation------MSGEPGQTS
------CCCCCCCCC
52.4422814378
2Phosphorylation------MSGEPGQTS
------CCCCCCCCC
52.4424505115
39PhosphorylationPCGFEATYLELASAV
CCCCCHHHHHHHHHH
12.77-
50PhosphorylationASAVKEQYPGIEIES
HHHHHHHCCCCEEEE
12.43-
85PhosphorylationLENGGFPYEKDLIEA
CCCCCCCCHHHHHHH
33.0928102081
87UbiquitinationNGGFPYEKDLIEAIR
CCCCCCHHHHHHHHH
52.57-
97PhosphorylationIEAIRRASNGETLEK
HHHHHHHHCCCHHHH
43.4828102081
101PhosphorylationRRASNGETLEKITNS
HHHHCCCHHHHHHCC
41.4328102081
112GeranylgeranylationITNSRPPCVIL----
HHCCCCCEEEC----
3.0919503095
112GeranylgeranylationITNSRPPCVIL----
HHCCCCCEEEC----
3.0919503095

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 MIEN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIEN1_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 MIEN1_HUMAN !!

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

Oops, there are no PPI records of MIEN1_HUMAN !!

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 MIEN1_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Prenylated c17orf37 induces filopodia formation to promote cellmigration and metastasis.";
Dasgupta S., Cushman I., Kpetemey M., Casey P.J., Vishwanatha J.K.;
J. Biol. Chem. 286:25935-25946(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112, ANDMUTAGENESIS OF CYS-112 AND 112-CYS--LEU-115.
"Novel gene C17orf37 in 17q12 amplicon promotes migration and invasionof prostate cancer cells.";
Dasgupta S., Wasson L.M., Rauniyar N., Prokai L., Borejdo J.,Vishwanatha J.K.;
Oncogene 28:2860-2872(2009).
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND PROBABLEISOPRENYLATION AT CYS-112.
"C35 (C17orf37) is a novel tumor biomarker abundantly expressed inbreast cancer.";
Evans E.E., Henn A.D., Jonason A., Paris M.J., Schiffhauer L.M.,Borrello M.A., Smith E.S., Sahasrabudhe D.M., Zauderer M.;
Mol. Cancer Ther. 5:2919-2930(2006).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,AND PROBABLE ISOPRENYLATION.

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