MALD2_HUMAN - dbPTM
MALD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MALD2_HUMAN
UniProt AC Q8N4S9
Protein Name MARVEL domain-containing protein 2
Gene Name MARVELD2
Organism Homo sapiens (Human).
Sequence Length 558
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell junction, tight junction. Found at tricellular contacts..
Protein Description Plays a role in the formation of the epithelial barriers. The separation of the endolymphatic and perilymphatic spaces of the organ of Corti from one another by epithelial barriers is required for normal hearing..
Protein Sequence MSNDGRSRNRDRRYDEVPSDLPYQDTTIRTHPTLHDSERAVSADPLPPPPLPLQPPFGPDFYSSDTEEPAIAPDLKPVRRFVPDSWKNFFRGKKKDPEWDKPVSDIRYISDGVECSPPASPARPNHRSPLNSCKDPYGGSEGTFSSRKEADAVFPRDPYGSLDRHTQTVRTYSEKVEEYNLRYSYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDSEWYNLFGYSQPYGMGGVGGLGSMYGGYYYTGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGINVALFILYMAAAIVYVNDTNRGGLCYYPLFNTPVNAVFCRVEGGQIAAMIFLFVTMIVYLISALVCLKLWRHEAARRHREYMEQQEINEPSLSSKRKMCEMATSGDRQRDSEVNFKELRTAKMKPELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDERERYKAVFQDQFSEYKELSAEVQAVLRKFDELDAVMSRLPHHSESRQEHERISRIHEEFKKKKNDPTFLEKKERCDYLKNKLSHIKQRIQEYDKVMNWDVQGYS
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
14PhosphorylationSRNRDRRYDEVPSDL
CCCCCCCCCCCCCCC		19.8328152594
19PhosphorylationRRYDEVPSDLPYQDT
CCCCCCCCCCCCCCC		57.8828152594
23PhosphorylationEVPSDLPYQDTTIRT
CCCCCCCCCCCCCCC		26.7320007894
26PhosphorylationSDLPYQDTTIRTHPT
CCCCCCCCCCCCCCC		14.4826356563
27PhosphorylationDLPYQDTTIRTHPTL
CCCCCCCCCCCCCCC		19.4226356563
33PhosphorylationTTIRTHPTLHDSERA
CCCCCCCCCCCCCCC		29.1724719451
37PhosphorylationTHPTLHDSERAVSAD
CCCCCCCCCCCCCCC		20.4528348404
42PhosphorylationHDSERAVSADPLPPP
CCCCCCCCCCCCCCC		26.4326657352
62PhosphorylationPPFGPDFYSSDTEEP
CCCCCCCCCCCCCCC		18.0425311616
63PhosphorylationPFGPDFYSSDTEEPA
CCCCCCCCCCCCCCC		23.0223898821
64PhosphorylationFGPDFYSSDTEEPAI
CCCCCCCCCCCCCCC		36.8526657352
66PhosphorylationPDFYSSDTEEPAIAP
CCCCCCCCCCCCCCC		44.1726657352
87 (in isoform 2)Ubiquitination-48.0721890473
87 (in isoform 1)Ubiquitination-48.0721890473
87 (in isoform 3)Ubiquitination-48.0721890473
87UbiquitinationRFVPDSWKNFFRGKK
HHCCHHHHHHHCCCC		48.0722817900
101UbiquitinationKKDPEWDKPVSDIRY
CCCCCCCCCCHHCEE		48.6829967540
104PhosphorylationPEWDKPVSDIRYISD
CCCCCCCHHCEEECC		35.5323186163
108PhosphorylationKPVSDIRYISDGVEC
CCCHHCEEECCCCCC		12.7123927012
110PhosphorylationVSDIRYISDGVECSP
CHHCEEECCCCCCCC		21.2723927012
116PhosphorylationISDGVECSPPASPAR
ECCCCCCCCCCCCCC		22.0323927012
120PhosphorylationVECSPPASPARPNHR
CCCCCCCCCCCCCCC		25.5125159151
128PhosphorylationPARPNHRSPLNSCKD
CCCCCCCCCCCCCCC		26.6225849741
132PhosphorylationNHRSPLNSCKDPYGG
CCCCCCCCCCCCCCC		30.1726356563
134 (in isoform 3)Ubiquitination-62.6521890473
134 (in isoform 2)Ubiquitination-62.6521890473
134 (in isoform 1)Ubiquitination-62.6521890473
134UbiquitinationRSPLNSCKDPYGGSE
CCCCCCCCCCCCCCC		62.6521906983
137PhosphorylationLNSCKDPYGGSEGTF
CCCCCCCCCCCCCCC		44.2326657352
140PhosphorylationCKDPYGGSEGTFSSR
CCCCCCCCCCCCCCH		28.6125849741
143PhosphorylationPYGGSEGTFSSRKEA
CCCCCCCCCCCHHHH		19.1128152594
145PhosphorylationGGSEGTFSSRKEADA
CCCCCCCCCHHHHCC		29.1321815630
146PhosphorylationGSEGTFSSRKEADAV
CCCCCCCCHHHHCCC		43.0825849741
148 (in isoform 1)Ubiquitination-60.2421890473
148 (in isoform 2)Ubiquitination-60.2421890473
148 (in isoform 3)Ubiquitination-60.2421890473
148UbiquitinationEGTFSSRKEADAVFP
CCCCCCHHHHCCCCC		60.2422817900
159PhosphorylationAVFPRDPYGSLDRHT
CCCCCCCCCCCHHCC		24.5217525332
161PhosphorylationFPRDPYGSLDRHTQT
CCCCCCCCCHHCCHH		22.6622167270
166PhosphorylationYGSLDRHTQTVRTYS
CCCCHHCCHHHHHHH		27.1617525332
168PhosphorylationSLDRHTQTVRTYSEK
CCHHCCHHHHHHHHH		17.0728152594
171PhosphorylationRHTQTVRTYSEKVEE
HCCHHHHHHHHHHHH		27.3623312004
172PhosphorylationHTQTVRTYSEKVEEY
CCHHHHHHHHHHHHH		12.3123186163
173PhosphorylationTQTVRTYSEKVEEYN
CHHHHHHHHHHHHHH		30.2625849741
175 (in isoform 2)Ubiquitination-49.3521890473
175 (in isoform 3)Ubiquitination-49.3521890473
175 (in isoform 1)Ubiquitination-49.3521890473
175UbiquitinationTVRTYSEKVEEYNLR
HHHHHHHHHHHHHHH		49.3522817900
183PhosphorylationVEEYNLRYSYMKSWA
HHHHHHHHHHHHHHH		13.8129759185
185PhosphorylationEYNLRYSYMKSWAGL
HHHHHHHHHHHHHHH		10.3029759185
377PhosphorylationAARRHREYMEQQEIN
HHHHHHHHHHHHCCC		13.1021955146
387PhosphorylationQQEINEPSLSSKRKM
HHCCCCCCHHHHHHH		34.4021955146
389PhosphorylationEINEPSLSSKRKMCE
CCCCCCHHHHHHHHH		37.8430576142
390PhosphorylationINEPSLSSKRKMCEM
CCCCCHHHHHHHHHH		41.6030108239
391UbiquitinationNEPSLSSKRKMCEMA
CCCCHHHHHHHHHHH		53.3021906983
391 (in isoform 1)Ubiquitination-53.3021890473
391 (in isoform 2)Ubiquitination-53.3021890473
393UbiquitinationPSLSSKRKMCEMATS
CCHHHHHHHHHHHCC		52.1922817900
400UbiquitinationKMCEMATSGDRQRDS
HHHHHHCCCCCHHHC		29.2033845483
400 (in isoform 3)Ubiquitination-29.2021890473
406UbiquitinationTSGDRQRDSEVNFKE
CCCCCHHHCCCCHHH		40.5923503661
407PhosphorylationSGDRQRDSEVNFKEL
CCCCHHHCCCCHHHH		45.7125849741
412 (in isoform 2)Ubiquitination-51.1121890473
412UbiquitinationRDSEVNFKELRTAKM
HHCCCCHHHHHHHCC		51.1121906983
412 (in isoform 1)Ubiquitination-51.1121890473
418UbiquitinationFKELRTAKMKPELLS
HHHHHHHCCCHHHHC		47.0123503661
442PhosphorylationKPIVMPDYVAKYPVI
CCCCCCCHHHCCCEE		9.0925159151
446PhosphorylationMPDYVAKYPVIQTDD
CCCHHHCCCEEECCC		7.9328102081
451PhosphorylationAKYPVIQTDDERERY
HCCCEEECCCHHHHH		34.0028102081
467PhosphorylationAVFQDQFSEYKELSA
HHHHHHHHHHHHHHH		34.0928102081
469PhosphorylationFQDQFSEYKELSAEV
HHHHHHHHHHHHHHH		14.4727259358
531PhosphorylationEKKERCDYLKNKLSH
HHHHHHHHHHHHHHH		24.1722817900
536UbiquitinationCDYLKNKLSHIKQRI
HHHHHHHHHHHHHHH		6.6922817900
536 (in isoform 3)Ubiquitination-6.6921890473
548 (in isoform 1)Ubiquitination-42.3421890473
548UbiquitinationQRIQEYDKVMNWDVQ
HHHHHHHHHHCCCCC		42.3422817900
557PhosphorylationMNWDVQGYS------
HCCCCCCCC------		8.3029978859
558PhosphorylationNWDVQGYS-------
CCCCCCCC-------		40.3429978859
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 MALD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MALD2_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 MALD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK38_HUMANSTK38physical
28514442
TTL_HUMANTTLphysical
28514442
DIAC_HUMANCTBSphysical
28514442
ACAD9_HUMANACAD9physical
28514442
BI2L1_HUMANBAIAP2L1physical
28514442
CIA30_HUMANNDUFAF1physical
28514442
RAP2A_HUMANRAP2Aphysical
28514442
ECSIT_HUMANECSITphysical
28514442
NEUM_HUMANGAP43physical
28514442
ITCH_HUMANITCHphysical
28436082
Drug and Disease Associations
Kegg Disease
H00605 Deafness, autosomal recessive
OMIM Disease
610153Deafness, autosomal recessive, 49 (DFNB49)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MALD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-120, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-120, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159 AND THR-166, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23, AND MASSSPECTROMETRY.

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