RMD5A_HUMAN - dbPTM
RMD5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RMD5A_HUMAN
UniProt AC Q9H871
Protein Name Protein RMD5 homolog A
Gene Name RMND5A
Organism Homo sapiens (Human).
Sequence Length 391
Subcellular Localization
Protein Description
Protein Sequence MDQCVTVERELEKVLHKFSGYGQLCERGLEELIDYTGGLKHEILQSHGQDAELSGTLSLVLTQCCKRIKDTVQKLASDHKDIHSSVSRVGKAIDKNFDSDISSVGIDGCWQADSQRLLNEVMVEHFFRQGMLDVAEELCQESGLSVDPSQKEPFVELNRILEALKVRVLRPALEWAVSNREMLIAQNSSLEFKLHRLYFISLLMGGTTNQREALQYAKNFQPFALNHQKDIQVLMGSLVYLRQGIENSPYVHLLDANQWADICDIFTRDACALLGLSVESPLSVSFSAGCVALPALINIKAVIEQRQCTGVWNQKDELPIEVDLGKKCWYHSIFACPILRQQTTDNNPPMKLVCGHIISRDALNKMFNGSKLKCPYCPMEQSPGDAKQIFF
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
1Acetylation-------MDQCVTVE
-------CCCCCHHH		7.8822814378
13UbiquitinationTVERELEKVLHKFSG
HHHHHHHHHHHHCCC		63.8229967540
17UbiquitinationELEKVLHKFSGYGQL
HHHHHHHHCCCHHHH		36.7429967540
17AcetylationELEKVLHKFSGYGQL
HHHHHHHHCCCHHHH		36.7425953088
21PhosphorylationVLHKFSGYGQLCERG
HHHHCCCHHHHHHHH		10.6629496907
69UbiquitinationTQCCKRIKDTVQKLA
HHHHHHHHHHHHHHH		51.91-
74UbiquitinationRIKDTVQKLASDHKD
HHHHHHHHHHHCCHH		41.5029967540
77PhosphorylationDTVQKLASDHKDIHS
HHHHHHHHCCHHHHH		51.1627794612
80 (in isoform 2)Ubiquitination-64.4721906983
80 (in isoform 1)Ubiquitination-64.4721890473
80UbiquitinationQKLASDHKDIHSSVS
HHHHHCCHHHHHHHH		64.4729967540
84PhosphorylationSDHKDIHSSVSRVGK
HCCHHHHHHHHHHHH		32.5427794612
85PhosphorylationDHKDIHSSVSRVGKA
CCHHHHHHHHHHHHH		15.2227794612
87PhosphorylationKDIHSSVSRVGKAID
HHHHHHHHHHHHHHH		24.1727794612
91UbiquitinationSSVSRVGKAIDKNFD
HHHHHHHHHHHCCCC		39.0329967540
95UbiquitinationRVGKAIDKNFDSDIS
HHHHHHHCCCCCCHH		54.09-
165UbiquitinationNRILEALKVRVLRPA
HHHHHHHHHHHHHHH		34.73-
218 (in isoform 1)Ubiquitination-54.0521890473
218UbiquitinationREALQYAKNFQPFAL
HHHHHHHHHCCCCCC		54.0521890473
315UbiquitinationCTGVWNQKDELPIEV
CCCCCCCCCCCCEEE		50.3829967540
326UbiquitinationPIEVDLGKKCWYHSI
CEEEECCCCHHHHHH		52.6432015554
327UbiquitinationIEVDLGKKCWYHSIF
EEEECCCCHHHHHHH		28.35-
330PhosphorylationDLGKKCWYHSIFACP
ECCCCHHHHHHHHCH		8.65-
343PhosphorylationCPILRQQTTDNNPPM
CHHHHHHCCCCCCCC		27.98-
359PhosphorylationLVCGHIISRDALNKM
EEHHHEECHHHHHHH		24.41-
365UbiquitinationISRDALNKMFNGSKL
ECHHHHHHHHCCCCC		45.8022817900
365 (in isoform 1)Ubiquitination-45.8021890473
371AcetylationNKMFNGSKLKCPYCP
HHHHCCCCCCCCCCC		54.0525953088
373UbiquitinationMFNGSKLKCPYCPME
HHCCCCCCCCCCCCC		36.5829967540
376PhosphorylationGSKLKCPYCPMEQSP
CCCCCCCCCCCCCCC		20.75-
382PhosphorylationPYCPMEQSPGDAKQI
CCCCCCCCCCCHHHH		19.9725159151
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 RMD5A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RMD5A_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 RMD5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAEA_HUMANMAEAphysical
17467196
A4_HUMANAPPphysical
21832049
RBP10_HUMANRANBP10physical
26186194
RANB9_HUMANRANBP9physical
26186194
WDR26_HUMANWDR26physical
26186194
ARMC8_HUMANARMC8physical
26186194
MKLN1_HUMANMKLN1physical
26186194
MAEA_HUMANMAEAphysical
26186194
SYWM_HUMANWARS2physical
26186194
HTRA2_HUMANHTRA2physical
26186194
GID4_HUMANGID4physical
26186194
GID8_HUMANGID8physical
26186194
TCAL9_HUMANWBP5physical
26186194
ZMY19_HUMANZMYND19physical
26186194
YPEL5_HUMANYPEL5physical
26186194
ZCH14_HUMANZCCHC14physical
26186194
HBP1_HUMANHBP1physical
26186194
PAPD7_HUMANPAPD7physical
26186194
TCAL9_HUMANWBP5physical
28514442
ZMY19_HUMANZMYND19physical
28514442
RBP10_HUMANRANBP10physical
28514442
WDR26_HUMANWDR26physical
28514442
MKLN1_HUMANMKLN1physical
28514442
GID4_HUMANGID4physical
28514442
ARMC8_HUMANARMC8physical
28514442
MAEA_HUMANMAEAphysical
28514442
HTRA2_HUMANHTRA2physical
28514442
PAPD7_HUMANPAPD7physical
28514442
RANB9_HUMANRANBP9physical
28514442
SYWM_HUMANWARS2physical
28514442
GID8_HUMANGID8physical
28514442
YPEL5_HUMANYPEL5physical
28514442
RBP10_HUMANRANBP10physical
27173435
MKLN1_HUMANMKLN1physical
27173435
RANB9_HUMANRANBP9physical
27173435
ARMC8_HUMANARMC8physical
27173435
WDR26_HUMANWDR26physical
27173435
DDX5_HUMANDDX5physical
27173435
MAML1_HUMANMAML1physical
27173435
RMD5B_HUMANRMND5Bphysical
27173435
YPEL5_HUMANYPEL5physical
27173435
MAEA_HUMANMAEAphysical
27173435
RAB8A_HUMANRAB8Aphysical
27173435
EFHC2_HUMANEFHC2physical
27173435
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 RMD5A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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