ARMC6_HUMAN - dbPTM
ARMC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARMC6_HUMAN
UniProt AC Q6NXE6
Protein Name Armadillo repeat-containing protein 6
Gene Name ARMC6
Organism Homo sapiens (Human).
Sequence Length 501
Subcellular Localization
Protein Description
Protein Sequence MSERCCSRYSSGASIGCTPTSTQAKMVSKRIAQETFDAAVRENIEEFAMGPEEAVKEAVEQFESQGVDLSNIVKTAPKVSADGSQEPTHDILQMLSDLQESVASSRPQEVSAYLTRFCDQCKQDKACRFLAAQKGAYPIIFTAWKLATAGDQGLLLQSLNALSVLTDGQPDLLDAQGLQLLVATLTQNADEADLTCSGIRCVRHACLKHEQNRQDLVKAGVLPLLTGAITHHGHHTDVVREACWALRVMTFDDDIRVPFGHAHNHAKMIVQENKGLKVLIEATKAFLDNPGILSELCGTLSRLAIRNEFCQEVVDLGGLSILVSLLADCNDHQMRDQSGVQELVKQVLSTLRAIAGNDDVKDAIVRAGGTESIVAAMTQHLTSPQVCEQSCAALCFLALRKPDNSRIIVEGGGAVAALQAMKAHPQKAGVQKQACMLIRNLVAHGQAFSKPILDLGAEALIMQARSAHRDCEDVAKAALRDLGCHVELRELWTGQRGNLAP
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
9PhosphorylationSERCCSRYSSGASIG
CCCCCCCCCCCCCCC		7.3027134283
10PhosphorylationERCCSRYSSGASIGC
CCCCCCCCCCCCCCC		22.6125627689
11PhosphorylationRCCSRYSSGASIGCT
CCCCCCCCCCCCCCC		29.4625627689
18PhosphorylationSGASIGCTPTSTQAK
CCCCCCCCCCHHHHH		25.1225159151
21PhosphorylationSIGCTPTSTQAKMVS
CCCCCCCHHHHHHHH		21.52-
49UbiquitinationENIEEFAMGPEEAVK
HHHHHHHCCHHHHHH		12.8121963094
53UbiquitinationEFAMGPEEAVKEAVE
HHHCCHHHHHHHHHH		62.9922817900
64PhosphorylationEAVEQFESQGVDLSN
HHHHHHHHCCCCHHH		33.2617525332
74UbiquitinationVDLSNIVKTAPKVSA
CCHHHHHHHCCCCCC		34.8621906983
78UbiquitinationNIVKTAPKVSADGSQ
HHHHHCCCCCCCCCC		46.4822817900
80PhosphorylationVKTAPKVSADGSQEP
HHHCCCCCCCCCCCC		27.1127732954
84PhosphorylationPKVSADGSQEPTHDI
CCCCCCCCCCCHHHH		31.7325159151
88PhosphorylationADGSQEPTHDILQML
CCCCCCCHHHHHHHH		31.2827732954
96PhosphorylationHDILQMLSDLQESVA
HHHHHHHHHHHHHHH		30.8227732954
97UbiquitinationDILQMLSDLQESVAS
HHHHHHHHHHHHHHH		48.7027667366
109UbiquitinationVASSRPQEVSAYLTR
HHHCCHHHHHHHHHH		40.9121963094
122AcetylationTRFCDQCKQDKACRF
HHHHHHHHHHHHHHH		56.7625953088
122UbiquitinationTRFCDQCKQDKACRF
HHHHHHHHHHHHHHH		56.7627667366
125UbiquitinationCDQCKQDKACRFLAA
HHHHHHHHHHHHHHH		47.06-
134UbiquitinationCRFLAAQKGAYPIIF
HHHHHHHCCCCCEEE		40.5621963094
183UbiquitinationQGLQLLVATLTQNAD
HHHHHHHHHHCCCCH		9.2527667366
193UbiquitinationTQNADEADLTCSGIR
CCCCHHHCCCHHHHH		40.2321963094
208UbiquitinationCVRHACLKHEQNRQD
HHHHHHHCCCHHHHH		45.0021906983
218UbiquitinationQNRQDLVKAGVLPLL
HHHHHHHHHCHHHHH		46.8821963094
242UbiquitinationHTDVVREACWALRVM
CHHHHHHHHHHHHCC		5.4229967540
249UbiquitinationACWALRVMTFDDDIR
HHHHHHCCCCCCCCC		2.2127667366
252UbiquitinationALRVMTFDDDIRVPF
HHHCCCCCCCCCCCC		43.4322817900
256MethylationMTFDDDIRVPFGHAH
CCCCCCCCCCCCCCC		36.73-
259UbiquitinationDDDIRVPFGHAHNHA
CCCCCCCCCCCCCCH		11.6521987572
267UbiquitinationGHAHNHAKMIVQENK
CCCCCCHHHHHHCCC		22.9329967540
274SumoylationKMIVQENKGLKVLIE
HHHHHCCCHHHHHHH		65.94-
274SumoylationKMIVQENKGLKVLIE
HHHHHCCCHHHHHHH		65.94-
274UbiquitinationKMIVQENKGLKVLIE
HHHHHCCCHHHHHHH		65.9421906983
277UbiquitinationVQENKGLKVLIEATK
HHCCCHHHHHHHHHH		43.6022817900
283PhosphorylationLKVLIEATKAFLDNP
HHHHHHHHHHHHHCC		15.32-
284UbiquitinationKVLIEATKAFLDNPG
HHHHHHHHHHHHCCC		44.1621987572
294PhosphorylationLDNPGILSELCGTLS
HHCCCHHHHHHHHHH		26.97-
299PhosphorylationILSELCGTLSRLAIR
HHHHHHHHHHHHHHH		22.14-
301PhosphorylationSELCGTLSRLAIRNE
HHHHHHHHHHHHHHH		25.70-
320UbiquitinationVVDLGGLSILVSLLA
HHHHCHHHHHHHHHH		19.7022817900
320 (in isoform 2)Ubiquitination-19.70-
336UbiquitinationCNDHQMRDQSGVQEL
CCCHHHCCCHHHHHH		41.4727667366
336 (in isoform 2)Ubiquitination-41.47-
338PhosphorylationDHQMRDQSGVQELVK
CHHHCCCHHHHHHHH		45.2621712546
345UbiquitinationSGVQELVKQVLSTLR
HHHHHHHHHHHHHHH		47.5221906983
349PhosphorylationELVKQVLSTLRAIAG
HHHHHHHHHHHHHHC		26.9230622161
350PhosphorylationLVKQVLSTLRAIAGN
HHHHHHHHHHHHHCC		18.9930622161
361UbiquitinationIAGNDDVKDAIVRAG
HHCCCCHHHHHHHCC		48.7321906983
361SumoylationIAGNDDVKDAIVRAG
HHCCCCHHHHHHHCC		48.73-
397UbiquitinationSCAALCFLALRKPDN
HHHHHHHHHCCCCCC		4.2421963094
397 (in isoform 2)Ubiquitination-4.24-
402UbiquitinationCFLALRKPDNSRIIV
HHHHCCCCCCCCEEE		39.3122817900
405PhosphorylationALRKPDNSRIIVEGG
HCCCCCCCCEEEECH		32.0324719451
407UbiquitinationRKPDNSRIIVEGGGA
CCCCCCCEEEECHHH		4.0921963094
422UbiquitinationVAALQAMKAHPQKAG
HHHHHHHHHCHHHCC		46.7021906983
425UbiquitinationLQAMKAHPQKAGVQK
HHHHHHCHHHCCHHH		42.0821963094
427UbiquitinationAMKAHPQKAGVQKQA
HHHHCHHHCCHHHHH		52.1127667366
432UbiquitinationPQKAGVQKQACMLIR
HHHCCHHHHHHHHHH		37.1421963094
450UbiquitinationAHGQAFSKPILDLGA
HCCCCCCCCHHHHCH		29.6221906983
451UbiquitinationHGQAFSKPILDLGAE
CCCCCCCCHHHHCHH		31.0427667366
476UbiquitinationRDCEDVAKAALRDLG
CCHHHHHHHHHHHCC		33.7627667366
484S-nitrosocysteineAALRDLGCHVELREL
HHHHHCCCCEEHHHH		4.17-
484S-nitrosylationAALRDLGCHVELREL
HHHHHCCCCEEHHHH		4.1719483679
496MethylationRELWTGQRGNLAP--
HHHHCCCCCCCCC--		36.99-
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 ARMC6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARMC6_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 ARMC6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PFD5_HUMANPFDN5physical
26344197
COPD_HUMANARCN1physical
26496610
C4BPA_HUMANC4BPAphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
CLUS_HUMANCLUphysical
26496610
CPSM_HUMANCPS1physical
26496610
HSPB1_HUMANHSPB1physical
26496610
P5CR1_HUMANPYCR1physical
26496610
RCN1_HUMANRCN1physical
26496610
LA_HUMANSSBphysical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
XPO1_HUMANXPO1physical
26496610
STX10_HUMANSTX10physical
26496610
PCH2_HUMANTRIP13physical
26496610
ATPK_HUMANATP5J2physical
26496610
SCO2_HUMANSCO2physical
26496610
TBA1B_HUMANTUBA1Bphysical
26496610
THIM_HUMANACAA2physical
26496610
SPTC1_HUMANSPTLC1physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPQ_HUMANCCT8physical
26496610
MAGD2_HUMANMAGED2physical
26496610
SC61B_HUMANSEC61Bphysical
26496610
GCN1_HUMANGCN1L1physical
26496610
XPOT_HUMANXPOTphysical
26496610
TCPE_HUMANCCT5physical
26496610
PNKD_HUMANPNKDphysical
26496610
HIG1A_HUMANHIGD1Aphysical
26496610
CAB45_HUMANSDF4physical
26496610
AR6P4_HUMANARL6IP4physical
26496610
VATH_HUMANATP6V1Hphysical
26496610
T161A_HUMANTMEM161Aphysical
26496610
S35E1_HUMANSLC35E1physical
26496610
USMG5_HUMANUSMG5physical
26496610
TBB5_HUMANTUBBphysical
26496610
PCSK9_HUMANPCSK9physical
26496610
S20A2_HUMANSLC20A2physical
28514442
RMD2_HUMANRMDN2physical
28514442
MUL1_HUMANMUL1physical
28514442
S27A2_HUMANSLC27A2physical
28514442
MOT10_HUMANSLC16A10physical
28514442
METL9_HUMANMETTL9physical
28514442
CA159_HUMANC1orf159physical
28514442
MICU2_HUMANMICU2physical
28514442
DAAM1_HUMANDAAM1physical
28514442
CA198_HUMANC1orf198physical
28514442
EPHA4_HUMANEPHA4physical
28514442
GLT11_HUMANGALNT11physical
28514442
GTR8_HUMANSLC2A8physical
28514442
MCU_HUMANMCUphysical
28514442
ORNT1_HUMANSLC25A15physical
28514442
OZF_HUMANZNF146physical
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 ARMC6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-64, AND MASSSPECTROMETRY.

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