RB6I2_HUMAN - dbPTM
RB6I2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB6I2_HUMAN
UniProt AC Q8IUD2
Protein Name ELKS/Rab6-interacting/CAST family member 1
Gene Name ERC1
Organism Homo sapiens (Human).
Sequence Length 1116
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Golgi apparatus membrane
Peripheral membrane protein. In neurons, localized closed to presynaptic membrane. Recruited on Golgi membranes by RAB6A in a GTP-dependent manner (By similarity)..
Protein Description Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport..
Protein Sequence MYGSARSVGKVEPSSQSPGRSPRLPRSPRLGHRRTNSTGGSSGSSVGGGSGKTLSMENIQSLNAAYATSGPMYLSDHENVGSETPKSTMTLGRSGGRLPYGVRMTAMGSSPNIASSGVASDTIAFGEHHLPPVSMASTVPHSLRQARDNTIMDLQTQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSPELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQDELRIQRDLNQLFQQDSSSRTGEPCVAELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENSMLREEMHRRFENAPDSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSTEEREEEMKQMEVYRSHSKFMKNKVEQLKEELSSKEAQWEELKKKAAGLQAEIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKETMLNKKTKQIQDMAEEKGTQAGEIHDLKDMLDVKERKVNVLQKKIENLQEQLRDKEKQMSSLKERVKSLQADTTNTDTALTTLEEALAEKERTIERLKEQRDRDEREKQEEIDNYKKDLKDLKEKVSLLQGDLSEKEASLLDLKEHASSLASSGLKKDSRLKTLEIALEQKKEECLKMESQLKKAHEAALEARASPEMSDRIQHLEREITRYKDESSKAQAEVDRLLEILKEVENEKNDKDKKIAELERQVKDQNKKVANLKHKEQVEKKKSAQMLEEARRREDNLNDSSQQLQDSLRKKDDRIEELEEALRESVQITAEREMVLAQEESARTNAEKQVEELLMAMEKVKQELESMKAKLSSTQQSLAEKETHLTNLRAERRKHLEEVLEMKQEALLAAISEKDANIALLELSSSKKKTQEEVAALKREKDRLVQQLKQQTQNRMKLMADNYEDDHFKSSHSNQTNHKPSPDQIIQPLLELDQNRSKLKLYIGHLTTLCHDRDPLILRGLTPPASYNLDDDQAAWENELQKMTRGQLQDELEKGERDNAELQEFANAILQQIADHCPDILEQVVNALEESS
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
2Phosphorylation------MYGSARSVG
------CCCCCCCCC
30.9623090842
4Phosphorylation----MYGSARSVGKV
----CCCCCCCCCCC
21.4425056879
6Methylation--MYGSARSVGKVEP
--CCCCCCCCCCCCC
33.31-
7Phosphorylation-MYGSARSVGKVEPS
-CCCCCCCCCCCCCC
34.6323927012
10AcetylationGSARSVGKVEPSSQS
CCCCCCCCCCCCCCC
41.0725953088
14PhosphorylationSVGKVEPSSQSPGRS
CCCCCCCCCCCCCCC
27.7522167270
14 (in isoform 2)Phosphorylation-27.75-
14 (in isoform 3)Phosphorylation-27.75-
14 (in isoform 4)Phosphorylation-27.75-
14 (in isoform 5)Phosphorylation-27.75-
15PhosphorylationVGKVEPSSQSPGRSP
CCCCCCCCCCCCCCC
45.4529255136
15 (in isoform 2)Phosphorylation-45.45-
15 (in isoform 3)Phosphorylation-45.45-
15 (in isoform 4)Phosphorylation-45.45-
15 (in isoform 5)Phosphorylation-45.45-
17PhosphorylationKVEPSSQSPGRSPRL
CCCCCCCCCCCCCCC
31.1329255136
17 (in isoform 2)Phosphorylation-31.13-
17 (in isoform 3)Phosphorylation-31.13-
17 (in isoform 4)Phosphorylation-31.13-
17 (in isoform 5)Phosphorylation-31.13-
20MethylationPSSQSPGRSPRLPRS
CCCCCCCCCCCCCCC
47.04-
21PhosphorylationSSQSPGRSPRLPRSP
CCCCCCCCCCCCCCC
21.9329255136
21 (in isoform 2)Phosphorylation-21.93-
21 (in isoform 3)Phosphorylation-21.93-
21 (in isoform 4)Phosphorylation-21.93-
21 (in isoform 5)Phosphorylation-21.93-
27PhosphorylationRSPRLPRSPRLGHRR
CCCCCCCCCCCCCCC
16.6628355574
27 (in isoform 2)Phosphorylation-16.66-
27 (in isoform 3)Phosphorylation-16.66-
27 (in isoform 4)Phosphorylation-16.66-
27 (in isoform 5)Phosphorylation-16.66-
35PhosphorylationPRLGHRRTNSTGGSS
CCCCCCCCCCCCCCC
33.2128176443
35 (in isoform 2)Phosphorylation-33.21-
35 (in isoform 3)Phosphorylation-33.21-
35 (in isoform 4)Phosphorylation-33.21-
35 (in isoform 5)Phosphorylation-33.21-
37PhosphorylationLGHRRTNSTGGSSGS
CCCCCCCCCCCCCCC
28.0227273156
38PhosphorylationGHRRTNSTGGSSGSS
CCCCCCCCCCCCCCC
47.8627273156
41PhosphorylationRTNSTGGSSGSSVGG
CCCCCCCCCCCCCCC
32.6328176443
42PhosphorylationTNSTGGSSGSSVGGG
CCCCCCCCCCCCCCC
46.0728176443
42 (in isoform 2)Phosphorylation-46.07-
42 (in isoform 3)Phosphorylation-46.07-
42 (in isoform 4)Phosphorylation-46.07-
42 (in isoform 5)Phosphorylation-46.07-
44PhosphorylationSTGGSSGSSVGGGSG
CCCCCCCCCCCCCCC
24.6520068231
45PhosphorylationTGGSSGSSVGGGSGK
CCCCCCCCCCCCCCC
28.4520068231
50PhosphorylationGSSVGGGSGKTLSME
CCCCCCCCCCCCCHH
40.1520068231
53PhosphorylationVGGGSGKTLSMENIQ
CCCCCCCCCCHHHHH
27.8225159151
55PhosphorylationGGSGKTLSMENIQSL
CCCCCCCCHHHHHHH
29.3123401153
55 (in isoform 2)Phosphorylation-29.31-
55 (in isoform 3)Phosphorylation-29.31-
55 (in isoform 4)Phosphorylation-29.31-
55 (in isoform 5)Phosphorylation-29.31-
61PhosphorylationLSMENIQSLNAAYAT
CCHHHHHHHHHHHHC
21.5727080861
66PhosphorylationIQSLNAAYATSGPMY
HHHHHHHHHCCCCEE
14.1723090842
68PhosphorylationSLNAAYATSGPMYLS
HHHHHHHCCCCEECC
22.8827080861
69PhosphorylationLNAAYATSGPMYLSD
HHHHHHCCCCEECCC
32.5027080861
73PhosphorylationYATSGPMYLSDHENV
HHCCCCEECCCCCCC
13.2422199227
75PhosphorylationTSGPMYLSDHENVGS
CCCCEECCCCCCCCC
21.3127422710
82PhosphorylationSDHENVGSETPKSTM
CCCCCCCCCCCCCCE
33.7322199227
84PhosphorylationHENVGSETPKSTMTL
CCCCCCCCCCCCEEC
37.4022199227
90PhosphorylationETPKSTMTLGRSGGR
CCCCCCEECCCCCCC
26.5828857561
93MethylationKSTMTLGRSGGRLPY
CCCEECCCCCCCCCC
34.93-
94PhosphorylationSTMTLGRSGGRLPYG
CCEECCCCCCCCCCC
43.7425159151
94 (in isoform 2)Phosphorylation-43.74-
94 (in isoform 3)Phosphorylation-43.74-
94 (in isoform 4)Phosphorylation-43.74-
94 (in isoform 5)Phosphorylation-43.74-
100PhosphorylationRSGGRLPYGVRMTAM
CCCCCCCCCEEEEEC
32.6123186163
105PhosphorylationLPYGVRMTAMGSSPN
CCCCEEEEECCCCCC
11.7022210691
109PhosphorylationVRMTAMGSSPNIASS
EEEEECCCCCCCCCC
29.5422210691
110PhosphorylationRMTAMGSSPNIASSG
EEEECCCCCCCCCCC
19.0820068231
110 (in isoform 2)Phosphorylation-19.08-
110 (in isoform 3)Phosphorylation-19.08-
110 (in isoform 4)Phosphorylation-19.08-
110 (in isoform 5)Phosphorylation-19.08-
115PhosphorylationGSSPNIASSGVASDT
CCCCCCCCCCCCCCC
24.6722210691
116PhosphorylationSSPNIASSGVASDTI
CCCCCCCCCCCCCCE
28.4122210691
120PhosphorylationIASSGVASDTIAFGE
CCCCCCCCCCEEECC
32.6420068231
122PhosphorylationSSGVASDTIAFGEHH
CCCCCCCCEEECCCC
16.2320068231
134PhosphorylationEHHLPPVSMASTVPH
CCCCCCCCHHHCCCH
17.8820068231
137PhosphorylationLPPVSMASTVPHSLR
CCCCCHHHCCCHHHH
22.6920068231
138PhosphorylationPPVSMASTVPHSLRQ
CCCCHHHCCCHHHHH
28.6320068231
142PhosphorylationMASTVPHSLRQARDN
HHHCCCHHHHHHHHC
21.1220068231
150PhosphorylationLRQARDNTIMDLQTQ
HHHHHHCCHHHHHHH
23.2028857561
177PhosphorylationKDVEVKESKLSSSMN
CCCHHCHHHHHHHHH
32.9323403867
181PhosphorylationVKESKLSSSMNSIKT
HCHHHHHHHHHHHHH
44.0025159151
182PhosphorylationKESKLSSSMNSIKTF
CHHHHHHHHHHHHHH
20.7125627689
188PhosphorylationSSMNSIKTFWSPELK
HHHHHHHHHCCHHHH
28.7730266825
191PhosphorylationNSIKTFWSPELKKER
HHHHHHCCHHHHHHH
12.3319664994
191 (in isoform 2)Phosphorylation-12.33-
191 (in isoform 3)Phosphorylation-12.33-
191 (in isoform 4)Phosphorylation-12.33-
191 (in isoform 5)Phosphorylation-12.33-
250PhosphorylationNQLFQQDSSSRTGEP
HHHHHHCCCCCCCCC
26.3523663014
251PhosphorylationQLFQQDSSSRTGEPC
HHHHHCCCCCCCCCC
31.9323663014
252PhosphorylationLFQQDSSSRTGEPCV
HHHHCCCCCCCCCCE
37.5023663014
299UbiquitinationELRIETQKQTLNARD
HHHHHHHHHHHHHCH
53.31-
319UbiquitinationLLEMLQSKGLSAKAT
HHHHHHHCCCCCCCC
51.41-
374PhosphorylationRFENAPDSAKTKALQ
HHHCCCCHHHHHHHH
30.5221815630
3762-HydroxyisobutyrylationENAPDSAKTKALQTV
HCCCCHHHHHHHHHH
55.28-
3902-HydroxyisobutyrylationVIEMKDSKISSMERG
HHHHCHHHHHHHHHH
57.66-
390AcetylationVIEMKDSKISSMERG
HHHHCHHHHHHHHHH
57.6625953088
392PhosphorylationEMKDSKISSMERGLR
HHCHHHHHHHHHHHH
27.6322210691
393PhosphorylationMKDSKISSMERGLRD
HCHHHHHHHHHHHHH
28.3022210691
407SulfoxidationDLEEEIQMLKSNGAL
HHHHHHHHHHHCCCC
6.6430846556
410PhosphorylationEEIQMLKSNGALSTE
HHHHHHHHCCCCCHH
36.2123312004
415PhosphorylationLKSNGALSTEEREEE
HHHCCCCCHHHHHHH
32.9922210691
416PhosphorylationKSNGALSTEEREEEM
HHCCCCCHHHHHHHH
42.5921815630
431PhosphorylationKQMEVYRSHSKFMKN
HHHHHHHHHHHHHHH
17.9028270605
433PhosphorylationMEVYRSHSKFMKNKV
HHHHHHHHHHHHHHH
28.9228270605
448PhosphorylationEQLKEELSSKEAQWE
HHHHHHHHHHHHHHH
42.5223403867
488UbiquitinationELLALQTKLETLTNQ
HHHHHHHHHHHHHHH
31.22-
491PhosphorylationALQTKLETLTNQFSD
HHHHHHHHHHHHCCC
49.6821406692
493PhosphorylationQTKLETLTNQFSDSK
HHHHHHHHHHCCCCH
34.1021406692
497PhosphorylationETLTNQFSDSKQHIE
HHHHHHCCCCHHHHH
31.0721406692
499PhosphorylationLTNQFSDSKQHIEVL
HHHHCCCCHHHHHHH
32.7721406692
5002-HydroxyisobutyrylationTNQFSDSKQHIEVLK
HHHCCCCHHHHHHHH
51.38-
552UbiquitinationIQDMAEEKGTQAGEI
HHHHHHHHCCCCHHC
59.78-
554PhosphorylationDMAEEKGTQAGEIHD
HHHHHHCCCCHHCCC
26.7223879269
569MalonylationLKDMLDVKERKVNVL
HHHHHCHHHHHHHHH
52.0126320211
572MalonylationMLDVKERKVNVLQKK
HHCHHHHHHHHHHHH
38.9726320211
5792-HydroxyisobutyrylationKVNVLQKKIENLQEQ
HHHHHHHHHHHHHHH
42.14-
579MalonylationKVNVLQKKIENLQEQ
HHHHHHHHHHHHHHH
42.1426320211
590AcetylationLQEQLRDKEKQMSSL
HHHHHHHHHHHHHHH
61.45156207
602UbiquitinationSSLKERVKSLQADTT
HHHHHHHHHHHCCCC
52.23-
603PhosphorylationSLKERVKSLQADTTN
HHHHHHHHHHCCCCC
23.9028857561
625UbiquitinationLEEALAEKERTIERL
HHHHHHHHHHHHHHH
47.06-
652AcetylationEEIDNYKKDLKDLKE
HHHHHHHHHHHHHHH
58.917365637
655AcetylationDNYKKDLKDLKEKVS
HHHHHHHHHHHHHHH
71.7620167786
658AcetylationKKDLKDLKEKVSLLQ
HHHHHHHHHHHHHHH
66.6720167786
669PhosphorylationSLLQGDLSEKEASLL
HHHHCCCCHHHHHHH
51.9026437602
671UbiquitinationLQGDLSEKEASLLDL
HHCCCCHHHHHHHHH
56.03-
674PhosphorylationDLSEKEASLLDLKEH
CCCHHHHHHHHHHHH
30.4727499020
6792-HydroxyisobutyrylationEASLLDLKEHASSLA
HHHHHHHHHHHHHHH
47.31-
679UbiquitinationEASLLDLKEHASSLA
HHHHHHHHHHHHHHH
47.31-
687PhosphorylationEHASSLASSGLKKDS
HHHHHHHHCCCCHHH
30.1725159151
688PhosphorylationHASSLASSGLKKDSR
HHHHHHHCCCCHHHH
42.4025159151
691UbiquitinationSLASSGLKKDSRLKT
HHHHCCCCHHHHCHH
59.05-
706AcetylationLEIALEQKKEECLKM
HHHHHHHHHHHHHHH
53.4223236377
719UbiquitinationKMESQLKKAHEAALE
HHHHHHHHHHHHHHH
64.66-
730PhosphorylationAALEARASPEMSDRI
HHHHHHCCHHHHHHH
18.8121815630
734PhosphorylationARASPEMSDRIQHLE
HHCCHHHHHHHHHHH
23.2929523821
736MethylationASPEMSDRIQHLERE
CCHHHHHHHHHHHHH
24.14-
766UbiquitinationDRLLEILKEVENEKN
HHHHHHHHHHHHHCC
66.43-
799AcetylationKVANLKHKEQVEKKK
HHHCHHHHHHHHHHH
48.537974731
805AcetylationHKEQVEKKKSAQMLE
HHHHHHHHHHHHHHH
38.157974745
807PhosphorylationEQVEKKKSAQMLEEA
HHHHHHHHHHHHHHH
32.3925159151
824PhosphorylationREDNLNDSSQQLQDS
HHHCCCHHHHHHHHH
29.0422496350
825PhosphorylationEDNLNDSSQQLQDSL
HHCCCHHHHHHHHHH
25.4725159151
831PhosphorylationSSQQLQDSLRKKDDR
HHHHHHHHHHHHHHH
19.6728787133
835UbiquitinationLQDSLRKKDDRIEEL
HHHHHHHHHHHHHHH
59.43-
858SulfoxidationQITAEREMVLAQEES
CHHHHHHHHHHHHHH
3.6121406390
890O-linked_GlycosylationKVKQELESMKAKLSS
HHHHHHHHHHHHHHH
37.9030379171
890PhosphorylationKVKQELESMKAKLSS
HHHHHHHHHHHHHHH
37.9029083192
894UbiquitinationELESMKAKLSSTQQS
HHHHHHHHHHHHHHH
43.30-
901PhosphorylationKLSSTQQSLAEKETH
HHHHHHHHHHHHHHH
21.52-
905UbiquitinationTQQSLAEKETHLTNL
HHHHHHHHHHHHHHH
63.41-
948PhosphorylationNIALLELSSSKKKTQ
HHHHHHHCCCCCCCH
24.1628555341
954PhosphorylationLSSSKKKTQEEVAAL
HCCCCCCCHHHHHHH
50.5228555341
973UbiquitinationDRLVQQLKQQTQNRM
HHHHHHHHHHHHHHH
35.70-
977 (in isoform 3)Phosphorylation-31.06-
983SulfoxidationTQNRMKLMADNYEDD
HHHHHHHHHCCCCCC
3.5230846556
987PhosphorylationMKLMADNYEDDHFKS
HHHHHCCCCCCCHHC
22.6825106551
994PhosphorylationYEDDHFKSSHSNQTN
CCCCCHHCCCCCCCC
32.1329523821
995PhosphorylationEDDHFKSSHSNQTNH
CCCCHHCCCCCCCCC
31.3729523821
997PhosphorylationDHFKSSHSNQTNHKP
CCHHCCCCCCCCCCC
32.3629523821
1000PhosphorylationKSSHSNQTNHKPSPD
HCCCCCCCCCCCCHH
43.4729523821
1003AcetylationHSNQTNHKPSPDQII
CCCCCCCCCCHHHCH
49.6226051181
1003UbiquitinationHSNQTNHKPSPDQII
CCCCCCCCCCHHHCH
49.62-
1005PhosphorylationNQTNHKPSPDQIIQP
CCCCCCCCHHHCHHH
46.0118669648
1018 (in isoform 3)Phosphorylation-60.92-
1046PhosphorylationPLILRGLTPPASYNL
CCHHCCCCCCCCCCC
30.0110470851
1050PhosphorylationRGLTPPASYNLDDDQ
CCCCCCCCCCCCCCH
21.9628857561
1051PhosphorylationGLTPPASYNLDDDQA
CCCCCCCCCCCCCHH
23.11-
1066UbiquitinationAWENELQKMTRGQLQ
HHHHHHHHHHHHHHH
55.66-

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 RB6I2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB6I2_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 RB6I2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB6A_HUMANRAB6Aphysical
11929610
RAB6B_HUMANRAB6Bphysical
11929610
NEMO_HUMANIKBKGphysical
20932476
IKKA_HUMANCHUKphysical
15218148
IKKB_HUMANIKBKBphysical
15218148
NEMO_HUMANIKBKGphysical
15218148
IKBA_HUMANNFKBIAphysical
15218148
A4_HUMANAPPphysical
21832049
VA0D1_HUMANATP6V0D1physical
22939629
WDR4_HUMANWDR4physical
22939629
ARHL2_HUMANADPRHL2physical
26344197
SNX2_HUMANSNX2physical
26344197
OFD1_HUMANOFD1physical
27173435

Drug and Disease Associations
Kegg Disease
OMIM Disease
188550Thyroid papillary carcinoma (TPC)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB6I2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.
"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-17; SER-21; SER-191 ANDTHR-1046, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-21, AND MASSSPECTROMETRY.

TOP