IKIP_HUMAN - dbPTM
IKIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IKIP_HUMAN
UniProt AC Q70UQ0
Protein Name Inhibitor of nuclear factor kappa-B kinase-interacting protein
Gene Name IKBIP
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Isoform 4 deletion of the hydrophobic, or transmembrane region between AA 45-63 results in uniform distribution throughout the cell, suggesting that this region is responsible for endopl
Protein Description Target of p53/TP53 with pro-apoptotic function..
Protein Sequence MSEVKSRKKSGPKGAPAAEPGKRSEGGKTPVARSSGGGGWADPRTCLSLLSLGTCLGLAWFVFQQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKWQKSEAIMEQLKSFQIIAHLKRLQEEINEVKTWSNRITEKQDILNNSLTTLSQDITKVDQSTTSMAKDVGLKITSVKTDIRRISGLVTDVISLTDSVQELENKIEKVEKNTVKNIGDLLSSSIDRTATLRKTASENSQRINSVKKTLTELKSDFDKHTDRFLSLEGDRAKVLKTVTFANDLKPKVYNLKKDFSRLEPLVNDLTLRIGRLVTDLLQREKEIAFLSEKISNLTIVQAEIKDIKDEIAHISDMN
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
10PhosphorylationEVKSRKKSGPKGAPA
CHHCCCCCCCCCCCC		64.4624719451
13UbiquitinationSRKKSGPKGAPAAEP
CCCCCCCCCCCCCCC		71.8333845483
22UbiquitinationAPAAEPGKRSEGGKT
CCCCCCCCCCCCCCC		64.5633845483
24PhosphorylationAAEPGKRSEGGKTPV
CCCCCCCCCCCCCCC		44.0425159151
28UbiquitinationGKRSEGGKTPVARSS
CCCCCCCCCCCCCCC		61.5924816145
76PhosphorylationFAKVENQYQLLKLET
HHHHHHHHHHHHHCC		16.83-
80UbiquitinationENQYQLLKLETNEFQ
HHHHHHHHHCCCHHH		53.5229967540
92UbiquitinationEFQQLQSKISLISEK
HHHHHHHHHHHHCHH		24.2921963094
92 (in isoform 4)Ubiquitination-24.29-
922-HydroxyisobutyrylationEFQQLQSKISLISEK
HHHHHHHHHHHHCHH		24.29-
97PhosphorylationQSKISLISEKWQKSE
HHHHHHHCHHHHHHH		38.1224719451
99AcetylationKISLISEKWQKSEAI
HHHHHCHHHHHHHHH		48.4027452117
103PhosphorylationISEKWQKSEAIMEQL
HCHHHHHHHHHHHHH		19.7030622161
144N-linked_GlycosylationTEKQDILNNSLTTLS
HHHHHHHHCHHHHHH		36.0619159218
160PhosphorylationDITKVDQSTTSMAKD
CHHHCCHHHHHHHHH		29.2329759185
161PhosphorylationITKVDQSTTSMAKDV
HHHCCHHHHHHHHHH		19.7729759185
162PhosphorylationTKVDQSTTSMAKDVG
HHCCHHHHHHHHHHC		23.0429759185
163PhosphorylationKVDQSTTSMAKDVGL
HCCHHHHHHHHHHCC		19.4822210691
173PhosphorylationKDVGLKITSVKTDIR
HHHCCEEEECHHHHH		26.3629759185
174PhosphorylationDVGLKITSVKTDIRR
HHCCEEEECHHHHHH		25.7029759185
183PhosphorylationKTDIRRISGLVTDVI
HHHHHHHHCHHHHHH		25.02-
187PhosphorylationRRISGLVTDVISLTD
HHHHCHHHHHHHHHH		29.59-
191PhosphorylationGLVTDVISLTDSVQE
CHHHHHHHHHHHHHH		25.68-
193PhosphorylationVTDVISLTDSVQELE
HHHHHHHHHHHHHHH		21.31-
203UbiquitinationVQELENKIEKVEKNT
HHHHHHHHHHHHHHH		10.5129967540
212UbiquitinationKVEKNTVKNIGDLLS
HHHHHHHCCHHHHHH		40.59-
219PhosphorylationKNIGDLLSSSIDRTA
CCHHHHHHHHHCCHH		29.3621712546
220PhosphorylationNIGDLLSSSIDRTAT
CHHHHHHHHHCCHHH		31.1421712546
221PhosphorylationIGDLLSSSIDRTATL
HHHHHHHHHCCHHHH		25.73-
225PhosphorylationLSSSIDRTATLRKTA
HHHHHCCHHHHHHHH		21.90-
236UbiquitinationRKTASENSQRINSVK
HHHHHHHHHHHHHHH		19.4532015554
240UbiquitinationSENSQRINSVKKTLT
HHHHHHHHHHHHHHH		42.8329967540
241PhosphorylationENSQRINSVKKTLTE
HHHHHHHHHHHHHHH		32.7024719451
247PhosphorylationNSVKKTLTELKSDFD
HHHHHHHHHHHHHHH		44.49-
258UbiquitinationSDFDKHTDRFLSLEG
HHHHHCHHHHHHCCC		38.7729967540
281AcetylationVTFANDLKPKVYNLK
HHCCCCCCHHHCCCC		45.7327452117
295UbiquitinationKKDFSRLEPLVNDLT
CCCHHHHHHHHHHHH		35.1632015554
3172-HydroxyisobutyrylationTDLLQREKEIAFLSE
HHHHHHHHHHHHHHH		57.52-
328N-linked_GlycosylationFLSEKISNLTIVQAE
HHHHHHHCCEEEEHH		44.6819159218
330 (in isoform 4)Phosphorylation-24.29-
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 IKIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
154NGlycosylation

31953408
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 IKIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NDUB6_HUMANNDUFB6physical
22939629
RUSD4_HUMANRPUSD4physical
22939629
TMED4_HUMANTMED4physical
22939629
OXA1L_HUMANOXA1Lphysical
22939629
SRSF5_HUMANSRSF5physical
22939629
PDCD6_HUMANPDCD6physical
22939629
SFXN2_HUMANSFXN2physical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
TPM3_HUMANTPM3physical
21516116
TNIP1_HUMANTNIP1physical
28514442
BORC7_HUMANC10orf32physical
28514442
PCNT_HUMANPCNTphysical
28514442
VPS52_HUMANVPS52physical
28514442
EXOC1_HUMANEXOC1physical
28514442
ABI1_HUMANABI1physical
28514442
NCKP1_HUMANNCKAP1physical
28514442
AGGF1_HUMANAGGF1physical
28514442
ATG5_HUMANATG5physical
28514442
A16L1_HUMANATG16L1physical
28514442
ABI2_HUMANABI2physical
28514442
BORC5_HUMANLOH12CR1physical
28514442
CYFP2_HUMANCYFIP2physical
28514442
TRAF7_HUMANTRAF7physical
28514442
BL1S1_HUMANBLOC1S1physical
28514442
PAWR_HUMANPAWRphysical
28514442
CK5P2_HUMANCDK5RAP2physical
28514442
BL1S2_HUMANBLOC1S2physical
28514442
EXOC4_HUMANEXOC4physical
28514442
CYFP1_HUMANCYFIP1physical
28514442
SNAPN_HUMANSNAPINphysical
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 IKIP_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144 AND ASN-328, AND MASSSPECTROMETRY.

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