CH034_HUMAN - dbPTM
CH034_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CH034_HUMAN
UniProt AC Q49A92
Protein Name Uncharacterized protein C8orf34
Gene Name C8orf34
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization
Protein Description
Protein Sequence MSSPLASELSELAALRPGFRLSAPHARVAPRAATHARGRGRASHAGQPRLRSSCPGPSPGKRRVVPSGGAQPRVLPALSSRSHLFPMASHPQTRIQAYLEKNKIGPLFEELMTKLITETPDQPIPFLIDHLQSKQGNRGQLQRTLSGSAALWAESEKSESKGTRRDFRSYDKPWQLNAKKPKKSKSDLAVSNISPPSPDSKSLPRSVEHPKWNWRTKPQSRDFDELNHILQESKKLGKALENLSRSIAISDELDKETVTFNSSLLRPRVIGEWIGREENDADPLAAEMLQPPIPRSKNDQWESEDSGSSPAGSLKMEPKNKGLKQQQQQHKKLLAAMLSQDSFESIHSPTPSVTEEDIDNEDDAMELLEDLNDLRMEGVTTLVPSGSKFNQGRPTYPAEPQAKVTLNICSRCARLQGDNLEERTEESLPILHSPDEKIPDSFDSLPGTEEALMEEGDEFEKASKLTGPGEASSGVGHSLKNYMEEDESLKQLQVVHQPWILPSDTESEGVEAEQEKRSADLLLCVPCSSCPTLVYSGL
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
2 (in isoform 6)Phosphorylation-19.2927732954
3 (in isoform 6)Phosphorylation-34.1127732954
3Phosphorylation-----MSSPLASELS
-----CCCHHHHHHH
34.1129514088
7 (in isoform 6)Phosphorylation-33.9027732954
7Phosphorylation-MSSPLASELSELAA
-CCCHHHHHHHHHHH
33.9029514088
10 (in isoform 6)Phosphorylation-22.2124719451
10PhosphorylationSPLASELSELAALRP
CHHHHHHHHHHHHCC
22.2124719451
12PhosphorylationLASELSELAALRPGF
HHHHHHHHHHHCCCC
10.0629514088
33PhosphorylationARVAPRAATHARGRG
CCCCCCHHHHHCCCC
24.4225332170
72PhosphorylationVPSGGAQPRVLPALS
CCCCCCCCCCHHCCC
42.95-
83PhosphorylationPALSSRSHLFPMASH
HCCCCCCCCCCCCCC
37.36-
84PhosphorylationALSSRSHLFPMASHP
CCCCCCCCCCCCCCC
24.59-
98PhosphorylationPQTRIQAYLEKNKIG
CHHHHHHHHHHCCCH
43.4428857561
108PhosphorylationKNKIGPLFEELMTKL
HCCCHHHHHHHHHHH
34.70-
111PhosphorylationIGPLFEELMTKLITE
CHHHHHHHHHHHHHC
44.7328857561
114PhosphorylationLFEELMTKLITETPD
HHHHHHHHHHHCCCC
27.7724719451
158PhosphorylationLWAESEKSESKGTRR
HHHHCCCCCCCCCCC
35.25-
177PhosphorylationYDKPWQLNAKKPKKS
CCCCCCCCCCCCCCC
32.3124719451
197PhosphorylationVSNISPPSPDSKSLP
CCCCCCCCCCCCCCC
26.1419413330
210PhosphorylationLPRSVEHPKWNWRTK
CCCCCCCCCCCCCCC
30.3824719451
220PhosphorylationNWRTKPQSRDFDELN
CCCCCCCCCCHHHHH
36.2023532336
233AcetylationLNHILQESKKLGKAL
HHHHHHHHHHHHHHH
58.97-
235AcetylationHILQESKKLGKALEN
HHHHHHHHHHHHHHH
72.287834081
301PhosphorylationPRSKNDQWESEDSGS
CCCCCCCCCCCCCCC
38.1132142685
347PhosphorylationQDSFESIHSPTPSVT
HHCHHHCCCCCCCCC
30.5122985185
378AcetylationLNDLRMEGVTTLVPS
HHHHHHCCCEEECCC
55.73-
386PhosphorylationVTTLVPSGSKFNQGR
CEEECCCCCCCCCCC
24.2728634298
387PhosphorylationTTLVPSGSKFNQGRP
EEECCCCCCCCCCCC
44.5428634298
392PhosphorylationSGSKFNQGRPTYPAE
CCCCCCCCCCCCCCC
34.8023186163
419PhosphorylationCARLQGDNLEERTEE
HHHHCCCCHHHHCHH
45.83-

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 CH034_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CH034_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 CH034_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CH034_HUMANC8orf34physical
25416956
ASB7_HUMANASB7physical
26186194
CNDP2_HUMANCNDP2physical
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 CH034_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASSSPECTROMETRY.

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