CCHCR_HUMAN - dbPTM
CCHCR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCHCR_HUMAN
UniProt AC Q8TD31
Protein Name Coiled-coil alpha-helical rod protein 1
Gene Name CCHCR1
Organism Homo sapiens (Human).
Sequence Length 782
Subcellular Localization Cytoplasm. Nucleus.
Protein Description May be a regulator of keratinocyte proliferation or differentiation..
Protein Sequence MFPPSGSTGLIPPSHFQARPLSTLPRMAPTWLSDIPLVQPPGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIVRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLHATAELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEGAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVTDVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPVAAAVPTRESIKGSLSVLLDDLQDLSEAISKEEAVCQGDNLDRCSSSNPQMSS
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
22PhosphorylationHFQARPLSTLPRMAP
HHCCCCCCCCCCCCC		30.4928188228
23PhosphorylationFQARPLSTLPRMAPT
HCCCCCCCCCCCCCC		48.7625106551
47PhosphorylationPPGHQDVSERRLDTQ
CCCCCCHHHHHCCCC		33.40-
88PhosphorylationLEGSQALSQQAEVIV
CCCHHHHHHHHHHHH		24.2218187866
112 (in isoform 2)Phosphorylation-50.1424719451
119 (in isoform 1)Ubiquitination-17.0221890473
119UbiquitinationRETSLQQKMRLEAQA
HHHCHHHHHHHHHHH		17.0221890473
196UbiquitinationALSSLTSKAEGLEKS
HHHHHHHHHHHHHHH		45.26-
202UbiquitinationSKAEGLEKSLSSLET
HHHHHHHHHHHHHHH		62.83-
206PhosphorylationGLEKSLSSLETRRAG
HHHHHHHHHHHHHHH		35.2022210691
208 (in isoform 2)Ubiquitination-42.0621890473
209PhosphorylationKSLSSLETRRAGEAK
HHHHHHHHHHHHHHH		30.6522210691
216UbiquitinationTRRAGEAKELAEAQR
HHHHHHHHHHHHHHH		49.29-
251UbiquitinationTLVENLRKYVGEQVP
HHHHHHHHHCCCCCC		47.67-
305 (in isoform 2)Ubiquitination-2.78-
315UbiquitinationQEEELTRKVQPSDSL
CHHHHHHCCCCCCCC		39.73-
319PhosphorylationLTRKVQPSDSLEPEF
HHHCCCCCCCCCHHH		23.81-
321PhosphorylationRKVQPSDSLEPEFTR
HCCCCCCCCCHHHHH		38.68-
327PhosphorylationDSLEPEFTRKCQSLL
CCCCHHHHHHHHHHH		27.79-
329UbiquitinationLEPEFTRKCQSLLNR
CCHHHHHHHHHHHHH		33.30-
340 (in isoform 2)Ubiquitination-33.79-
360UbiquitinationLEHSDSVKQLKGQVA
HCCCHHHHHHHHHHH		54.59-
363UbiquitinationSDSVKQLKGQVASLQ
CHHHHHHHHHHHHHH		44.82-
372UbiquitinationQVASLQEKVTSQSQE
HHHHHHHHHCCHHHH		37.54-
386PhosphorylationEQAILQRSLQDKAAE
HHHHHHHHHHHHHHH		19.88-
390UbiquitinationLQRSLQDKAAEVEVE
HHHHHHHHHHHHHHH		36.2121906983
402UbiquitinationEVERMGAKGLQLELS
HHHHHCCCHHHHHHH		55.19-
404 (in isoform 2)Ubiquitination-5.31-
437PhosphorylationRLVVNAVSSSQIWLE
HHHHHHHCCCHHHHH		23.1229052541
438PhosphorylationLVVNAVSSSQIWLET
HHHHHHCCCHHHHHH		21.4729052541
439PhosphorylationVVNAVSSSQIWLETT
HHHHHCCCHHHHHHH		20.4122210691
446PhosphorylationSQIWLETTMAKVEGA
CHHHHHHHHHHHHHH		13.0322210691
449 (in isoform 2)Ubiquitination-29.96-
452 (in isoform 2)Ubiquitination-24.41-
459PhosphorylationGAAAQLPSLNNRLSY
HHHHHCCCHHHHHHH		52.93-
479 (in isoform 2)Ubiquitination-13.96-
481UbiquitinationIRGLIARKLALAQLR
HHHHHHHHHHHHHHH		29.14-
491 (in isoform 2)Ubiquitination-16.82-
522PhosphorylationLDAELQLSARLIQQE
HHHHHHHHHHHHHHH		9.81-
570 (in isoform 2)Ubiquitination-22.59-
604UbiquitinationYGQALQEKVAEVETR
HHHHHHHHHHHHHHH		33.51-
610PhosphorylationEKVAEVETRLREQLS
HHHHHHHHHHHHHHH		39.9328842319
617PhosphorylationTRLREQLSDTERRLN
HHHHHHHHHHHHHHH		42.0328842319
632UbiquitinationEARREHAKAVVSLRQ
HHHHHHHHHHHHHHH		43.55-
680UbiquitinationLQELERDKNLMLATL
HHHHHHHHCHHHHHH		59.1921906983
686PhosphorylationDKNLMLATLQQEGLL
HHCHHHHHHHHHCHH		22.5723186163
703PhosphorylationYKQQRLLTVLPSLLD
HHHHHHHHHHHHHHH		25.29-
707PhosphorylationRLLTVLPSLLDKKKS
HHHHHHHHHHHHCCC		37.09-
711UbiquitinationVLPSLLDKKKSVVSS
HHHHHHHHCCCCCCC		63.17-
713UbiquitinationPSLLDKKKSVVSSPR
HHHHHHCCCCCCCCC		54.98-
714PhosphorylationSLLDKKKSVVSSPRP
HHHHHCCCCCCCCCC		36.3128111955
717PhosphorylationDKKKSVVSSPRPPEC
HHCCCCCCCCCCCCC		32.2528111955
718PhosphorylationKKKSVVSSPRPPECS
HCCCCCCCCCCCCCC		17.2028111955
725PhosphorylationSPRPPECSASAPVAA
CCCCCCCCCCCCEEE		24.4822468782
727PhosphorylationRPPECSASAPVAAAV
CCCCCCCCCCEEEEC		19.4628111955
736PhosphorylationPVAAAVPTRESIKGS
CEEEECCCHHHHHHH		40.2322468782
769 (in isoform 2)Ubiquitination-51.14-
775PhosphorylationDNLDRCSSSNPQMSS
CCCCCCCCCCCCCCC		37.45-
776PhosphorylationNLDRCSSSNPQMSS-
CCCCCCCCCCCCCC-		35.91-
781PhosphorylationSSSNPQMSS------
CCCCCCCCC------		27.87-
782PhosphorylationSSNPQMSS-------
CCCCCCCC-------		38.61-
800 (in isoform 2)Ubiquitination--
802 (in isoform 2)Ubiquitination--
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 CCHCR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCHCR_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 CCHCR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB3_HUMANPOLR2Cphysical
16141233
DPOD2_HUMANPOLD2physical
21988832
NEMO_HUMANIKBKGphysical
21988832
CCHCR_HUMANCCHCR1physical
25416956
CEP55_HUMANCEP55physical
25416956
CARD9_HUMANCARD9physical
25416956
CC136_HUMANCCDC136physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
EFHC2_HUMANEFHC2physical
25416956
TSG10_HUMANTSGA10physical
25416956
NDEL1_HUMANNDEL1physical
25416956
TEKT1_HUMANTEKT1physical
25416956
USBP1_HUMANUSHBP1physical
25416956
DTBP1_HUMANDTNBP1physical
25416956
ANCHR_HUMANZFYVE19physical
25416956
CA094_HUMANC1orf94physical
25416956
SPF45_HUMANRBM17physical
25416956
HAUS1_HUMANHAUS1physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
FSD2_HUMANFSD2physical
25416956
K1C40_HUMANKRT40physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
TXLNA_HUMANTXLNAphysical
25416956
NUTM1_HUMANNUTM1physical
25416956
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
TUFT1_HUMANTUFT1physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RABX5_HUMANRABGEF1physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
NUF2_HUMANNUF2physical
27173435
THA11_HUMANTHAP11physical
27173435
EIPR1_HUMANTSSC1physical
27173435
VPS51_HUMANVPS51physical
27173435
RABE1_HUMANRABEP1physical
27173435
STRN_HUMANSTRNphysical
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 CCHCR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.

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