CRUM1_HUMAN - dbPTM
CRUM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRUM1_HUMAN
UniProt AC P82279
Protein Name Protein crumbs homolog 1
Gene Name CRB1
Organism Homo sapiens (Human).
Sequence Length 1406
Subcellular Localization Isoform 1: Apical cell membrane
Single-pass type I membrane protein. Distributed at the apical membrane of all retinal epithelial cells. Located in the apical membrane of the adherens junction in outer limiting membrane (OLM) of the retina.
Isoform
Protein Description Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion..
Protein Sequence MALKNINYLLIFYLSFSLLIYIKNSFCNKNNTRCLSNSCQNNSTCKDFSKDNDCSCSDTANNLDKDCDNMKDPCFSNPCQGSATCVNTPGERSFLCKCPPGYSGTICETTIGSCGKNSCQHGGICHQDPIYPVCICPAGYAGRFCEIDHDECASSPCQNGAVCQDGIDGYSCFCVPGYQGRHCDLEVDECASDPCKNEATCLNEIGRYTCICPHNYSGVNCELEIDECWSQPCLNGATCQDALGAYFCDCAPGFLGDHCELNTDECASQPCLHGGLCVDGENRYSCNCTGSGFTGTHCETLMPLCWSKPCHNNATCEDSVDNYTCHCWPGYTGAQCEIDLNECNSNPCQSNGECVELSSEKQYGRITGLPSSFSYHEASGYVCICQPGFTGIHCEEDVNECSSNPCQNGGTCENLPGNYTCHCPFDNLSRTFYGGRDCSDILLGCTHQQCLNNGTCIPHFQDGQHGFSCLCPSGYTGSLCEIATTLSFEGDGFLWVKSGSVTTKGSVCNIALRFQTVQPMALLLFRSNRDVFVKLELLSGYIHLSIQVNNQSKVLLFISHNTSDGEWHFVEVIFAEAVTLTLIDDSCKEKCIAKAPTPLESDQSICAFQNSFLGGLPVGMTSNGVALLNFYNMPSTPSFVGCLQDIKIDWNHITLENISSGSSLNVKAGCVRKDWCESQPCQSRGRCINLWLSYQCDCHRPYEGPNCLREYVAGRFGQDDSTGYVIFTLDESYGDTISLSMFVRTLQPSGLLLALENSTYQYIRVWLERGRLAMLTPNSPKLVVKFVLNDGNVHLISLKIKPYKIELYQSSQNLGFISASTWKIEKGDVIYIGGLPDKQETELNGGFFKGCIQDVRLNNQNLEFFPNPTNNASLNPVLVNVTQGCAGDNSCKSNPCHNGGVCHSRWDDFSCSCPALTSGKACEEVQWCGFSPCPHGAQCQPVLQGFECIANAVFNGQSGQILFRSNGNITRELTNITFGFRTRDANVIILHAEKEPEFLNISIQDSRLFFQLQSGNSFYMLSLTSLQSVNDGTWHEVTLSMTDPLSQTSRWQMEVDNETPFVTSTIATGSLNFLKDNTDIYVGDRAIDNIKGLQGCLSTIEIGGIYLSYFENVHGFINKPQEEQFLKISTNSVVTGCLQLNVCNSNPCLHGGNCEDIYSSYHCSCPLGWSGKHCELNIDECFSNPCIHGNCSDRVAAYHCTCEPGYTGVNCEVDIDNCQSHQCANGATCISHTNGYSCLCFGNFTGKFCRQSRLPSTVCGNEKTNLTCYNGGNCTEFQTELKCMCRPGFTGEWCEKDIDECASDPCVNGGLCQDLLNKFQCLCDVAFAGERCEVDLADDLISDIFTTIGSVTVALLLILLLAIVASVVTSNKRATQGTYSPSRQEKEGSRVEMWNLMPPPAMERLI
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
30N-linked_GlycosylationKNSFCNKNNTRCLSN
HHHHCCCCCCEECCC		40.91UniProtKB CARBOHYD
41N-linked_GlycosylationCLSNSCQNNSTCKDF
ECCCHHCCCCCCCCC		49.07UniProtKB CARBOHYD
42N-linked_GlycosylationLSNSCQNNSTCKDFS
CCCHHCCCCCCCCCC		16.90UniProtKB CARBOHYD
215N-linked_GlycosylationYTCICPHNYSGVNCE
EEEECCCCCCCCCEE		20.15UniProtKB CARBOHYD
287N-linked_GlycosylationGENRYSCNCTGSGFT
CCCCEEEECCCCCCC		22.05UniProtKB CARBOHYD
313N-linked_GlycosylationWSKPCHNNATCEDSV
CCCCCCCCCCCCCCC		16.98UniProtKB CARBOHYD
322N-linked_GlycosylationTCEDSVDNYTCHCWP
CCCCCCCCEEEEECC		31.68UniProtKB CARBOHYD
418N-linked_GlycosylationTCENLPGNYTCHCPF
CCCCCCCCEEEECCC		27.31UniProtKB CARBOHYD
427N-linked_GlycosylationTCHCPFDNLSRTFYG
EEECCCCCCCCCEEC		40.05UniProtKB CARBOHYD
453N-linked_GlycosylationTHQQCLNNGTCIPHF
CCHHHHCCCEEECCC		33.91UniProtKB CARBOHYD
550N-linked_GlycosylationHLSIQVNNQSKVLLF
EEEEEECCCCEEEEE		48.96UniProtKB CARBOHYD
561N-linked_GlycosylationVLLFISHNTSDGEWH
EEEEEEECCCCCCEE		34.19UniProtKB CARBOHYD
657N-linked_GlycosylationWNHITLENISSGSSL
CCEEEEEECCCCCCE		42.42UniProtKB CARBOHYD
721PhosphorylationGRFGQDDSTGYVIFT
CCCCCCCCCCEEEEE		31.83-
722PhosphorylationRFGQDDSTGYVIFTL
CCCCCCCCCEEEEEE		39.26-
757N-linked_GlycosylationGLLLALENSTYQYIR
CEEEEEECCCHHHHH		40.27UniProtKB CARBOHYD
776PhosphorylationRGRLAMLTPNSPKLV
HCCEEEECCCCCCEE		13.8229396449
779PhosphorylationLAMLTPNSPKLVVKF
EEEECCCCCCEEEEE		25.3129396449
797PhosphorylationDGNVHLISLKIKPYK
CCCEEEEEEEEECEE		29.9424719451
871N-linked_GlycosylationFFPNPTNNASLNPVL
CCCCCCCCCCCCCEE		33.13UniProtKB CARBOHYD
880N-linked_GlycosylationSLNPVLVNVTQGCAG
CCCCEEEECCCCCCC		27.27UniProtKB CARBOHYD
968N-linked_GlycosylationILFRSNGNITRELTN
EEEECCCCCCEEEEE		36.39UniProtKB CARBOHYD
975N-linked_GlycosylationNITRELTNITFGFRT
CCCEEEEEEEEEEEC		43.88UniProtKB CARBOHYD
1000N-linked_GlycosylationEKEPEFLNISIQDSR
CCCCCEEEEEEECCE		31.14UniProtKB CARBOHYD
1190N-linked_GlycosylationSNPCIHGNCSDRVAA
CCCCCCCCCHHHEEE		14.14UniProtKB CARBOHYD
1243N-linked_GlycosylationYSCLCFGNFTGKFCR
EEEEEECCCCCCCCC		15.85UniProtKB CARBOHYD
1265N-linked_GlycosylationVCGNEKTNLTCYNGG
CCCCCCCCEEEECCC		44.41UniProtKB CARBOHYD
1273N-linked_GlycosylationLTCYNGGNCTEFQTE
EEEECCCCCCEEEEE		30.82UniProtKB CARBOHYD
1378PhosphorylationNKRATQGTYSPSRQE
CCCCCCCCCCCCCCC		15.82-
1380PhosphorylationRATQGTYSPSRQEKE
CCCCCCCCCCCCCCC		19.0825627689
1389PhosphorylationSRQEKEGSRVEMWNL
CCCCCCCCCCCCCCC		33.9524043423
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 CRUM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRUM1_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 CRUM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CRUM1_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRUM1_HUMAN

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Related Literatures of Post-Translational Modification

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