PROM1_HUMAN - dbPTM
PROM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PROM1_HUMAN
UniProt AC O43490
Protein Name Prominin-1
Gene Name PROM1
Organism Homo sapiens (Human).
Sequence Length 865
Subcellular Localization Apical cell membrane
Multi-pass membrane protein. Cell projection, microvillus membrane
Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate compartment.
Protein Description May play a role in cell differentiation, proliferation and apoptosis. [PubMed: 24556617 Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner]
Protein Sequence MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAGPIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKPETVILGLKIVYYEAGIILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFAISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETPEQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSMATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLVHPSSETCNSIRLSLSQLNSNPELRQLPPVDAELDNVNNVLRTDLDGLVQQGYQSLNDIPDRVQRQTTTVVAGIKRVLNSIGSDIDNVTQRLPIQDILSAFSVYVNNTESYIHRNLPTLEEYDSYWWLGGLVICSLLTLIVIFYYLGLLCGVCGYDRHATPTTRGCVSNTGGVFLMVGVGLSFLFCWILMIIVVLTFVFGANVEKLICEPYTSKELFRVLDTPYLLNEDWEYYLSGKLFNKSKMKLTFEQVYSDCKKNRGTYGTLHLQNSFNISEHLNINEHTGSISSELESLKVNLNIFLLGAAGRKNLQDFAACGIDRMNYDSYLAQTGKSPAGVNLLSFAYDLEAKANSLPPGNLRNSLKRDAQTIKTIHQQRVLPIEQSLSTLYQSVKILQRTGNGLLERVTRILASLDFAQNFITNNTSSVIIEETKKYGRTIIGYFEHYLQWIEFSISEKVASCKPVATALDTAVDVFLCSYIIDPLNLFWFGIGKATVFLLPALIFAVKLAKYYRRMDSEDVYDDVETIPMKNMENGNNGYHKDHVYGIHNPVMTSPSQH
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
34PhosphorylationDAPKAWNYELPATNY
CCCCCCCCCCCCCCC		14.24-
82AcetylationTLRKFLQKAYESKID
HHHHHHHHHHHCCCC		55.9020167786
129AcetylationLMPLVGYFFCMCRCC
HHHHHHHHHHHHHHH		2.9019413330
138AcetylationCMCRCCNKCGGEMHQ
HHHHHHCCCCCHHHH		21.9719413330
203PhosphorylationSNFKDLRTLLNETPE
CCHHHHHHHHHCCHH		42.7826074081
208PhosphorylationLRTLLNETPEQIKYI
HHHHHHCCHHHHHHH		30.9326074081
214PhosphorylationETPEQIKYILAQYNT
CCHHHHHHHHHHCCC		11.6426074081
219PhosphorylationIKYILAQYNTTKDKA
HHHHHHHCCCCCCHH		14.6326074081
220N-linked_GlycosylationKYILAQYNTTKDKAF
HHHHHHCCCCCCHHC		29.23UniProtKB CARBOHYD
221PhosphorylationYILAQYNTTKDKAFT
HHHHHCCCCCCHHCC		30.2326074081
222PhosphorylationILAQYNTTKDKAFTD
HHHHCCCCCCHHCCC		33.3426074081
225AcetylationQYNTTKDKAFTDLNS
HCCCCCCHHCCCHHH		47.1324556617
257AcetylationIPVLDEIKSMATAIK
HHHHHHHHHHHHHHH		31.9324556617
258PhosphorylationPVLDEIKSMATAIKE
HHHHHHHHHHHHHHH		21.2225954137
264AcetylationKSMATAIKETKEALE
HHHHHHHHHHHHHHH		57.7924556617
266PhosphorylationMATAIKETKEALENM
HHHHHHHHHHHHHHH		29.2317081983
274N-linked_GlycosylationKEALENMNSTLKSLH
HHHHHHHHHHHHHHH		43.34UniProtKB CARBOHYD
275PhosphorylationEALENMNSTLKSLHQ
HHHHHHHHHHHHHHH		25.0917081983
276PhosphorylationALENMNSTLKSLHQQ
HHHHHHHHHHHHHHH		32.9517081983
375PhosphorylationPDRVQRQTTTVVAGI
CHHHHHHHHHHHHHH		26.9921406692
376PhosphorylationDRVQRQTTTVVAGIK
HHHHHHHHHHHHHHH		14.8421406692
377PhosphorylationRVQRQTTTVVAGIKR
HHHHHHHHHHHHHHH		19.1721406692
395N-linked_GlycosylationSIGSDIDNVTQRLPI
HHCCCCCCHHCCCCH		38.78UniProtKB CARBOHYD
414N-linked_GlycosylationSAFSVYVNNTESYIH
HHHHHEECCCCCCCC		31.83UniProtKB CARBOHYD
548N-linked_GlycosylationYLSGKLFNKSKMKLT
HHHCCCCCHHHCEEE		59.12UniProtKB CARBOHYD
580N-linked_GlycosylationLHLQNSFNISEHLNI
EEECCCCCCCCCCCC		36.38UniProtKB CARBOHYD
691PhosphorylationRVLPIEQSLSTLYQS
CCCCHHHHHHHHHHH		16.1126503514
693PhosphorylationLPIEQSLSTLYQSVK
CCHHHHHHHHHHHHH		22.9326503514
696PhosphorylationEQSLSTLYQSVKILQ
HHHHHHHHHHHHHHH		9.9926503514
698PhosphorylationSLSTLYQSVKILQRT
HHHHHHHHHHHHHHH		16.3026503514
719PhosphorylationRVTRILASLDFAQNF
HHHHHHHHCCHHHHH		25.65-
729N-linked_GlycosylationFAQNFITNNTSSVII
HHHHHHCCCCCCEEE		44.99UniProtKB CARBOHYD
730N-linked_GlycosylationAQNFITNNTSSVIIE
HHHHHCCCCCCEEEE		32.46UniProtKB CARBOHYD
733PhosphorylationFITNNTSSVIIEETK
HHCCCCCCEEEECHH		18.46-
739PhosphorylationSSVIIEETKKYGRTI
CCEEEECHHHHCCEE		21.75-
819 (in isoform 5)Phosphorylation-7.34-
824PhosphorylationKYYRRMDSEDVYDDV
HHHHCCCCCCCCCCC		26.76-
828PhosphorylationRMDSEDVYDDVETIP
CCCCCCCCCCCCCCC		20.8126356563
828 (in isoform 6)Phosphorylation-20.81-
833PhosphorylationDVYDDVETIPMKNME
CCCCCCCCCCCCCCC		30.1726356563
852PhosphorylationGYHKDHVYGIHNPVM
CCCCCCCCCCCCCCC		13.6226356563
860PhosphorylationGIHNPVMTSPSQH--
CCCCCCCCCCCCC--		37.4126356563
861PhosphorylationIHNPVMTSPSQH---
CCCCCCCCCCCC---		12.4029116813
863PhosphorylationNPVMTSPSQH-----
CCCCCCCCCC-----		40.4224556617
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
828YPhosphorylationKinaseFYNP06241
PSP
828YPhosphorylationKinaseSRCP12931
PSP
852YPhosphorylationKinaseFYNP06241
PSP
852YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
225KAcetylation

24556617
257KAcetylation

24556617
264KAcetylation

24556617
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 PROM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDHR1_HUMANCDHR1physical
18654668
ACTB_HUMANACTBphysical
18654668
P85A_HUMANPIK3R1physical
23569237
Drug and Disease Associations
Kegg Disease
H00481 Cone-rod dystrophy and cone dystrophy, including: Cone-rod dystrophy (CORD); Cone dystrophy (COD); R
H00527 Retinitis pigmentosa (RP)
H00819 Stargardt disease (STGD); Fundus flavimaculatus
H00821 Macular degeneration, including: Age-related macular degeneration (ARMD); Patterned dystrophy of ret
OMIM Disease
612095Retinitis pigmentosa 41 (RP41)
612657Cone-rod dystrophy 12 (CORD12)
603786Stargardt disease 4 (STGD4)
608051Retinal macular dystrophy 2 (MCDR2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PROM1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-275 ANDTHR-276, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory