PRLR_HUMAN - dbPTM
PRLR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRLR_HUMAN
UniProt AC P16471
Protein Name Prolactin receptor
Gene Name PRLR
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Membrane
Single-pass type I membrane protein .
Isoform 7: Secreted.
Protein Description This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling..
Protein Sequence MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPPVPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGMKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANPSTFYDPEVIEKPENPETTHTWDPQCISMEGKIPYFHAGGSKCSTWPLPQPSQHNPRSSYHNITDVCELAVGPAGAPATLLNEAGKDALKSSQTIKSREEGKATQQREVESFHSETDQDTPWLLPQEKTPFGSAKPLDYVEIHKVNKDGALSLLPKQRENSGKPKKPGTPENNKEYAKVSGVMDNNILVLVPDPHAKNVACFEESAKEAPPSLEQNQAEKALANFTATSSKCRLQLGGLDYLDPACFTHSFH
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
59N-linked_GlycosylationTDGGLPTNYSLTYHR
CCCCCCCEEEEEEEC		23.589544990
59N-linked_GlycosylationTDGGLPTNYSLTYHR
CCCCCCCEEEEEEEC		23.58UniProtKB CARBOHYD
104N-linked_GlycosylationRTYIMMVNATNQMGS
EEEEEECCCCCCCCC		24.13UniProtKB CARBOHYD
104N-linked_GlycosylationRTYIMMVNATNQMGS
EEEEEECCCCCCCCC		24.139544990
195PhosphorylationQTEFKILSLHPGQKY
CCEEEEEEECCCCEE		28.27-
202PhosphorylationSLHPGQKYLVQVRCK
EECCCCEEEEEEEEC		12.29-
233N-linked_GlycosylationIPSDFTMNDTTVWIS
CCCCCCCCCCCHHHH		40.18UniProtKB CARBOHYD
233N-linked_GlycosylationIPSDFTMNDTTVWIS
CCCCCCCCCCCHHHH		40.189544990
277AcetylationPVPGPKIKGFDAHLL
CCCCCCCCCCHHHHH		60.7020962278
339AcetylationEHPSQGMKPTYLDPD
CCCCCCCCCCEECCC		40.8220962278
341PhosphorylationPSQGMKPTYLDPDTD
CCCCCCCCEECCCCC		31.0626356563
342PhosphorylationSQGMKPTYLDPDTDS
CCCCCCCEECCCCCC		20.0326356563
349PhosphorylationYLDPDTDSGRGSCDS
EECCCCCCCCCCCCC		32.2716278670
356PhosphorylationSGRGSCDSPSLLSEK
CCCCCCCCHHHHHHH		22.2525849741
357 (in isoform 4)Methylation-18.75-
358PhosphorylationRGSCDSPSLLSEKCE
CCCCCCHHHHHHHCC		45.9930278072
361PhosphorylationCDSPSLLSEKCEEPQ
CCCHHHHHHHCCCCC		40.0624719451
369 (in isoform 4)Methylation-40.39-
405PhosphorylationSMEGKIPYFHAGGSK
ECCCCCCEEECCCCC		16.0927642862
412AcetylationYFHAGGSKCSTWPLP
EEECCCCCCCCCCCC		35.1620962278
414PhosphorylationHAGGSKCSTWPLPQP
ECCCCCCCCCCCCCC		36.9228348404
415PhosphorylationAGGSKCSTWPLPQPS
CCCCCCCCCCCCCCC		40.3422817900
428PhosphorylationPSQHNPRSSYHNITD
CCCCCCCCCCCCCCH		36.1828450419
429PhosphorylationSQHNPRSSYHNITDV
CCCCCCCCCCCCCHH		31.5228450419
430PhosphorylationQHNPRSSYHNITDVC
CCCCCCCCCCCCHHH		10.5128450419
434PhosphorylationRSSYHNITDVCELAV
CCCCCCCCHHHHHCC		27.9128450419
456AcetylationTLLNEAGKDALKSSQ
HHHHHHHHHHHHCCH		47.0420962278
461PhosphorylationAGKDALKSSQTIKSR
HHHHHHHCCHHHHHH		28.6425849741
462PhosphorylationGKDALKSSQTIKSRE
HHHHHHCCHHHHHHH		29.7425849741
464PhosphorylationDALKSSQTIKSREEG
HHHHCCHHHHHHHCC		32.1128450419
466AcetylationLKSSQTIKSREEGKA
HHCCHHHHHHHCCCC		47.0120962278
472AcetylationIKSREEGKATQQREV
HHHHHCCCCCCHHHH		52.0920962278
481PhosphorylationTQQREVESFHSETDQ
CCHHHHHHHHCCCCC		33.1728348404
484PhosphorylationREVESFHSETDQDTP
HHHHHHHCCCCCCCC		39.9328348404
486PhosphorylationVESFHSETDQDTPWL
HHHHHCCCCCCCCCC		41.8128348404
490PhosphorylationHSETDQDTPWLLPQE
HCCCCCCCCCCCCCC		15.6728348404
503PhosphorylationQEKTPFGSAKPLDYV
CCCCCCCCCCCCCEE		33.2326356563
505AcetylationKTPFGSAKPLDYVEI
CCCCCCCCCCCEEEE		48.0520962278
509PhosphorylationGSAKPLDYVEIHKVN
CCCCCCCEEEEEEEC		13.9926356563
514AcetylationLDYVEIHKVNKDGAL
CCEEEEEEECCCCHH		53.8420962278
517AcetylationVEIHKVNKDGALSLL
EEEEEECCCCHHHCC		61.6020962278
522PhosphorylationVNKDGALSLLPKQRE
ECCCCHHHCCCCCCC		27.5922199227
526AcetylationGALSLLPKQRENSGK
CHHHCCCCCCCCCCC		63.0520962278
533AcetylationKQRENSGKPKKPGTP
CCCCCCCCCCCCCCC		54.1820962278
536AcetylationENSGKPKKPGTPENN
CCCCCCCCCCCCCCC		58.1520962278
567AcetylationLVPDPHAKNVACFEE
EECCCCCCCCHHHHH		49.2520962278
590AcetylationLEQNQAEKALANFTA
HHHHHHHHHHHHHHH		52.2820962278
600PhosphorylationANFTATSSKCRLQLG
HHHHHCCCCEEEEEC		31.27-
601AcetylationNFTATSSKCRLQLGG
HHHHCCCCEEEEECC		24.1220962278
611PhosphorylationLQLGGLDYLDPACFT
EEECCCCCCCHHHCC		20.327537382
618PhosphorylationYLDPACFTHSFH---
CCCHHHCCCCCC---		19.2526356563
620PhosphorylationDPACFTHSFH-----
CHHHCCCCCC-----		23.2026356563
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
349SPhosphorylationKinaseJAK2O60674
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:15082796
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:15082796
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRLR_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 PRLR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPIA_HUMANPPIAphysical
12668872
TEC_HUMANTECphysical
11328862
VAV_HUMANVAV1physical
11328862
VAV_HUMANVAV1physical
7768923
JAK2_HUMANJAK2physical
9202403
PTN11_HUMANPTPN11physical
10991949
TF3A_HUMANGTF3Aphysical
18573876
FBW1B_HUMANFBXW11physical
15082796
CBP_HUMANCREBBPphysical
20962278
PRLR_HUMANPRLRphysical
20962278
FBW1A_HUMANBTRCphysical
16278670
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615554Multiple fibroadenomas of the breast (MFAB)
615555Hyperprolactinemia (HPRL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRLR_HUMAN

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Related Literatures of Post-Translational Modification

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