PP16B_HUMAN - dbPTM
PP16B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP16B_HUMAN
UniProt AC Q96T49
Protein Name Protein phosphatase 1 regulatory inhibitor subunit 16B
Gene Name PPP1R16B
Organism Homo sapiens (Human).
Sequence Length 567
Subcellular Localization Cell membrane . Cell membrane
Lipid-anchor . Nucleus . Cell projection . Colocalizes with RPSA/LAMR1 in the cell membrane (PubMed:16263087). Localizes to the perinuclear region (By similarity). Colocalizes with PTEN at the tip of EC projections (Pu
Protein Description Regulator of protein phosphatase 1 (PP1) that acts as a positive regulator of pulmonary endothelial cell (EC) barrier function. [PubMed: 18586956 Involved in the regulation of the PI3K/AKT signaling pathway, angiogenesis and endothelial cell proliferation]
Protein Sequence MASHVDLLTELQLLEKVPTLERLRAAQKRRAQQLKKWAQYEQDLQHRKRKHERKRSTGGRRKKVSFEASVALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEKINEMRVAPEQQMIADIHCMIAAGQDLDWIDAQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMQMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVLLLELKHKHDVIMKSQLRHKSSLSRRTSSAGSRGKVVRRASLSDRTNLYRKEYEGEAILWQRSAAEDQRTSTYNGDIRETRTDQENKDPNPRLEKPVLLSEFPTKIPRGELDMPVENGLRAPVSAYQYALANGDVWKVHEVPDYSMAYGNPGVADATPPWSSYKEQSPQTLLELKRQRAAAKLLSHPFLSTHLGSSMARTGESSSEGKAPLIGGRTSPYSSNGTSVYYTVTSGDPPLLKFKAPIEEMEEKVHGCCRIS
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
16UbiquitinationTELQLLEKVPTLERL
HHHHHHHHCCCHHHH		54.1830230243
19PhosphorylationQLLEKVPTLERLRAA
HHHHHCCCHHHHHHH		44.2127067055
36UbiquitinationRRAQQLKKWAQYEQD
HHHHHHHHHHHHHHH		57.2529967540
56PhosphorylationRKHERKRSTGGRRKK
HHHHHHHCCCCCCCC		34.14-
69PhosphorylationKKVSFEASVALLEAS
CCCCHHHHHHHHHHH		10.75-
130UbiquitinationHGANVNAKDNELWTP
CCCCCCCCCCCCCCH		56.7529967540
281UbiquitinationQMQMAELLVSHGASL
HHHHHHHHHHCCCCC		2.5329967540
318UbiquitinationLLELKHKHDVIMKSQ
HHHHHHCCCHHHHHH		34.0029967540
323UbiquitinationHKHDVIMKSQLRHKS
HCCCHHHHHHHCCHH		24.7529967540
324PhosphorylationKHDVIMKSQLRHKSS
CCCHHHHHHHCCHHH		19.6427251275
331PhosphorylationSQLRHKSSLSRRTSS
HHHCCHHHHCCCCCC		34.86-
333PhosphorylationLRHKSSLSRRTSSAG
HCCHHHHCCCCCCCC		22.97-
337PhosphorylationSSLSRRTSSAGSRGK
HHHCCCCCCCCCCCC		19.17-
350PhosphorylationGKVVRRASLSDRTNL
CCEEEECCCCCCCCC		26.9623403867
360UbiquitinationDRTNLYRKEYEGEAI
CCCCCCHHHHCCCEE		51.6029967540
362UbiquitinationTNLYRKEYEGEAILW
CCCCHHHHCCCEEEE		32.0629967540
372UbiquitinationEAILWQRSAAEDQRT
CEEEEECCHHHCCCC		19.4130230243
382PhosphorylationEDQRTSTYNGDIRET
HCCCCCCCCCCCCCC		19.54-
404UbiquitinationDPNPRLEKPVLLSEF
CCCCCCCCCEEHHCC		45.0529967540
414UbiquitinationLLSEFPTKIPRGELD
EHHCCCCCCCCCCCC		51.4530230243
435PhosphorylationLRAPVSAYQYALANG
CCCCCHHHHHHHHCC		8.44-
437PhosphorylationAPVSAYQYALANGDV
CCCHHHHHHHHCCCC		7.3029978859
442UbiquitinationYQYALANGDVWKVHE
HHHHHHCCCCEEEEE		25.8229967540
453PhosphorylationKVHEVPDYSMAYGNP
EEEECCCCHHHCCCC		8.3525884760
475UbiquitinationPWSSYKEQSPQTLLE
CCHHHCCCCHHHHHH		57.1530230243
476PhosphorylationWSSYKEQSPQTLLEL
CHHHCCCCHHHHHHH		21.7730108239
479PhosphorylationYKEQSPQTLLELKRQ
HCCCCHHHHHHHHHH		36.3723186163
484UbiquitinationPQTLLELKRQRAAAK
HHHHHHHHHHHHHHH		36.7929967540
494PhosphorylationRAAAKLLSHPFLSTH
HHHHHHHCCHHHHHH		39.2826503514
499PhosphorylationLLSHPFLSTHLGSSM
HHCCHHHHHHHCCCC		17.7326503514
504PhosphorylationFLSTHLGSSMARTGE
HHHHHHCCCCCCCCC		24.2524247654
505PhosphorylationLSTHLGSSMARTGES
HHHHHCCCCCCCCCC		18.0526503514
508UbiquitinationHLGSSMARTGESSSE
HHCCCCCCCCCCCCC		34.3229967540
517UbiquitinationGESSSEGKAPLIGGR
CCCCCCCCCCCCCCC		42.6630230243
536PhosphorylationSSNGTSVYYTVTSGD
CCCCCEEEEEEECCC		8.0021552520
537PhosphorylationSNGTSVYYTVTSGDP
CCCCEEEEEEECCCC		7.80-
550UbiquitinationDPPLLKFKAPIEEME
CCCCEEEECCHHHHH		52.2229967540
563S-palmitoylationMEEKVHGCCRIS---
HHHHHCCCCCCC---		0.58-
564MethylationEEKVHGCCRIS----
HHHHCCCCCCC----		5.25-
564FarnesylationEEKVHGCCRIS----
HHHHCCCCCCC----		5.25-
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
331SPhosphorylationKinasePRKCAP17252
GPS
333SPhosphorylationKinasePKACAP17612
PSP
337SPhosphorylationKinasePKACAP17612
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP16B_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 PP16B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_HUMANTGFBR1physical
15761153
TGFR2_HUMANTGFBR2physical
15761153
KCTD9_HUMANKCTD9physical
25416956
F208B_HUMANFAM208Bphysical
25416956
CEP55_HUMANCEP55physical
25416956
CDA7L_HUMANCDCA7Lphysical
25416956
CEP70_HUMANCEP70physical
25416956
ZN627_HUMANZNF627physical
28514442
ARBK1_HUMANADRBK1physical
28514442
PP1A_HUMANPPP1CAphysical
28514442
PP1G_HUMANPPP1CCphysical
28514442
PP1B_HUMANPPP1CBphysical
28514442
ZN564_HUMANZNF564physical
28514442
PP1R7_HUMANPPP1R7physical
28514442
PXDNL_HUMANPXDNLphysical
28514442
ZNF24_HUMANZNF24physical
28514442
KLH13_HUMANKLHL13physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP16B_HUMAN

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Related Literatures of Post-Translational Modification

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