ST14_HUMAN - dbPTM
ST14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST14_HUMAN
UniProt AC Q9Y5Y6
Protein Name Suppressor of tumorigenicity 14 protein
Gene Name ST14
Organism Homo sapiens (Human).
Sequence Length 855
Subcellular Localization Membrane
Single-pass type II membrane protein .
Protein Description Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing..
Protein Sequence MGSDRARKGGGGPKDFGAGLKYNSRHEKVNGLEEGVEFLPVNNVKKVEKHGPGRWVVLAAVLIGLLLVLLGIGFLVWHLQYRDVRVQKVFNGYMRITNENFVDAYENSNSTEFVSLASKVKDALKLLYSGVPFLGPYHKESAVTAFSEGSVIAYYWSEFSIPQHLVEEAERVMAEERVVMLPPRARSLKSFVVTSVVAFPTDSKTVQRTQDNSCSFGLHARGVELMRFTTPGFPDSPYPAHARCQWALRGDADSVLSLTFRSFDLASCDERGSDLVTVYNTLSPMEPHALVQLCGTYPPSYNLTFHSSQNVLLITLITNTERRHPGFEATFFQLPRMSSCGGRLRKAQGTFNSPYYPGHYPPNIDCTWNIEVPNNQHVKVRFKFFYLLEPGVPAGTCPKDYVEINGEKYCGERSQFVVTSNSNKITVRFHSDQSYTDTGFLAEYLSYDSSDPCPGQFTCRTGRCIRKELRCDGWADCTDHSDELNCSCDAGHQFTCKNKFCKPLFWVCDSVNDCGDNSDEQGCSCPAQTFRCSNGKCLSKSQQCNGKDDCGDGSDEASCPKVNVVTCTKHTYRCLNGLCLSKGNPECDGKEDCSDGSDEKDCDCGLRSFTRQARVVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVINQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
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
14UbiquitinationRKGGGGPKDFGAGLK
CCCCCCCCCCCCCCC		69.80-
21MethylationKDFGAGLKYNSRHEK
CCCCCCCCCCCCCCC		41.2842371721
21UbiquitinationKDFGAGLKYNSRHEK
CCCCCCCCCCCCCCC		41.2821906983
22PhosphorylationDFGAGLKYNSRHEKV
CCCCCCCCCCCCCCC		24.3428152594
24PhosphorylationGAGLKYNSRHEKVNG
CCCCCCCCCCCCCCC		31.7428152594
28UbiquitinationKYNSRHEKVNGLEEG
CCCCCCCCCCCCCCC		34.5721906983
45UbiquitinationFLPVNNVKKVEKHGP
EEEECCEEEEHHHCC		53.9021906983
46UbiquitinationLPVNNVKKVEKHGPG
EEECCEEEEHHHCCC		51.8822817900
49UbiquitinationNNVKKVEKHGPGRWV
CCEEEEHHHCCCHHH		57.7722817900
109N-linked_GlycosylationVDAYENSNSTEFVSL
HHHHCCCCCHHHHHH		65.61UniProtKB CARBOHYD
129PhosphorylationDALKLLYSGVPFLGP
HHHHHHHCCCCCCCC		33.03-
189UbiquitinationPPRARSLKSFVVTSV
CCCHHCCCEEEEEEE		42.9923503661
204UbiquitinationVAFPTDSKTVQRTQD
EECCCCCCCCEECCC		56.3721963094
209O-linked_GlycosylationDSKTVQRTQDNSCSF
CCCCCEECCCCCCCC		24.1555832007
236PhosphorylationTTPGFPDSPYPAHAR
ECCCCCCCCCCCHHH		26.94-
302N-linked_GlycosylationGTYPPSYNLTFHSSQ
CCCCCCCEEEEECCC		36.6212738778
302N-linked_GlycosylationGTYPPSYNLTFHSSQ
CCCCCCCEEEEECCC		36.62UniProtKB CARBOHYD
338PhosphorylationFFQLPRMSSCGGRLR
EEECCCCCCCCCHHE		24.61-
339PhosphorylationFQLPRMSSCGGRLRK
EECCCCCCCCCHHEE		13.87-
424UbiquitinationVVTSNSNKITVRFHS
EEECCCCEEEEEECC		39.3121963094
485N-linked_GlycosylationTDHSDELNCSCDAGH
CCCCCCCCEECCCCC		17.38UniProtKB CARBOHYD
497UbiquitinationAGHQFTCKNKFCKPL
CCCCEECCCCCCCEE		61.1821963094
499UbiquitinationHQFTCKNKFCKPLFW
CCEECCCCCCCEEEE		37.3222817900
502UbiquitinationTCKNKFCKPLFWVCD
ECCCCCCCEEEEEEC		48.1422817900
536UbiquitinationTFRCSNGKCLSKSQQ
EEECCCCEECCHHHH		35.9322817900
536AcetylationTFRCSNGKCLSKSQQ
EEECCCCEECCHHHH		35.9330592689
540UbiquitinationSNGKCLSKSQQCNGK
CCCEECCHHHHCCCC		39.0621963094
547AcetylationKSQQCNGKDDCGDGS
HHHHCCCCCCCCCCC		36.0826051181
554PhosphorylationKDDCGDGSDEASCPK
CCCCCCCCCCCCCCC		36.70-
558PhosphorylationGDGSDEASCPKVNVV
CCCCCCCCCCCEEEE		28.98-
561UbiquitinationSDEASCPKVNVVTCT
CCCCCCCCEEEEEEC		51.2521963094
582UbiquitinationLNGLCLSKGNPECDG
HCCEEECCCCCCCCC		50.1621963094
590UbiquitinationGNPECDGKEDCSDGS
CCCCCCCCCCCCCCC		36.8121963094
594PhosphorylationCDGKEDCSDGSDEKD
CCCCCCCCCCCCHHC		58.28-
597PhosphorylationKEDCSDGSDEKDCDC
CCCCCCCCCHHCCCC		47.81-
600UbiquitinationCSDGSDEKDCDCGLR
CCCCCCHHCCCCCCH		69.5121963094
772N-linked_GlycosylationKGEIRVINQTTCENL
CCEEEEEECCCHHHC		30.2312738778
772N-linked_GlycosylationKGEIRVINQTTCENL
CCEEEEEECCCHHHC		30.23UniProtKB CARBOHYD
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 ST14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST14_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 ST14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPIT1_HUMANSPINT1physical
10373425
PDGFC_HUMANPDGFCphysical
22035541
Drug and Disease Associations
Kegg Disease
H00739 Ichthyosis with hypotrichosis
OMIM Disease
602400Ichthyosis, congenital, autosomal recessive 11 (ARCI11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ST14_HUMAN

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Related Literatures of Post-Translational Modification

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