TEN1_HUMAN - dbPTM
TEN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEN1_HUMAN
UniProt AC Q9UKZ4
Protein Name Teneurin-1
Gene Name TENM1
Organism Homo sapiens (Human).
Sequence Length 2725
Subcellular Localization Cell membrane
Single-pass membrane protein.
Ten-1 intracellular domain: Nucleus. Nucleus speckle. Nucleus matrix. Cytoplasm, cytoskeleton.
Teneurin C-terminal-associated peptide: Nucleus. Cytoplasm. Cell membrane. Colocalizes with the dystroglycan
Protein Description Involved in neural development, regulating the establishment of proper connectivity within the nervous system. May function as a cellular signal transducer (By similarity).; Teneurin C-terminal-associated peptide: Plays a role in the regulation of neuroplasticity in the limbic system. Mediates a rapid reorganization of actin- and tubulin-based cytoskeleton elements with an increase in dendritic arborization and spine density formation of neurons in the hippocampus and amygdala. Induces BDNF transcription inhibition in neurons. Activates the mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade. Acts also as a bioactive neuroprotective peptide on limbic neurons of the brain and regulates stress-induced behavior: attenuates alkalosis-associated necrotic cell death and the effects of corticotropin-releasing factor (CRF) on c-fos/FOS induction and on the reinstatement of cocaine seeking (By similarity).; Ten-1 intracellular domain: Induces gene transcription activation..
Protein Sequence MEQTDCKPYQPLPKVKHEMDLAYTSSSDESEDGRKPRQSYNSRETLHEYNQELRMNYNSQSRKRKEVEKSTQEMEFCETSHTLCSGYQTDMHSVSRHGYQLEMGSDVDTETEGAASPDHALRMWIRGMKSEHSSCLSSRANSALSLTDTDHERKSDGENGFKFSPVCCDMEAQAGSTQDVQSSPHNQFTFRPLPPPPPPPHACTCARKPPPAADSLQRRSMTTRSQPSPAAPAPPTSTQDSVHLHNSWVLNSNIPLETRHFLFKHGSGSSAIFSAASQNYPLTSNTVYSPPPRPLPRSTFSRPAFTFNKPYRCCNWKCTALSATAITVTLALLLAYVIAVHLFGLTWQLQPVEGELYANGVSKGNRGTESMDTTYSPIGGKVSDKSEKKVFQKGRAIDTGEVDIGAQVMQTIPPGLFWRFQITIHHPIYLKFNISLAKDSLLGIYGRRNIPPTHTQFDFVKLMDGKQLVKQDSKGSDDTQHSPRNLILTSLQETGFIEYMDQGPWYLAFYNDGKKMEQVFVLTTAIEIMDDCSTNCNGNGECISGHCHCFPGFLGPDCARDSCPVLCGGNGEYEKGHCVCRHGWKGPECDVPEEQCIDPTCFGHGTCIMGVCICVPGYKGEICEEEDCLDPMCSNHGICVKGECHCSTGWGGVNCETPLPVCQEQCSGHGTFLLDAGVCSCDPKWTGSDCSTELCTMECGSHGVCSRGICQCEEGWVGPTCEERSCHSHCTEHGQCKDGKCECSPGWEGDHCTIAHYLDAVRDGCPGLCFGNGRCTLDQNGWHCVCQVGWSGTGCNVVMEMLCGDNLDNDGDGLTDCVDPDCCQQSNCYISPLCQGSPDPLDLIQQSQTLFSQHTSRLFYDRIKFLIGKDSTHVIPPEVSFDSRRACVIRGQVVAIDGTPLVGVNVSFLHHSDYGFTISRQDGSFDLVAIGGISVILIFDRSPFLPEKRTLWLPWNQFIVVEKVTMQRVVSDPPSCDISNFISPNPIVLPSPLTSFGGSCPERGTIVPELQVVQEEIPIPSSFVRLSYLSSRTPGYKTLLRILLTHSTIPVGMIKVHLTVAVEGRLTQKWFPAAINLVYTFAWNKTDIYGQKVWGLAEALVSVGYEYETCPDFILWEQRTVVLQGFEMDASNLGGWSLNKHHILNPQSGIIHKGNGENMFISQQPPVISTIMGNGHQRSVACTNCNGPAHNNKLFAPVALASGPDGSVYVGDFNFVRRIFPSGNSVSILELSTSPAHKYYLAMDPVSESLYLSDTNTRKVYKLKSLVETKDLSKNFEVVAGTGDQCLPFDQSHCGDGGRASEASLNSPRGITVDRHGFIYFVDGTMIRKIDENAVITTVIGSNGLTSTQPLSCDSGMDITQVRLEWPTDLAVNPMDNSLYVLDNNIVLQISENRRVRIIAGRPIHCQVPGIDHFLVSKVAIHSTLESARAISVSHSGLLFIAETDERKVNRIQQVTTNGEIYIIAGAPTDCDCKIDPNCDCFSGDGGYAKDAKMKAPSSLAVSPDGTLYVADLGNVRIRTISRNQAHLNDMNIYEIASPADQELYQFTVNGTHLHTLNLITRDYVYNFTYNSEGDLGAITSSNGNSVHIRRDAGGMPLWLVVPGGQVYWLTISSNGVLKRVSAQGYNLALMTYPGNTGLLATKSNENGWTTVYEYDPEGHLTNATFPTGEVSSFHSDLEKLTKVELDTSNRENVLMSTNLTATSTIYILKQENTQSTYRVNPDGSLRVTFASGMEIGLSSEPHILAGAVNPTLGKCNISLPGEHNANLIEWRQRKEQNKGNVSAFERRLRAHNRNLLSIDFDHITRTGKIYDDHRKFTLRILYDQTGRPILWSPVSRYNEVNITYSPSGLVTFIQRGTWNEKMEYDQSGKIISRTWADGKIWSYTYLEKSVMLLLHSQRRYIFEYDQPDCLLSVTMPSMVRHSLQTMLSVGYYRNIYTPPDSSTSFIQDYSRDGRLLQTLHLGTGRRVLYKYTKQARLSEVLYDTTQVTLTYEESSGVIKTIHLMHDGFICTIRYRQTGPLIGRQIFRFSEEGLVNARFDYSYNNFRVTSMQAVINETPLPIDLYRYVDVSGRTEQFGKFSVINYDLNQVITTTVMKHTKIFSANGQVIEVQYEILKAIAYWMTIQYDNVGRMVICDIRVGVDANITRYFYEYDADGQLQTVSVNDKTQWRYSYDLNGNINLLSHGKSARLTPLRYDLRDRITRLGEIQYKMDEDGFLRQRGNDIFEYNSNGLLQKAYNKASGWTVQYYYDGLGRRVASKSSLGQHLQFFYADLTNPIRVTHLYNHTSSEITSLYYDLQGHLIAMELSSGEEYYVACDNTGTPLAVFSSRGQVIKEILYTPYGDIYHDTYPDFQVIIGFHGGLYDFLTKLVHLGQRDYDVVAGRWTTPNHHIWKQLNLLPKPFNLYSFENNYPVGKIQDVAKYTTDIRSWLELFGFQLHNVLPGFPKPELENLELTYELLRLQTKTQEWDPGKTILGIQCELQKQLRNFISLDQLPMTPRYNDGRCLEGGKQPRFAAVPSVFGKGIKFAIKDGIVTADIIGVANEDSRRLAAILNNAHYLENLHFTIEGRDTHYFIKLGSLEEDLVLIGNTGGRRILENGVNVTVSQMTSVLNGRTRRFADIQLQHGALCFNIRYGTTVEEEKNHVLEIARQRAVAQAWTKEQRRLQEGEEGIRAWTEGEKQQLLSTGRVQGYDGYFVLSVEQYLELSDSANNIHFMRQSEIGRR
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
99PhosphorylationHSVSRHGYQLEMGSD
CCCCCCCEEEEECCC		12.0929978859
105PhosphorylationGYQLEMGSDVDTETE
CEEEEECCCCCCCCC		32.9029978859
109PhosphorylationEMGSDVDTETEGAAS
EECCCCCCCCCCCCC		44.6629978859
111PhosphorylationGSDVDTETEGAASPD
CCCCCCCCCCCCCHH		41.6429978859
116PhosphorylationTETEGAASPDHALRM
CCCCCCCCHHHHHHH		30.26-
142PhosphorylationCLSSRANSALSLTDT
HHHHHCCCCCCCCCC		29.6026471730
145PhosphorylationSRANSALSLTDTDHE
HHCCCCCCCCCCCCC		29.0124719451
289PhosphorylationLTSNTVYSPPPRPLP
CCCCCCCCCCCCCCC		26.9626329039
368PhosphorylationVSKGNRGTESMDTTY
CCCCCCCCCCCCCCC		22.9625072903
370PhosphorylationKGNRGTESMDTTYSP
CCCCCCCCCCCCCCC		23.0725072903
373PhosphorylationRGTESMDTTYSPIGG
CCCCCCCCCCCCCCC		20.9925072903
374PhosphorylationGTESMDTTYSPIGGK
CCCCCCCCCCCCCCC		20.1025072903
375PhosphorylationTESMDTTYSPIGGKV
CCCCCCCCCCCCCCC		17.9725072903
376PhosphorylationESMDTTYSPIGGKVS
CCCCCCCCCCCCCCC		14.1425072903
383PhosphorylationSPIGGKVSDKSEKKV
CCCCCCCCCHHHHHH		42.6925072903
386PhosphorylationGGKVSDKSEKKVFQK
CCCCCCHHHHHHHHC		60.6925072903
433N-linked_GlycosylationHPIYLKFNISLAKDS
CCEEEEEEEEECCCC		22.73UniProtKB CARBOHYD
880PhosphorylationHVIPPEVSFDSRRAC
CCCCCCCCCCCCCEE		22.9825002506
883PhosphorylationPPEVSFDSRRACVIR
CCCCCCCCCCEEEEE		22.9625002506
905N-linked_GlycosylationGTPLVGVNVSFLHHS
CCCCEEEEEEEEECC		20.14UniProtKB CARBOHYD
1033PhosphorylationLSYLSSRTPGYKTLL
HHHHCCCCCCHHHHH		24.0226270265
1036PhosphorylationLSSRTPGYKTLLRIL
HCCCCCCHHHHHHHH		11.2926270265
1038PhosphorylationSRTPGYKTLLRILLT
CCCCCHHHHHHHHHH		23.6526270265
1047PhosphorylationLRILLTHSTIPVGMI
HHHHHHCCCCCCCEE		23.85-
1084N-linked_GlycosylationLVYTFAWNKTDIYGQ
HEEEEECCCCCCCCH		33.64UniProtKB CARBOHYD
1179PhosphorylationMGNGHQRSVACTNCN
CCCCCCCEEEECCCC		13.9022210691
1239PhosphorylationSTSPAHKYYLAMDPV
CCCCCHHEEEECCCC		8.21-
1240PhosphorylationTSPAHKYYLAMDPVS
CCCCHHEEEECCCCC		7.87-
1483PhosphorylationDPNCDCFSGDGGYAK
CCCCCCCCCCCCCCC		42.16-
1488PhosphorylationCFSGDGGYAKDAKMK
CCCCCCCCCCCCCCC		18.92-
1503PhosphorylationAPSSLAVSPDGTLYV
CCCCEEECCCCCEEE		16.2129759185
1550N-linked_GlycosylationELYQFTVNGTHLHTL
HHEEEEECCCEEEEE		46.73UniProtKB CARBOHYD
1567N-linked_GlycosylationITRDYVYNFTYNSEG
EECCEEEEEECCCCC		16.85UniProtKB CARBOHYD
1572PhosphorylationVYNFTYNSEGDLGAI
EEEEECCCCCCEEEE		32.32-
1663N-linked_GlycosylationDPEGHLTNATFPTGE
CCCCCEECCEECCCC		43.26UniProtKB CARBOHYD
1682PhosphorylationHSDLEKLTKVELDTS
CHHHHHCEEEEECCC		44.08-
1697PhosphorylationNRENVLMSTNLTATS
CCCCEEEEEECEEEE		15.24-
1698PhosphorylationRENVLMSTNLTATST
CCCEEEEEECEEEEE		21.93-
1699N-linked_GlycosylationENVLMSTNLTATSTI
CCEEEEEECEEEEEE		28.25UniProtKB CARBOHYD
1757N-linked_GlycosylationNPTLGKCNISLPGEH
CCCCCCCCEECCCCC		30.30UniProtKB CARBOHYD
1781N-linked_GlycosylationRKEQNKGNVSAFERR
HHHHCCCCHHHHHHH		26.61UniProtKB CARBOHYD
1798PhosphorylationAHNRNLLSIDFDHIT
HHCCCCEEEEHHHCC		24.23-
1818PhosphorylationYDDHRKFTLRILYDQ
ECCCCCEEEEEEECC		20.4024719451
1842N-linked_GlycosylationVSRYNEVNITYSPSG
CCCCCEECEEECCCC		18.08UniProtKB CARBOHYD
1868PhosphorylationEKMEYDQSGKIISRT
CCCCCCCCCCEEEEE		38.8724114839
1875PhosphorylationSGKIISRTWADGKIW
CCCEEEEEECCCCEE		20.4324719451
1882PhosphorylationTWADGKIWSYTYLEK
EECCCCEEEEEEHHH		6.7024719451
1886PhosphorylationGKIWSYTYLEKSVML
CCEEEEEEHHHHHHH		12.48-
1901PhosphorylationLLHSQRRYIFEYDQP
HHHCCCEEEEECCCC		16.4922210691
1905PhosphorylationQRRYIFEYDQPDCLL
CCEEEEECCCCCEEE		14.7722210691
1959PhosphorylationRDGRLLQTLHLGTGR
CCCCEEEEEECCCCC		19.0026074081
1964PhosphorylationLQTLHLGTGRRVLYK
EEEEECCCCCHHHHH		33.6026074081
1979PhosphorylationYTKQARLSEVLYDTT
HHCHHCHHEEEEECC		21.8023663014
1983PhosphorylationARLSEVLYDTTQVTL
HCHHEEEEECCEEEE		19.2023663014
1985PhosphorylationLSEVLYDTTQVTLTY
HHEEEEECCEEEEEE		12.9323663014
1986PhosphorylationSEVLYDTTQVTLTYE
HEEEEECCEEEEEEE		20.3923663014
1989PhosphorylationLYDTTQVTLTYEESS
EEECCEEEEEEECCC		11.9923663014
1991PhosphorylationDTTQVTLTYEESSGV
ECCEEEEEEECCCCC		21.3723663014
1992PhosphorylationTTQVTLTYEESSGVI
CCEEEEEEECCCCCE		22.3223663014
1995PhosphorylationVTLTYEESSGVIKTI
EEEEEECCCCCEEEE		22.0623663014
1996PhosphorylationTLTYEESSGVIKTIH
EEEEECCCCCEEEEE		40.1223663014
2018PhosphorylationCTIRYRQTGPLIGRQ
EEEEECCCCCCCCEE		31.5921712546
2092PhosphorylationYDLNQVITTTVMKHT
CCCCCCCCHHHHHCC		19.9829759185
2093PhosphorylationDLNQVITTTVMKHTK
CCCCCCCHHHHHCCE		13.2829759185
2094PhosphorylationLNQVITTTVMKHTKI
CCCCCCHHHHHCCEE		15.2329759185
2145N-linked_GlycosylationIRVGVDANITRYFYE
EEECCCCCEEEEEEE		31.53UniProtKB CARBOHYD
2184PhosphorylationNGNINLLSHGKSARL
CCCEEEECCCCCCCC		33.1020068231
2187AcetylationINLLSHGKSARLTPL
EEEECCCCCCCCCCC		35.207491777
2285N-linked_GlycosylationIRVTHLYNHTSSEIT
EEEEEEECCCCCCCH		38.02UniProtKB CARBOHYD
2378PhosphorylationVHLGQRDYDVVAGRW
HHHCCCCCCEECCCC		16.90-
2580PhosphorylationHYFIKLGSLEEDLVL
EEEEECCCCCCCEEE		42.9423092983
2602N-linked_GlycosylationRILENGVNVTVSQMT
HHHCCCEEEEHHHCH		25.74UniProtKB 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 TEN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEN1_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 TEN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRBS1_HUMANSORBS1physical
15777793
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2580, AND MASSSPECTROMETRY.

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