TEX14_HUMAN - dbPTM
TEX14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEX14_HUMAN
UniProt AC Q8IWB6
Protein Name Inactive serine/threonine-protein kinase TEX14
Gene Name TEX14
Organism Homo sapiens (Human).
Sequence Length 1497
Subcellular Localization Cytoplasm. Midbody. Chromosome, centromere, kinetochore. Detected in the intercellular bridges that connect male germ cell daughter cells after cell division..
Protein Description Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity)..
Protein Sequence MSRAVRLPVPCPVQLGTLRNDSLEAQLHEYVKQGNYVKVKKILKKGIYVDAVNSLGQTALFVAALLGLRKFVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKLLDAGGDLRLHDERGQNPKTWALTAGKERSTQIVEFMQRCASHMQAIIQGFSYDLLKKIDSPQRLVYSPSWCGGLVQGNPNGSPNRLLKAGVISAQNIYSFGFGKAMPWFQFYLTGATQMAYLGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNGSRVTVKELNLPTHPHCSRLRLADLLIAEQEHSSKLRHPYLLQLMAVCLSQDLEKTRLVYERITIGTLFSVLHERRSQFPVLHMEVIVHLLLQISDALRYLHFQGFIHRSLSSYAVHIISPGEARLTNLEYMLESEDRGVQRDLTRVPLPTQLYNWAAPEVILQKAATVKSDIYSFSMIMQEILTDDIPWKGLDGSVVKKAVVSGNYLEADVRLPKPYYDIVKSGIHVKQKDRTMNLQDIRYILKNDLKDFTGAQRTQPTESPRVQRYGLHPDVNVYLGLTSEHPRETPDMEIIELKEMGSQPHSPRVHSLFTEGTLDPQAPDPCLMARETQNQDAPCPAPFMAEEASSPSTGQPSLCSFEINEIYSGCLILEDDIEEPPGAASSLEADGPNQVDELKSMEEELDKMEREACCFGSEDESSSKAETEYSFDDWDWQNGSLSSLSLPESTREAKSNLNNMSTTEEYLISKCVLDLKIMQTIMHENDDRLRNIEQILDEVEMKQKEQEERMSLWATSREFTNAYKLPLAVGPPSLNYIPPVLQLSGGQKPDTSGNYPTLPRFPRMLPTLCDPGKQNTDEQFQCTQGAKDSLETSRIQNTSSQGRPRESTAQAKATQFNSALFTLSSHRQGPSASPSCHWDSTRMSVEPVSSEIYNAESRNKDDGKVHLKWKMEVKEMAKKAATGQLTVPPWHPQSSLTLESEAENEPDALLQPPIRSPENTDWQRVIEYHRENDEPRGNGKFDKTGNNDCDSDQHGRQPRLGSFTSIRHPSPRQKEQPEHSEAFQASSDTLVAVEKSYSHQSMQSTCSPESSEDITDEFLTPDGEYFYSSTAQENLALETSSPIEEDFEGIQGAFAQPQVSGEEKFQMRKILGKNAEILPRSQFQPVRSTEDEQEETSKESPKELKEKDISLTDIQDLSSISYEPDSSFKEASCKTPKINHAPTSVSTPLSPGSVSSAASQYKDCLESITFQVKTEFASCWNSQEFIQTLSDDFISVRERAKKLDSLLTSSETPPSRLTGLKRLSSFIGAGSPSLVKACDSSPPHATQRRSLPKVEAFSQHHIDELPPPSQELLDDIELLKQQQGSSTVLHENTASDGGGTANDQRHLEEQETDSKKEDSSMLLSKETEDLGEDTERAHSTLDEDLERWLQPPEESVELQDLPKGSERETNIKDQKVGEEKRKREDSITPERRKSEGVLGTSEEDELKSCFWKRLGWSESSRIIVLDQSDLSD
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
36PhosphorylationEYVKQGNYVKVKKIL
HHHHCCCEEEHHHHH
14.42-
168PhosphorylationDLLKKIDSPQRLVYS
HHHHCCCCCCEEEEC
26.8028555341
174PhosphorylationDSPQRLVYSPSWCGG
CCCCEEEECCCCCCC
21.3227307780
175PhosphorylationSPQRLVYSPSWCGGL
CCCEEEECCCCCCCH
12.6527307780
177PhosphorylationQRLVYSPSWCGGLVQ
CEEEECCCCCCCHHC
29.1127307780
206PhosphorylationVISAQNIYSFGFGKA
EEEEEEEEECCCCCC
12.90-
284PhosphorylationLPTHPHCSRLRLADL
CCCCCCHHHHHHHHH
31.17-
437PhosphorylationQKAATVKSDIYSFSM
HHCCCCCHHHHHHHH
25.5522405274
508PhosphorylationMNLQDIRYILKNDLK
CCHHHHHHHHHHCHH
15.7822817900
511AcetylationQDIRYILKNDLKDFT
HHHHHHHHHCHHCCC
38.57133703
515AcetylationYILKNDLKDFTGAQR
HHHHHCHHCCCCCCC
54.37133699
554PhosphorylationTSEHPRETPDMEIIE
CCCCCCCCCCCEEEE
26.3525690035
567PhosphorylationIELKEMGSQPHSPRV
EEHHHCCCCCCCCCC
38.95-
571PhosphorylationEMGSQPHSPRVHSLF
HCCCCCCCCCCHHCC
22.5323403867
618PhosphorylationEEASSPSTGQPSLCS
CCCCCCCCCCCCCCC
43.1322405274
665PhosphorylationNQVDELKSMEEELDK
CHHHHHHHHHHHHHH
44.01-
687PhosphorylationFGSEDESSSKAETEY
CCCCCCCCCCCCCEE
33.5322468782
688PhosphorylationGSEDESSSKAETEYS
CCCCCCCCCCCCEEE
45.2022468782
707PhosphorylationDWQNGSLSSLSLPES
CCCCCCCCCCCCCHH
30.8122468782
727PhosphorylationSNLNNMSTTEEYLIS
HHHCCCCCHHHHHHH
27.7122405274
728PhosphorylationNLNNMSTTEEYLISK
HHCCCCCHHHHHHHH
21.3622405274
776PhosphorylationKEQEERMSLWATSRE
HHHHHHHHHHHHCHH
27.2929083192
780PhosphorylationERMSLWATSREFTNA
HHHHHHHHCHHHHHH
19.4129083192
781PhosphorylationRMSLWATSREFTNAY
HHHHHHHCHHHHHHC
23.2829083192
785PhosphorylationWATSREFTNAYKLPL
HHHCHHHHHHCCCCC
17.7429083192
788PhosphorylationSREFTNAYKLPLAVG
CHHHHHHCCCCCCCC
18.3529083192
863PhosphorylationETSRIQNTSSQGRPR
HHHCCCCCCCCCCCC
17.2429978859
864PhosphorylationTSRIQNTSSQGRPRE
HHCCCCCCCCCCCCC
28.3729978859
865PhosphorylationSRIQNTSSQGRPRES
HCCCCCCCCCCCCCC
34.3229978859
873PhosphorylationQGRPRESTAQAKATQ
CCCCCCCHHHHHHHH
20.3122210691
877AcetylationRESTAQAKATQFNSA
CCCHHHHHHHHHHHH
39.637925333
915PhosphorylationMSVEPVSSEIYNAES
CCEECCCHHHCCCCC
28.40-
923UbiquitinationEIYNAESRNKDDGKV
HHCCCCCCCCCCCCE
45.8030230243
925AcetylationYNAESRNKDDGKVHL
CCCCCCCCCCCCEEE
56.9619815641
929UbiquitinationSRNKDDGKVHLKWKM
CCCCCCCCEEEEEEH
33.2130230243
935SumoylationGKVHLKWKMEVKEMA
CCEEEEEEHHHHHHH
24.48-
935AcetylationGKVHLKWKMEVKEMA
CCEEEEEEHHHHHHH
24.487429667
935SumoylationGKVHLKWKMEVKEMA
CCEEEEEEHHHHHHH
24.48-
1027PhosphorylationGRQPRLGSFTSIRHP
CCCCCCCCCCCCCCC
29.9129449344
1029PhosphorylationQPRLGSFTSIRHPSP
CCCCCCCCCCCCCCC
25.5829449344
1030PhosphorylationPRLGSFTSIRHPSPR
CCCCCCCCCCCCCCC
18.6729496963
1035PhosphorylationFTSIRHPSPRQKEQP
CCCCCCCCCCCCCCC
26.9617081983
1106PhosphorylationNLALETSSPIEEDFE
CEEECCCCCCHHHCC
37.00-
1187PhosphorylationQDLSSISYEPDSSFK
HHHHHCCCCCCCCCC
29.79-
1215PhosphorylationTSVSTPLSPGSVSSA
CCCCCCCCCCCHHHH
28.55-
1226PhosphorylationVSSAASQYKDCLESI
HHHHHHHHHHHHHHC
13.29-
1277PhosphorylationSLLTSSETPPSRLTG
HHHHCCCCCHHHHHH
42.3122817900
1280PhosphorylationTSSETPPSRLTGLKR
HCCCCCHHHHHHHHH
40.9222817900
1289PhosphorylationLTGLKRLSSFIGAGS
HHHHHHHHHHHCCCC
27.5128857561
1290PhosphorylationTGLKRLSSFIGAGSP
HHHHHHHHHHCCCCH
26.0228857561
1305PhosphorylationSLVKACDSSPPHATQ
HHHHHCCCCCCCHHC
44.63-
1384PhosphorylationTDSKKEDSSMLLSKE
CCCHHHHHHHHHCHH
20.81-
1385PhosphorylationDSKKEDSSMLLSKET
CCHHHHHHHHHCHHH
26.27-
1389PhosphorylationEDSSMLLSKETEDLG
HHHHHHHCHHHHCCC
25.2029457462
1404PhosphorylationEDTERAHSTLDEDLE
CCCHHHHHCCCHHHH
29.67-
1459PhosphorylationITPERRKSEGVLGTS
CCHHHHHCCCCCCCC
37.46-
1496PhosphorylationVLDQSDLSD------
EEEHHHCCC------
46.38-

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
437SPhosphorylationKinasePLK1P53350
Uniprot
618TPhosphorylationKinaseCDK1P06493
PSP
727TPhosphorylationKinaseCDK1P06493
PSP
728TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
437SPhosphorylation

22405274

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 TEX14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP55_HUMANCEP55physical
20176808
TEX14_HUMANTEX14physical
20176808

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 TEX14_HUMAN

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Related Literatures of Post-Translational Modification

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