TM245_HUMAN - dbPTM
TM245_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM245_HUMAN
UniProt AC Q9H330
Protein Name Transmembrane protein 245
Gene Name TMEM245
Organism Homo sapiens (Human).
Sequence Length 879
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MADGGGPKDAPSLRSSPGPAPRVPRAVGPSGGGGETPRTAALALRFDKPIKQAFYNTGAVLFVCLCCGAAVLVYFILEAFLRPLLWAVLCGTFLHPFKSSLTRLGRHWLQRLHRAHTPIVLAALLLPLCFVDYGVEALGEQALRRRRLLLLLGAGGPLLYGLYCLGSYLGVQVLLVHAATLICRGLDYFSSLWIWTLVVGYVLTVSFKWNASTERYLRAVSIPVWIILLFHLASLAGSWRIPVFLVIVFLMSVGTLYEKQNGKESSGAELPGQVISMAASTLANLAISITGYESSSEDQPSTQPAEAVDRGESAPTLSTSPSPSSPSPTSPSPTLGRRRPEIGTFLRKKKTSDIYFVSLVWAIVVMQIWLNLWIVQLLPVPIAVWILKKLVIHFGVVDFLEKRYHVWWGIIESFLKERQGALAPWPIVGLGKFLLKVDSKLWHWLNKKMIIWLEKMLDKIISIFIIFLLVIGTLLLALLLTAKVHQESVHMIEVTSNLINETLANHPEWANWLPEAQVVQRALNSAANNVYQYGREWITHKLHKILGDKVNNTAVIEKQVLELWDRLYHSWFVKNVTHSGRHKGQKLHVSRQNSWLGDILDWQDIVSFVHENIETFLSILESLWIVMSRNVSLLFTTVTTLLTILFYSGTALLNFVLSLIIFLTTLFYLLSSSDEYYKPVKWVISLTPLSQPGPSSNIIGQSVEEAIRGVFDASLKMAGFYGLYTWLTHTMFGINIVFIPSALAAILGAVPFLGTYWAAVPAVLDLWLTQGLGCKAILLLIFHLLPTYFVDTAIYSDISGGGHPYLTGLAVAGGAYYLGLEGAIIGPILLCILVVASNIYSAMLVSPTNSVPTPNQTPWPAQPQRTFRDISEDLKSSVG
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
2Acetylation------MADGGGPKD
------CCCCCCCCC		24.93-
12PhosphorylationGGPKDAPSLRSSPGP
CCCCCCCHHCCCCCC		37.8323401153
15PhosphorylationKDAPSLRSSPGPAPR
CCCCHHCCCCCCCCC		46.2923401153
16PhosphorylationDAPSLRSSPGPAPRV
CCCHHCCCCCCCCCC		27.6925159151
30PhosphorylationVPRAVGPSGGGGETP
CCCCCCCCCCCCCCC		44.1130266825
36PhosphorylationPSGGGGETPRTAALA
CCCCCCCCCHHHHHH		22.7330266825
39PhosphorylationGGGETPRTAALALRF
CCCCCCHHHHHHHHC		19.9329396449
101 (in isoform 3)Ubiquitination-4.1121906983
210N-linked_GlycosylationLTVSFKWNASTERYL
HEEEECCCCCCHHHH		25.30UniProtKB CARBOHYD
257PhosphorylationLMSVGTLYEKQNGKE
HHHHHHHHHHHCCCC		22.4025137130
292PhosphorylationLAISITGYESSSEDQ
HHHHHHCCCCCCCCC		12.1820736484
294PhosphorylationISITGYESSSEDQPS
HHHHCCCCCCCCCCC		30.58-
296PhosphorylationITGYESSSEDQPSTQ
HHCCCCCCCCCCCCC		55.24-
313PhosphorylationEAVDRGESAPTLSTS
HHHCCCCCCCCCCCC		42.2330278072
316PhosphorylationDRGESAPTLSTSPSP
CCCCCCCCCCCCCCC		32.8130278072
318PhosphorylationGESAPTLSTSPSPSS
CCCCCCCCCCCCCCC		29.3523927012
319PhosphorylationESAPTLSTSPSPSSP
CCCCCCCCCCCCCCC		48.0130278072
320PhosphorylationSAPTLSTSPSPSSPS
CCCCCCCCCCCCCCC		21.7230266825
322PhosphorylationPTLSTSPSPSSPSPT
CCCCCCCCCCCCCCC		36.8630266825
324PhosphorylationLSTSPSPSSPSPTSP
CCCCCCCCCCCCCCC		60.2530266825
325PhosphorylationSTSPSPSSPSPTSPS
CCCCCCCCCCCCCCC		32.5530266825
327PhosphorylationSPSPSSPSPTSPSPT
CCCCCCCCCCCCCCC		42.6430266825
329PhosphorylationSPSSPSPTSPSPTLG
CCCCCCCCCCCCCCC		58.5730266825
330PhosphorylationPSSPSPTSPSPTLGR
CCCCCCCCCCCCCCC		27.1130266825
332PhosphorylationSPSPTSPSPTLGRRR
CCCCCCCCCCCCCCC		30.2229255136
334PhosphorylationSPTSPSPTLGRRRPE
CCCCCCCCCCCCCCC		46.3029255136
344PhosphorylationRRRPEIGTFLRKKKT
CCCCCHHHHHCCCCC		25.7626074081
354UbiquitinationRKKKTSDIYFVSLVW
CCCCCCHHHHHHHHH		2.6222817900
358UbiquitinationTSDIYFVSLVWAIVV
CCHHHHHHHHHHHHH		13.8022817900
362UbiquitinationYFVSLVWAIVVMQIW
HHHHHHHHHHHHHHH		4.1722817900
369UbiquitinationAIVVMQIWLNLWIVQ
HHHHHHHHHHHHHHH		2.2323503661
373UbiquitinationMQIWLNLWIVQLLPV
HHHHHHHHHHHHCCC		6.4023503661
377UbiquitinationLNLWIVQLLPVPIAV
HHHHHHHHCCCCHHH		3.9623503661
381UbiquitinationIVQLLPVPIAVWILK
HHHHCCCCHHHHHHH		13.5923503661
393UbiquitinationILKKLVIHFGVVDFL
HHHHHHHHHCHHHHH		13.1122817900
397UbiquitinationLVIHFGVVDFLEKRY
HHHHHCHHHHHHHHH		4.3922817900
401UbiquitinationFGVVDFLEKRYHVWW
HCHHHHHHHHHHHHH		35.1722817900
413PhosphorylationVWWGIIESFLKERQG
HHHHHHHHHHHHCCC		26.0224719451
416UbiquitinationGIIESFLKERQGALA
HHHHHHHHHCCCCCC		49.1723503661
420UbiquitinationSFLKERQGALAPWPI
HHHHHCCCCCCCCCC		28.8723503661
423 (in isoform 3)Phosphorylation-11.9928348404
428 (in isoform 3)Phosphorylation-4.5520068231
429 (in isoform 3)Phosphorylation-29.4510564813
431UbiquitinationPWPIVGLGKFLLKVD
CCCCCCHHHHHHHHC		16.8522817900
432UbiquitinationWPIVGLGKFLLKVDS
CCCCCHHHHHHHHCH		37.5722817900
435UbiquitinationVGLGKFLLKVDSKLW
CCHHHHHHHHCHHHH		5.9822817900
436 (in isoform 4)Ubiquitination-46.2521906983
436UbiquitinationGLGKFLLKVDSKLWH
CHHHHHHHHCHHHHH		46.2522817900
436 (in isoform 2)Ubiquitination-46.2521906983
439UbiquitinationKFLLKVDSKLWHWLN
HHHHHHCHHHHHHHC		32.4122817900
440UbiquitinationFLLKVDSKLWHWLNK
HHHHHCHHHHHHHCH		51.6522817900
446UbiquitinationSKLWHWLNKKMIIWL
HHHHHHHCHHHHHHH		36.3923503661
447UbiquitinationKLWHWLNKKMIIWLE
HHHHHHCHHHHHHHH		41.3623503661
450UbiquitinationHWLNKKMIIWLEKML
HHHCHHHHHHHHHHH		2.5423503661
451UbiquitinationWLNKKMIIWLEKMLD
HHCHHHHHHHHHHHH		2.8423503661
454UbiquitinationKKMIIWLEKMLDKII
HHHHHHHHHHHHHHH		22.7923503661
455UbiquitinationKMIIWLEKMLDKIIS
HHHHHHHHHHHHHHH		42.4623503661
455 (in isoform 2)Ubiquitination-42.46-
458UbiquitinationIWLEKMLDKIISIFI
HHHHHHHHHHHHHHH		36.2922817900
459UbiquitinationWLEKMLDKIISIFII
HHHHHHHHHHHHHHH		37.6723503661
459 (in isoform 2)Ubiquitination-37.67-
463UbiquitinationMLDKIISIFIIFLLV
HHHHHHHHHHHHHHH		1.7022817900
466UbiquitinationKIISIFIIFLLVIGT
HHHHHHHHHHHHHHH		1.0722817900
471UbiquitinationFIIFLLVIGTLLLAL
HHHHHHHHHHHHHHH		3.3522817900
472UbiquitinationIIFLLVIGTLLLALL
HHHHHHHHHHHHHHH		11.6623503661
480UbiquitinationTLLLALLLTAKVHQE
HHHHHHHHHHHHHHH		4.5623503661
500N-linked_GlycosylationEVTSNLINETLANHP
CCCHHHHHHHHHHCH		39.09UniProtKB CARBOHYD
501UbiquitinationVTSNLINETLANHPE
CCHHHHHHHHHHCHH		37.9022817900
505UbiquitinationLINETLANHPEWANW
HHHHHHHHCHHHHHC		55.1222817900
506UbiquitinationINETLANHPEWANWL
HHHHHHHCHHHHHCC		18.9522817900
510UbiquitinationLANHPEWANWLPEAQ
HHHCHHHHHCCCHHH		8.8222817900
515UbiquitinationEWANWLPEAQVVQRA
HHHHCCCHHHHHHHH		49.9523503661
519UbiquitinationWLPEAQVVQRALNSA
CCCHHHHHHHHHHHH		1.8023503661
531PhosphorylationNSAANNVYQYGREWI
HHHHHCHHHHHHHHH		9.72-
533PhosphorylationAANNVYQYGREWITH
HHHCHHHHHHHHHHH		10.64-
535UbiquitinationNNVYQYGREWITHKL
HCHHHHHHHHHHHHH		31.0122817900
536UbiquitinationNVYQYGREWITHKLH
CHHHHHHHHHHHHHH		38.5822817900
540UbiquitinationYGREWITHKLHKILG
HHHHHHHHHHHHHHC		22.8822817900
541UbiquitinationGREWITHKLHKILGD
HHHHHHHHHHHHHCC		43.5722817900
541 (in isoform 4)Ubiquitination-43.5721906983
543UbiquitinationEWITHKLHKILGDKV
HHHHHHHHHHHCCCC		21.6622817900
544UbiquitinationWITHKLHKILGDKVN
HHHHHHHHHHCCCCC		50.4922817900
548UbiquitinationKLHKILGDKVNNTAV
HHHHHHCCCCCCCHH		48.5722817900
549UbiquitinationLHKILGDKVNNTAVI
HHHHHCCCCCCCHHH		45.0922817900
549 (in isoform 2)Ubiquitination-45.0921906983
550UbiquitinationHKILGDKVNNTAVIE
HHHHCCCCCCCHHHH		8.7523503661
551N-linked_GlycosylationKILGDKVNNTAVIEK
HHHCCCCCCCHHHHH		45.9719159218
553PhosphorylationLGDKVNNTAVIEKQV
HCCCCCCCHHHHHHH		19.6621406692
553O-linked_GlycosylationLGDKVNNTAVIEKQV
HCCCCCCCHHHHHHH		19.6630059200
557UbiquitinationVNNTAVIEKQVLELW
CCCCHHHHHHHHHHH		30.7323503661
558 (in isoform 2)Ubiquitination-34.28-
558UbiquitinationNNTAVIEKQVLELWD
CCCHHHHHHHHHHHH		34.2823503661
575N-linked_GlycosylationYHSWFVKNVTHSGRH
HHHHHHCCCCCCCCC		38.32UniProtKB CARBOHYD
690PhosphorylationVISLTPLSQPGPSSN
EEEECCCCCCCCCCC		35.22-
695PhosphorylationPLSQPGPSSNIIGQS
CCCCCCCCCCCCCHH		41.76-
871 (in isoform 2)Phosphorylation-31.1128348404
876 (in isoform 2)Phosphorylation-5.0820068231
877 (in isoform 2)Phosphorylation-5.1910564813
877PhosphorylationISEDLKSSVG-----
HHHHHHHHCC-----		5.1920068231
878PhosphorylationSEDLKSSVG------
HHHHHHHCC------		37.1124719451
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 TM245_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM245_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 TM245_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM245_HUMAN !!
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 TM245_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-551, AND MASSSPECTROMETRY.
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 THR-36; SER-332 AND THR-334,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND SER-332, AND MASSSPECTROMETRY.

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