C1TM_HUMAN - dbPTM
C1TM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C1TM_HUMAN
UniProt AC Q6UB35
Protein Name Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Gene Name MTHFD1L
Organism Homo sapiens (Human).
Sequence Length 978
Subcellular Localization Mitochondrion .
Protein Description May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2..
Protein Sequence MGTRLPLVLRQLRRPPQPPGPPRRLRVPCRASSGGGGGGGGGREGLLGQRRPQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFKPVLAIIQAGDDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIEEDDVILLAAALRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRLVPLVNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVDLARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF
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
33PhosphorylationRVPCRASSGGGGGGG
ECEEECCCCCCCCCC		40.2430624053
59PhosphorylationPQDGQARSSCSPGGR
CCCCCCCCCCCCCCC		38.4228450419
60PhosphorylationQDGQARSSCSPGGRT
CCCCCCCCCCCCCCC		17.0428450419
62PhosphorylationGQARSSCSPGGRTPA
CCCCCCCCCCCCCHH		28.6426074081
67PhosphorylationSCSPGGRTPAARDSI
CCCCCCCCHHHHHHH		22.1326074081
73PhosphorylationRTPAARDSIVREVIQ
CCHHHHHHHHHHHHH		19.8926074081
82PhosphorylationVREVIQNSKEVLSLL
HHHHHHCCHHHHHHH		17.5125247763
87PhosphorylationQNSKEVLSLLQEKNP
HCCHHHHHHHHHHCC		32.0125247763
92MalonylationVLSLLQEKNPAFKPV
HHHHHHHHCCCCCCE		56.1026320211
168AcetylationSENLFSNKVLNALKP
CCCHHCCHHHHHCCC		47.0730590503
174AcetylationNKVLNALKPEKDVDG
CHHHHHCCCCCCCCC		49.0419608861
189MalonylationVTDINLGKLVRGDAH
CEECCCCHHCCCCHH		47.1526320211
189SuccinylationVTDINLGKLVRGDAH
CEECCCCHHCCCCHH		47.15-
189SuccinylationVTDINLGKLVRGDAH
CEECCCCHHCCCCHH		47.15-
189AcetylationVTDINLGKLVRGDAH
CEECCCCHHCCCCHH		47.1519608861
189UbiquitinationVTDINLGKLVRGDAH
CEECCCCHHCCCCHH		47.1519608861
198GlutathionylationVRGDAHECFVSPVAK
CCCCHHHHCCHHHHH		2.6822555962
198S-palmitoylationVRGDAHECFVSPVAK
CCCCHHHHCCHHHHH		2.6821044946
271PhosphorylationADIVVLGSPKPEEIP
CCEEEECCCCCCCCC		26.11-
352AcetylationRWRLHCLKLQPLSPV
HHHHEEEECEECCCC		50.9323749302
357PhosphorylationCLKLQPLSPVPSDIE
EEECEECCCCCCCCE		30.4529255136
358PhosphorylationLKLQPLSPVPSDIEI
EECEECCCCCCCCEE		50.1227251275
361PhosphorylationQPLSPVPSDIEISRG
EECCCCCCCCEECCC		51.9929255136
366PhosphorylationVPSDIEISRGQTPKA
CCCCCEECCCCCHHH		19.9823403867
391PhosphorylationLADEIEIYGKSKAKV
HHHEEEEECCCCCHH		13.0028064214
392PhosphorylationADEIEIYGKSKAKVR
HHEEEEECCCCCHHH		33.1625147952
393UbiquitinationDEIEIYGKSKAKVRL
HEEEEECCCCCHHHH		31.63-
401PhosphorylationSKAKVRLSVLERLKD
CCCHHHHHHHHHHHH		17.6823898821
414PhosphorylationKDQADGKYVLVAGIT
HHHCCCCEEEEEEEE		12.4428152594
421PhosphorylationYVLVAGITPTPLGEG
EEEEEEEECCCCCCC		21.8621406692
423PhosphorylationLVAGITPTPLGEGKS
EEEEEECCCCCCCCC		23.6121406692
448PhosphorylationTAHLNVNSFACLRQP
HHHCCCCCEECCCCC		15.2222210691
516AcetylationHENTQTDKALYNRLV
CCCCCCCHHHHHHHH		43.6123954790
516MalonylationHENTQTDKALYNRLV
CCCCCCCHHHHHHHH		43.6126320211
516UbiquitinationHENTQTDKALYNRLV
CCCCCCCHHHHHHHH		43.61-
516SuccinylationHENTQTDKALYNRLV
CCCCCCCHHHHHHHH		43.6127452117
554PhosphorylationKTDPSTLTEEEVSKF
CCCHHCCCHHHHHHH		41.25-
560UbiquitinationLTEEEVSKFARLDID
CCHHHHHHHHCCCCC		48.49-
579PhosphorylationTWQRVLDTNDRFLRK
CEEEEECCCCCCCCE		34.55-
582MethylationRVLDTNDRFLRKITI
EEECCCCCCCCEEEE		34.27-
586UbiquitinationTNDRFLRKITIGQGN
CCCCCCCEEEECCCC		46.47-
588O-linked_GlycosylationDRFLRKITIGQGNTE
CCCCCEEEECCCCCC		23.3030379171
594PhosphorylationITIGQGNTEKGHYRQ
EEECCCCCCCCCCCH		45.9919664995
596MalonylationIGQGNTEKGHYRQAQ
ECCCCCCCCCCCHHH		49.2826320211
596SuccinylationIGQGNTEKGHYRQAQ
ECCCCCCCCCCCHHH		49.28-
596AcetylationIGQGNTEKGHYRQAQ
ECCCCCCCCCCCHHH		49.2823749302
596SuccinylationIGQGNTEKGHYRQAQ
ECCCCCCCCCCCHHH		49.28-
636O-linked_GlycosylationLGRMVVASDKSGQPV
HCCEEEEECCCCCCC		33.6830379171
639PhosphorylationMVVASDKSGQPVTAD
EEEEECCCCCCCCHH		47.8821406692
644PhosphorylationDKSGQPVTADDLGVT
CCCCCCCCHHHHCCC		30.9321406692
651PhosphorylationTADDLGVTGALTVLM
CHHHHCCCHHHHHHC		18.2321406692
655PhosphorylationLGVTGALTVLMKDAI
HCCCHHHHHHCHHCC		15.8521406692
727UbiquitinationMEKFFNIKCRASGLV
CHHCCCCCCCCCCCC		20.83-
763AcetylationVTAGVPLKKEYTEEN
CCCCCCCCCCCCHHH		37.1725953088
814GlutathionylationRAEIDLVCELAKRAG
HHHHHHHHHHHHHCC		4.6322555962
818AcetylationDLVCELAKRAGAFDA
HHHHHHHHHCCCCCE		56.2426051181
819MethylationLVCELAKRAGAFDAV
HHHHHHHHCCCCCEE		32.42115484039
850PhosphorylationRAVREAASKRSRFQF
HHHHHHHHCCCCCCH		35.3324260401
859PhosphorylationRSRFQFLYDVQVPIV
CCCCCHHEECCCCHH		18.50-
885PhosphorylationGAKDIELSPEAQAKI
CCCCCCCCHHHHHHH		14.1220068231
891UbiquitinationLSPEAQAKIDRYTQQ
CCHHHHHHHHHHHHC		32.81-
932PhosphorylationRDFILPISDVRASIG
CCEEEEHHHHHHHCC		28.2820068231
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
357SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C1TM_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 C1TM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAPOA_HUMANPAPOLAphysical
26344197
PAPOB_HUMANPAPOLBphysical
26344197
XPP1_HUMANXPNPEP1physical
26344197
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 C1TM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174 AND LYS-189, AND MASSSPECTROMETRY.

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