CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008754
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TTC3 
Protein Synonyms/Alias
 Protein DCRR1; RING finger protein 105; TPR repeat protein D; Tetratricopeptide repeat protein 3; TPR repeat protein 3 
Gene Name
 TTC3 
Gene Synonyms/Alias
 DCRR1; RNF105; TPRD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
53DGVGVQYKDYIQSERubiquitination[1]
123RASEINLKKLQHLELubiquitination[1]
124ASEINLKKLQHLELMubiquitination[1]
140DIVDLAKKVANDSFLubiquitination[1]
237EGELMKMKGNEEFSKubiquitination[1]
244KGNEEFSKERFDIAIubiquitination[1]
337KNDPEGIKDLIQQHVubiquitination[1]
345DLIQQHVKLQKQIEDubiquitination[1]
348QQHVKLQKQIEDLQGubiquitination[1]
360LQGRTANKDPIKAFYubiquitination[1]
397EKERDFRKINHEMANubiquitination[1]
465LTLPADLKNILEKQFubiquitination[1]
470DLKNILEKQFSKSSRubiquitination[1, 2]
488QDFANIMKMLRSLIQubiquitination[1]
601EALNHFEKARTLIYRubiquitination[1]
629IEESQPQKIKMLLEKubiquitination[1]
799LRESNPPKNEEQKETubiquitination[1]
804PPKNEEQKETVDNVQubiquitination[1]
967FSEPASLKEARCLIWubiquitination[1]
1097EYVVRNKKLWDMNPKubiquitination[1]
1153LEKAGGLKPFLLGCPubiquitination[1]
1190KKKNIKTKVEEISKAubiquitination[1]
1196TKVEEISKAGEYVRVubiquitination[1]
1204AGEYVRVKLQLNPAAubiquitination[1]
1530ETRDLEEKLKRHLEEubiquitination[1]
1596QKNDGKEKEHELHLDacetylation[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of 'Lys-48'- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT. 
Sequence Annotation
 REPEAT 231 264 TPR 1.
 REPEAT 266 298 TPR 2.
 REPEAT 536 572 TPR 3.
 REPEAT 576 609 TPR 4.
 ZN_FING 1957 1997 RING-type.
 MOD_RES 378 378 Phosphoserine; by PKB/AKT2.  
Keyword
 Alternative splicing; Complete proteome; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2025 AA 
Protein Sequence
MDNFAEGDFT VADYALLEDC PHVDDCVFAA EFMSNDYVRV TQLYCDGVGV QYKDYIQSER 60
NLEFDICSIW CSKPISVLQD YCDAIKINIF WPLLFQHQNS SVISRLHPCV DANNSRASEI 120
NLKKLQHLEL MEDIVDLAKK VANDSFLIGG LLRIGCKIEN KILAMEEALN WIKYAGDVTI 180
LTKLGSIDNC WPMLSIFFTE YKYHITKIVM EDCNLLEELK TQSCMDCIEE GELMKMKGNE 240
EFSKERFDIA IIYYTRAIEY RPENYLLYGN RALCFLRTGQ FRNALGDGKR ATILKNTWPK 300
GHYRYCDALS MLGEYDWALQ ANIKAQKLCK NDPEGIKDLI QQHVKLQKQI EDLQGRTANK 360
DPIKAFYENR AYTPRSLSAP IFTTSLNFVE KERDFRKINH EMANGGNQNL KVADEALKVD 420
DCDCHPEFSP PSSQPPKHKG KQKSRNNESE KFSSSSPLTL PADLKNILEK QFSKSSRAAH 480
QDFANIMKML RSLIQDGYMA LLEQRCRSAA QAFTELLNGL DPQKIKQLNL AMINYVLVVY 540
GLAISLLGIG QPEELSEAEN QFKRIIEHYP SEGLDCLAYC GIGKVYLKKN RFLEALNHFE 600
KARTLIYRLP GVLTWPTSNV IIEESQPQKI KMLLEKFVEE CKFPPVPDAI CCYQKCHGYS 660
KIQIYITDPD FKGFIRISCC QYCKIEFHMN CWKKLKTTTF NDKIDKDFLQ GICLTPDCEG 720
VISKIIIFSS GGEVKCEFEH KVIKEKVPPR PILKQKCSSL EKLRLKEDKK LKRKIQKKEA 780
KKLAQERMEE DLRESNPPKN EEQKETVDNV QRCQFLDDRI LQCIKQYADK IKSGIQNTAM 840
LLKELLSWKV LSTEDYTTCF SSRNFLNEAV DYVIRHLIQE NNRVKTRIFL HVLSELKEVE 900
PKLAAWIQKL NSFGLDATGT FFSRYGASLK LLDFSIMTFL WNEKYGHKLD SIEGKQLDYF 960
SEPASLKEAR CLIWLLEEHR DKFPALHSAL DEFFDIMDSR CTVLRKQDSG EAPFSSTKVK 1020
NKSKKKKPKD SKPMLVGSGT TSVTSNNEII TSSEDHSNRN SDSAGPFAVP DHLRQDVEEF 1080
EALYDQHSNE YVVRNKKLWD MNPKQKCSTL YDYFSQFLEE HGPLDMSNKM FSAEYEFFPE 1140
ETRQILEKAG GLKPFLLGCP RFVVIDNCIA LKKVASRLKK KRKKKNIKTK VEEISKAGEY 1200
VRVKLQLNPA AREFKPDVKS KPVSDSSSAP AFENVKPKPV SANSPKPACE DVKAKPVSDN 1260
SSRQVSEDGQ PKGVSSNSPK PGSEDANYKR VSCNSPKPVL EDVKPTYWAQ SHLVTGYCTY 1320
LPFQRFDITQ TPPAYINVLP GLPQYTSIYT PLASLSPEYQ LPRSVPVVPS FVANDRADKN 1380
AAAYFEGHHL NAENVAGHQI ASETQILEGS LGISVKSHCS TGDAHTVLSE SNRNDEHCGN 1440
SNNKCEVIPE STSAVTNIPH VQMVAIQVSW NIIHQEVNTE PYNPFEERQG EISRIEKEHQ 1500
VLQDQLQEVY ENYEQIKLKG LEETRDLEEK LKRHLEENKI SKTELDWFLQ DLEREIKKWQ 1560
QEKKEIQERL KSLKKKIKKV SNASEMYTQK NDGKEKEHEL HLDQSLEISN TLTNEKMKIE 1620
EYIKKGKEDY EESHQRAVAA EVSVLENWKE SEVYKLQIME SQAEAFLKKL GLISRDPAAY 1680
PDMESDIRSW ELFLSNVTKE IEKAKSQFEE QIKAIKNGSR LSELSKVQIS ELSFPACNTV 1740
HPELLPESSG DDGQGLVTSA SDVTGNHAAL HRDPSVFSAG DSPGEAPSAL LPGPPPGQPE 1800
ATQLTGPKRA GQAALSERSP VADRKQPVPP GRAARSSQSP KKPFNSIIEH LSVVFPCYNS 1860
TELAGFIKKV RSKNKNSLSG LSIDEIVQRV TEHILDEQKK KKPNPGKDKR TYEPSSATPV 1920
TRSSQGSPSV VVAPSPKTKG QKAEDVPVRI ALGASSCEIC HEVFKSKNVR VLKCGHKYHK 1980
GCFKQWLKGQ SACPACQGRD LLTEESPSGR GWPSQNQELP SCSSR 2025 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005773; C:vacuole; IEA:Compara.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0010771; P:negative regulation of cell morphogenesis involved in differentiation; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. 
Interpro
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00515; TPR_1
 PF13639; zf-RING_2 
SMART
 SM00184; RING
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS