CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020175
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin-specific chaperone D 
Protein Synonyms/Alias
 Beta-tubulin cofactor D; tfcD; SSD-1; Tubulin-folding cofactor D 
Gene Name
 TBCD 
Gene Synonyms/Alias
 KIAA0988; SSD1; TFCD; PP1096 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
202SYLIVSDKARDAAAVubiquitination[1, 2]
221FITRPDVKQSKMAEFubiquitination[1]
224RPDVKQSKMAEFLDWubiquitination[1]
265AQIFKHGKREDCLPYubiquitination[1]
295SNQTLLRKLGVKLVQubiquitination[1]
299LLRKLGVKLVQRLGLubiquitination[1]
310RLGLTFLKPKVAAWRubiquitination[1, 2, 3, 4]
312GLTFLKPKVAAWRYQubiquitination[1]
340TQGQSEQKPLILTEDubiquitination[2]
370EQLLVGLKDKDTVVRubiquitination[1, 2]
372LLVGLKDKDTVVRWSubiquitination[1]
382VVRWSAAKGIGRMAGubiquitination[1, 3]
453KALTYDEKRGACSVGubiquitination[1, 3]
656EQAVQGLKQIHQQLYubiquitination[1, 2]
686AVCVLIEKLSLSKMPubiquitination[1]
691IEKLSLSKMPFRGDTubiquitination[1]
788ALPGFLLKGRLQQVLubiquitination[1]
820ESRRDGLKAIARICQubiquitination[1, 3]
873DVGTWVRKAAMTSLMubiquitination[1]
913VAQQASEKIDRFRAHubiquitination[1, 3]
947PHRGELEKLFPRSDVubiquitination[1, 2]
1077KLLALCKKEIKNSKDubiquitination[1]
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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Tubulin-folding protein; involved in the first step of the tubulin folding pathway. Modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Acts as a GTPase- activating protein (GAP) for ARL2. Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. 
Sequence Annotation
 REPEAT 361 399 HEAT 1.
 REPEAT 557 594 HEAT 2.
 REPEAT 596 632 HEAT 3.  
Keyword
 Alternative splicing; Cell junction; Cell membrane; Chaperone; Complete proteome; Cytoplasm; GTPase activation; Membrane; Polymorphism; Reference proteome; Repeat; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1192 AA 
Protein Sequence
MALSDEPAAG GPEEEAEDET LAFGAALEAF GESAETRALL GRLREVHGGG AEREVALERF 60
RVIMDKYQEQ PHLLDPHLEW MMNLLLDIVQ DQTSPASLVH LAFKFLYIIT KVRGYKTFLR 120
LFPHEVADVE PVLDLVTIQN PKDHEAWETR YMLLLWLSVT CLIPFDFSRL DGNLLTQPGQ 180
ARMSIMDRIL QIAESYLIVS DKARDAAAVL VSRFITRPDV KQSKMAEFLD WSLCNLARSS 240
FQTMQGVITM DGTLQALAQI FKHGKREDCL PYAATVLRCL DGCRLPESNQ TLLRKLGVKL 300
VQRLGLTFLK PKVAAWRYQR GCRSLAANLQ LLTQGQSEQK PLILTEDDDE DDDVPEGVER 360
VIEQLLVGLK DKDTVVRWSA AKGIGRMAGR LPRALADDVV GSVLDCFSFQ ETDKAWHGGC 420
LALAELGRRG LLLPSRLVDV VAVILKALTY DEKRGACSVG TNVRDAACYV CWAFARAYEP 480
QELKPFVTAI SSALVIAAVF DRDINCRRAA SAAFQENVGR QGTFPHGIDI LTTADYFAVG 540
NRSNCFLVIS VFIAGFPEYT QPMIDHLVTM KISHWDGVIR ELAARALHNL AQQAPEFSAT 600
QVFPRLLSMT LSPDLHMRHG SILACAEVAY ALYKLAAQEN RPVTDHLDEQ AVQGLKQIHQ 660
QLYDRQLYRG LGGQLMRQAV CVLIEKLSLS KMPFRGDTVI DGWQWLINDT LRHLHLISSH 720
SRQQMKDAAV SALAALCSEY YMKEPGEADP AIQEELITQY LAELRNPEEM TRCGFSLALG 780
ALPGFLLKGR LQQVLTGLRA VTHTSPEDVS FAESRRDGLK AIARICQTVG VKAGAPDEAV 840
CGENVSQIYC ALLGCMDDYT TDSRGDVGTW VRKAAMTSLM DLTLLLARSQ PELIEAHTCE 900
RIMCCVAQQA SEKIDRFRAH AASVFLTLLH FDSPPIPHVP HRGELEKLFP RSDVASVNWS 960
APSQAFPRIT QLLGLPTYRY HVLLGLVVSL GGLTESTIRH STQSLFEYMK GIQSDPQALG 1020
SFSGTLLQIF EDNLLNERVS VPLLKTLDHV LTHGCFDIFT TEEDHPFAVK LLALCKKEIK 1080
NSKDIQKLLS GIAVDFPSAT LVCVGTVQMY AHTHLRLGAP GPHCAHGSAM PRFCEMVQFP 1140
GDVRRQALLQ LCLLLCHRFP LIRKTTASQV YETLLTYSDV VGADVLDEVV TVLSDTAWDA 1200
ELAVVREQRN RLCDLLGVPS PTWCPAWCLL KPVLEPIPHP CLVRMSCS 1248 
Gene Ontology
 GO:0005912; C:adherens junction; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
 GO:0005874; C:microtubule; TAS:ProtInc.
 GO:0005923; C:tight junction; ISS:UniProtKB.
 GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
 GO:0051087; F:chaperone binding; TAS:ProtInc.
 GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
 GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
 GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
 GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:UniProtKB.
 GO:0070830; P:tight junction assembly; ISS:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR022577; Tubulin_specific_chaperoneD_C. 
Pfam
 PF12612; TFCD_C 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS