CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Clathrin heavy chain 
Protein Synonyms/Alias
  
Gene Name
 CHC1 
Gene Synonyms/Alias
 YGL206C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
43FVTVRETKDGTNSVAubiquitination[1]
56VAIVDLAKGNEVTRKubiquitination[1]
140FDGNVNAKPQLLTLRubiquitination[1]
372GADDLFQKQFESLLLubiquitination[1]
454DRKQLFEKWLKEDKLacetylation[2]
640LENYTDIKDIKRCVVacetylation[2]
898DSNNSPEKFLKENDQacetylation[2]
947TNENSMYKYQARYLLacetylation[2]
947TNENSMYKYQARYLLubiquitination[1]
1107RAASYADKINTPELWubiquitination[1, 3]
1447RTVKIFSKSDNLPLIacetylation[2]
1495DAVDSYDKFDQLGLAacetylation[2]
1509ASRLESHKLIFFKKIacetylation[2]
1515HKLIFFKKIGALLYRubiquitination[1]
1535AKSLSILKEEKLWKDacetylation[2]
1535AKSLSILKEEKLWKDubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. 
Sequence Annotation
 REPEAT 543 689 CHCR 1.
 REPEAT 692 834 CHCR 2.
 REPEAT 839 978 CHCR 3.
 REPEAT 985 1130 CHCR 4.
 REPEAT 1134 1275 CHCR 5.
 REPEAT 1280 1426 CHCR 6.
 REPEAT 1429 1572 CHCR 7.
 REGION 1 483 Globular terminal domain.
 REGION 23 66 WD40-like repeat 1.
 REGION 67 107 WD40-like repeat 2.
 REGION 108 152 WD40-like repeat 3.
 REGION 153 198 WD40-like repeat 4.
 REGION 199 263 WD40-like repeat 5.
 REGION 264 307 WD40-like repeat 6.
 REGION 308 336 WD40-like repeat 7.
 REGION 453 469 Binding site for the uncoating ATPase,
 REGION 484 527 Flexible linker.
 REGION 528 1653 Heavy chain arm.
 REGION 528 ? Distal segment.
 REGION 1219 1528 Involved in binding clathrin light chain
 REGION ? 1653 Proximal segment.  
Keyword
 Coated pit; Complete proteome; Cytoplasmic vesicle; Membrane; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1653 AA 
Protein Sequence
MSDLPIEFTE LVDLMSLGIS PQFLDFRSTT FESDHFVTVR ETKDGTNSVA IVDLAKGNEV 60
TRKNMGGDSA IMHPSQMVIS VRANGTIVQI FNLETKSKLK SFTLDEPVIF WRWLSETTLG 120
FVTARSILTS NVFDGNVNAK PQLLTLRHAN LNNTQIINFV ANKNLDWFAV VGILQENGRI 180
AGRIQLFSKQ RNISQAIDGH VAIFTNILLE GNGSTPVQVF VTGNRNATTG AGELRIIEID 240
HDASLPSQYQ KETTDIFFPP DATNDFPIAV QVSEKYGIIY LLTKYGFIHL YELETGTNLF 300
VNRITAESVF TAAPYNHENG IACINKKGQV LAVEISTSQI VPYILNKLSN VALALIVATR 360
GGLPGADDLF QKQFESLLLQ NDYQNAAKVA ASSTSLRNQN TINRLKNIQA PPGAISPILL 420
YFSTLLDKGK LNKEETIELA RPVLQQDRKQ LFEKWLKEDK LECSEELGDI VKPFDTTLAL 480
ACYLRAGAHA KVISCLAELQ QFEKIIPYCQ KVGYQPNFLV LISSLIRSSP DRASEFAVSL 540
LQNPETASQI DIEKIADLFF SQNHIQQGTS LLLDALKGDT PDQGHLQTRV LEVNLLHAPQ 600
VADAILGNNI FSHYDKPTIA SLSEKAGLYQ RALENYTDIK DIKRCVVHTN ALPIDWLVGY 660
FGKLNVEQSL ACLKALMDNN IQANIQTVVQ VATKFSDLIG PSTLIKLFED YNATEGLYYY 720
LASLVNLTED KDVVYKYIEA AAKMKQYREI ERIVKDNNVY DPERVKNFLK DANLEDQLPL 780
VIVCDRFDFV HEMILYLYKS QNLKFIETYV QQVNPSKTAQ VVGALLDMDC DEAFIQSLLQ 840
SVLGQVPINE LTTEVEKRNR LKILLPFLEQ SLSQGIQDQA VYNALAKIYI DSNNSPEKFL 900
KENDQYDTLD VGHYCEKRDP YLAYIAYEKG QNDDDLIRIT NENSMYKYQA RYLLERSDLD 960
LWNKVLNQEN IHRRQLIDSV ISVGIPELTD PEPVSLTVQA FMTNGLKLEL IELLEKIILE 1020
PSPFNENVAL QGLLLLSAIK YEPTKVSSYI EKLDNYDADE IAPLCIEHDL KEEAFEIYDK 1080
HEMYGKALKV LIEDIMSLDR AASYADKINT PELWSQIGTA QLDGLRIPDA IESYIKAEDP 1140
SNYENVIDIA EQAGKYEELI PFLLMARKTL KEPKIDGALI LAYAELNKIH EIENLLAGSN 1200
VANLDHVGDK LFENKEYKAA RLCYSAVSNY SKLASTLVYL GDYQAAVDTA RKASNIKVWK 1260
LVNDACIEKK EFKLAQICGL NLIVHAEELD ELVERYESNG YFEELISLFE AGLGLERAHM 1320
GMFTELAILY SKYEPDKTFE HLKLFWSRIN IPKVIRAVEQ AHLWSELVFL YAHYDEWDNA 1380
ALTLIEKSTK DLDHAYFKEV VVKVSNLEIY YKAINFYVKF HPSLLVDLLT SLTPRLDIPR 1440
TVKIFSKSDN LPLIKPFLIN VLPKNNSVVN QAYHDLMIEE EDYKALQDAV DSYDKFDQLG 1500
LASRLESHKL IFFKKIGALL YRRNKKWAKS LSILKEEKLW KDAIETAAIS QDPKVVEALL 1560
TYFVETGNRE GFVALLYAAY NLVRIEFVLE ISWMNSLEDY IKPFEISIKK EQNDSIKKIT 1620
EELAKKSGSN EEHKDGQPLM LMNSAMNVQP TGF 1653 
Gene Ontology
 GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
 GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
 GO:0030125; C:clathrin vesicle coat; TAS:SGD.
 GO:0005198; F:structural molecule activity; TAS:SGD.
 GO:0006897; P:endocytosis; IDA:SGD.
 GO:0006886; P:intracellular protein transport; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR000547; Clathrin_H-chain/VPS_repeat.
 IPR016025; Clathrin_H-chain_link/propller.
 IPR015348; Clathrin_H-chain_linker_core.
 IPR001473; Clathrin_H-chain_propeller_N.
 IPR022365; Clathrin_H-chain_propeller_rpt.
 IPR016341; Clathrin_heavy_chain.
 IPR011990; TPR-like_helical. 
Pfam
 PF00637; Clathrin
 PF09268; Clathrin-link
 PF01394; Clathrin_propel 
SMART
 SM00299; CLH 
PROSITE
 PS50236; CHCR 
PRINTS