CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005809
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Clathrin heavy chain 
Protein Synonyms/Alias
  
Gene Name
 Chc 
Gene Synonyms/Alias
 CG9012 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
370LFVRKFNKLFTAGQYacetylation[1]
743ACKTNQIKEVERICRacetylation[1]
1502ALAQKLEKHELTEFRacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
Functional Description
 Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. 
Sequence Annotation
 REPEAT 538 684 CHCR 1.
 REPEAT 687 829 CHCR 2.
 REPEAT 834 973 CHCR 3.
 REPEAT 980 1125 CHCR 4.
 REPEAT 1129 1270 CHCR 5.
 REPEAT 1275 1421 CHCR 6.
 REPEAT 1424 1567 CHCR 7.
 REGION 24 67 WD40-like repeat 1.
 REGION 68 107 WD40-like repeat 2.
 REGION 108 149 WD40-like repeat 3.
 REGION 150 195 WD40-like repeat 4.
 REGION 196 257 WD40-like repeat 5.
 REGION 258 301 WD40-like repeat 6.
 REGION 302 330 WD40-like repeat 7.
 REGION 1334 1643 Involved in binding clathrin light chain
 REGION 1552 1677 Trimerization (By similarity).  
Keyword
 Coated pit; Complete proteome; Cytoplasmic vesicle; Membrane; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1678 AA 
Protein Sequence
MTQPLPIRFQ EHLQLTNVGI NANSFSFSTL TMESDKFICV REKVNDTAQV VIIDMNDATN 60
PTRRPISADS AIMNPASKVI ALKAQKTLQI FNIEMKSKMK AHTMNEDVVF WKWISLNTLA 120
LVTETSVFHW SMEGDSMPQK MFDRHSSLNG CQIINYRCNA SQQWLLLVGI SALPSRVAGA 180
MQLYSVERKV SQAIEGHAAS FATFKIDANK EPTTLFCFAV RTATGGKLHI IEVGAPPNGN 240
QPFAKKAVDV FFPPEAQNDF PVAMQVSAKY DTIYLITKYG YIHLYDMETA TCIYMNRISA 300
DTIFVTAPHE ASGGIIGVNR KGQVLSVTVD EEQIIPYINT VLQNPDLALR MAVRNNLAGA 360
EDLFVRKFNK LFTAGQYAEA AKVAALAPKA ILRTPQTIQR FQQVQTPAGS TTPPLLQYFG 420
ILLDQGKLNK FESLELCRPV LLQGKKQLCE KWLKEEKLEC SEELGDLVKA SDLTLALSIY 480
LRANVPNKVI QCFAETGQFQ KIVLYAKKVN YTPDYVFLLR SVMRSNPEQG AGFASMLVAE 540
EEPLADINQI VDIFMEHSMV QQCTAFLLDA LKHNRPAEGA LQTRLLEMNL MSAPQVADAI 600
LGNAMFTHYD RAHIAQLCEK AGLLQRALEH YTDLYDIKRA VVHTHMLNAE WLVSFFGTLS 660
VEDSLECLKA MLTANLRQNL QICVQIATKY HEQLTNKALI DLFEGFKSYD GLFYFLSSIV 720
NFSQDPEVHF KYIQAACKTN QIKEVERICR ESNCYNPERV KNFLKEAKLT DQLPLIIVCD 780
RFDFVHDLVL YLYRNNLQKY IEIYVQKVNP SRLPVVVGGL LDVDCSEDII KNLILVVKGQ 840
FSTDELVEEV EKRNRLKLLL PWLESRVHEG CVEPATHNAL AKIYIDSNNN PERYLKENQY 900
YDSRVVGRYC EKRDPHLACV AYERGLCDRE LIAVCNENSL FKSEARYLVG RRDAELWAEV 960
LSESNPYKRQ LIDQVVQTAL SETQDPDDIS VTVKAFMTAD LPNELIELLE KIILDSSVFS 1020
DHRNLQNLLI LTAIKADRTR VMDYINRLEN YDAPDIANIA ISNQLYEEAF AIFKKFDVNT 1080
SAIQVLIDQV NNLERANEFA ERCNEPAVWS QLAKAQLQQG LVKEAIDSYI KADDPSAYVD 1140
VVDVASKVES WDDLVRYLQM ARKKARESYI ESELIYAYAR TGRLADLEEF ISGPNHADIQ 1200
KIGNRCFSDG MYDAAKLLYN NVSNFARLAI TLVYLKEFQG AVDSARKANS TRTWKEVCFA 1260
CVDAEEFRLA QMCGLHIVVH ADELEDLINY YQNRGYFDEL IALLESALGL ERAHMGMFTE 1320
LAILYSKFKP SKMREHLELF WSRVNIPKVL RAAESAHLWS ELVFLYDKYE EYDNAVLAMM 1380
AHPTEAWREG HFKDIITKVA NIELYYKAIE FYLDFKPLLL NDMLLVLAPR MDHTRAVSYF 1440
SKTGYLPLVK PYLRSVQSLN NKAINEALNG LLIDEEDYQG LRNSIDGFDN FDNIALAQKL 1500
EKHELTEFRR IAAYLYKGNN RWKQSVELCK KDKLYKDAME YAAESCKQDI AEELLGWFLE 1560
RDAYDCFAAC LYQCYDLLRP DVILELAWKH KIVDFAMPYL IQVLREYTTK VDKLELNEAQ 1620
REKEDDSTEH KNIIQMEPQL MITAGPAMGI PPQYAQNYPP GAATVTAAGG RNMGYPYL 1678 
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:FlyBase.
 GO:0005905; C:coated pit; TAS:FlyBase.
 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
 GO:0005886; C:plasma membrane; IDA:FlyBase.
 GO:0030141; C:secretory granule; IDA:FlyBase.
 GO:0008021; C:synaptic vesicle; TAS:FlyBase.
 GO:0005802; C:trans-Golgi network; IDA:FlyBase.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
 GO:0033227; P:dsRNA transport; IMP:FlyBase.
 GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
 GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
 GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
 GO:0007594; P:puparial adhesion; IMP:FlyBase.
 GO:0040008; P:regulation of growth; IMP:FlyBase.
 GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
 GO:0033363; P:secretory granule organization; IMP:FlyBase.
 GO:0007291; P:sperm individualization; IMP:FlyBase.
 GO:0016183; P:synaptic vesicle coating; TAS:FlyBase.
 GO:0016079; P:synaptic vesicle exocytosis; IMP:FlyBase. 
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