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P49951

- CLH1_BOVIN

UniProt

P49951 - CLH1_BOVIN

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Protein
Clathrin heavy chain 1
Gene
CLTC
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. intracellular protein transport Source: InterPro
  2. negative regulation of hyaluronan biosynthetic process Source: UniProtKB
  3. vesicle-mediated transport Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 1
Gene namesi
Name:CLTC
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. clathrin coat of coated pit Source: InterPro
  2. clathrin coat of trans-Golgi network vesicle Source: InterPro
  3. melanosome Source: UniProtKB-SubCell
  4. membrane coat Source: AgBase
  5. mitochondrion Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 16751674Clathrin heavy chain 1
PRO_0000205777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei184 – 1841Phosphotyrosine By similarity
Modified residuei394 – 3941Phosphothreonine By similarity
Modified residuei634 – 6341Phosphotyrosine By similarity
Modified residuei737 – 7371N6-succinyllysine By similarity
Modified residuei856 – 8561N6-acetyllysine By similarity
Modified residuei899 – 8991Phosphotyrosine By similarity
Modified residuei1206 – 12061Phosphotyrosine By similarity
Modified residuei1441 – 14411N6-acetyllysine; alternate By similarity
Modified residuei1441 – 14411N6-succinyllysine; alternate By similarity
Modified residuei1477 – 14771Phosphotyrosine By similarity
Modified residuei1487 – 14871Phosphotyrosine By similarity
Modified residuei1494 – 14941Phosphoserine By similarity
Modified residuei1501 – 15011N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP49951.
PRIDEiP49951.

Interactioni

Subunit structurei

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat. In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1. Interacts with DENND1A, DENND1B and DENND1C. Interacts with OCRL. Interacts with ERBB2. Interacts with FKBP6 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-448355,EBI-448355

Protein-protein interaction databases

BioGridi158448. 1 interaction.
IntActiP49951. 7 interactions.
MINTiMINT-122490.
STRINGi9913.ENSBTAP00000022210.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149
Helixi15 – 184
Helixi22 – 243
Turni27 – 293
Beta strandi30 – 345
Beta strandi37 – 426
Beta strandi49 – 546
Beta strandi62 – 665
Beta strandi69 – 735
Beta strandi75 – 8410
Beta strandi87 – 926
Turni93 – 964
Beta strandi97 – 1037
Beta strandi108 – 1136
Beta strandi115 – 13319
Beta strandi139 – 1435
Helixi146 – 1483
Beta strandi152 – 1587
Beta strandi164 – 1729
Beta strandi177 – 1859
Turni186 – 1894
Beta strandi190 – 1945
Beta strandi197 – 2048
Beta strandi213 – 22210
Beta strandi225 – 2328
Beta strandi246 – 2494
Beta strandi261 – 2677
Turni268 – 2714
Beta strandi272 – 2776
Beta strandi280 – 2867
Turni287 – 2893
Beta strandi292 – 2976
Beta strandi303 – 3097
Helixi310 – 3123
Beta strandi314 – 3196
Beta strandi322 – 3298
Turni331 – 3333
Helixi334 – 3407
Helixi345 – 35511
Helixi1183 – 11864
Turni1187 – 11915
Turni1211 – 12133
Helixi1214 – 12207
Helixi1224 – 12329
Turni1233 – 12353
Helixi1237 – 124711
Helixi1250 – 126213
Helixi1266 – 12716
Turni1272 – 12787
Helixi1280 – 129213
Helixi1296 – 130611
Helixi1314 – 132512
Helixi1329 – 133911
Helixi1345 – 13539
Turni1354 – 13563
Helixi1358 – 136710
Helixi1371 – 138010
Turni1382 – 13854
Helixi1388 – 139710
Helixi1402 – 141413
Helixi1416 – 14183
Helixi1419 – 14268
Helixi1427 – 14293
Helixi1432 – 144110
Turni1445 – 14484
Helixi1449 – 14568
Helixi1461 – 147313
Helixi1477 – 148610
Helixi1492 – 14998
Helixi1505 – 151511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B89X-ray2.60A1074-1522[»]
1UTCX-ray2.30A/B1-363[»]
1XI4electron microscopy7.90A/B/C/D/E/F/G/H/I1-1630[»]
1XI5electron microscopy12.00A/B/C/D/E/F/G/H/I1-1630[»]
3GC3X-ray2.20B1-363[»]
3GD1X-ray3.50I1-363[»]
3IYVelectron microscopy7.90A/B/C/D/E/F/G/H/I1-1630[»]
3LVGX-ray7.94A/B/C1074-1675[»]
3LVHX-ray9.00A/B/C1074-1675[»]
3QILX-ray3.92A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1521-1624[»]
ProteinModelPortaliP49951.
SMRiP49951. Positions 1-493, 1182-1516.

Miscellaneous databases

EvolutionaryTraceiP49951.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati537 – 683147CHCR 1
Add
BLAST
Repeati686 – 828143CHCR 2
Add
BLAST
Repeati833 – 972140CHCR 3
Add
BLAST
Repeati979 – 1124146CHCR 4
Add
BLAST
Repeati1128 – 1269142CHCR 5
Add
BLAST
Repeati1274 – 1420147CHCR 6
Add
BLAST
Repeati1423 – 1566144CHCR 7
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 479478Globular terminal domain
Add
BLAST
Regioni24 – 6744WD40-like repeat 1
Add
BLAST
Regioni68 – 10740WD40-like repeat 2
Add
BLAST
Regioni108 – 14942WD40-like repeat 3
Add
BLAST
Regioni150 – 19546WD40-like repeat 4
Add
BLAST
Regioni196 – 25762WD40-like repeat 5
Add
BLAST
Regioni258 – 30144WD40-like repeat 6
Add
BLAST
Regioni302 – 33029WD40-like repeat 7
Add
BLAST
Regioni449 – 46517Binding site for the uncoating ATPase, involved in lattice disassembly Reviewed prediction
Add
BLAST
Regioni480 – 52344Flexible linker
Add
BLAST
Regioni524 – 16751152Heavy chain arm
Add
BLAST
Regioni524 – 634111Distal segment
Add
BLAST
Regioni639 – 16751037Proximal segment
Add
BLAST
Regioni1213 – 1522310Involved in binding clathrin light chain
Add
BLAST
Regioni1550 – 1675126Trimerization
Add
BLAST

Domaini

The C-terminal third of the heavy chains forms the hub of the triskelion. This region contains the trimerization domain and the light-chain binding domain involved in the assembly of the clathrin lattice.
The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It consitutes a major protein-protein interaction node By similarity.

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG314149.
HOVERGENiHBG005344.
KOiK04646.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProiIPR016024. 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.
[Graphical view]
PfamiPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view]
PIRSFiPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTiSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEiPS50236. CHCR. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49951-1 [UniParc]FASTAAdd to Basket

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MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV     50
VIIDMNDPSN PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK 100
AHTMTDDVTF WKWISLNTVA LVTDNAVYHW SMEGESQPVK MFDRHSSLAG 150
CQIINYRTDA KQKWLLLTGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAS 200
FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN QPFPKKAVDV 250
FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG 300
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR 350
MAVRNNLAGA EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR 400
FQSVPAQPGQ TSPLLQYFGI LLDQGQLNKY ESLELCRPVL QQGRKQLLEK 450
WLKEDKLECS EELGDLVKSV DPTLALSVYL RANVPNKVIQ CFAETGQVQK 500
IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE EPLADITQIV 550
DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL 600
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW 650
LVNYFGSLSV EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE 700
LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE 750
SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNNLQKYI 800
EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF STDELVAEVE 850
KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY 900
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR 950
KDPELWGSVL LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL 1000
PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYINRLDNY 1050
DAPDIANIAI SNELFEEAFA IFRKFDVNTS AVQVLIEHIG NLDRAYEFAE 1100
RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV VQAANTSGNW 1150
EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ 1200
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST 1250
RTWKEVCFAC VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI 1300
TMLEAALGLE RAHMGMFTEL AILYSKFKPQ KMREHLELFW SRVNIPKVLR 1350
AAEQAHLWAE LVFLYDKYEE YDNAIITMMN HPTDAWKEGQ FKDIITKVAN 1400
VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS KVKQLPLVKP 1450
YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE 1500
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA 1550
EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI 1600
QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP 1650
PQAPFGYGYT APAYGQPQPG FGYSM 1675
Length:1,675
Mass (Da):191,589
Last modified:October 1, 1996 - v1
Checksum:i6C4F2D54801579E2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31757 mRNA. Translation: AAC48524.1.
RefSeqiNP_776448.1. NM_174023.2.
UniGeneiBt.44506.

Genome annotation databases

GeneIDi281080.
KEGGibta:281080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31757 mRNA. Translation: AAC48524.1 .
RefSeqi NP_776448.1. NM_174023.2.
UniGenei Bt.44506.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B89 X-ray 2.60 A 1074-1522 [» ]
1UTC X-ray 2.30 A/B 1-363 [» ]
1XI4 electron microscopy 7.90 A/B/C/D/E/F/G/H/I 1-1630 [» ]
1XI5 electron microscopy 12.00 A/B/C/D/E/F/G/H/I 1-1630 [» ]
3GC3 X-ray 2.20 B 1-363 [» ]
3GD1 X-ray 3.50 I 1-363 [» ]
3IYV electron microscopy 7.90 A/B/C/D/E/F/G/H/I 1-1630 [» ]
3LVG X-ray 7.94 A/B/C 1074-1675 [» ]
3LVH X-ray 9.00 A/B/C 1074-1675 [» ]
3QIL X-ray 3.92 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1521-1624 [» ]
ProteinModelPortali P49951.
SMRi P49951. Positions 1-493, 1182-1516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158448. 1 interaction.
IntActi P49951. 7 interactions.
MINTi MINT-122490.
STRINGi 9913.ENSBTAP00000022210.

Proteomic databases

PaxDbi P49951.
PRIDEi P49951.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281080.
KEGGi bta:281080.

Organism-specific databases

CTDi 1213.

Phylogenomic databases

eggNOGi NOG314149.
HOVERGENi HBG005344.
KOi K04646.

Miscellaneous databases

EvolutionaryTracei P49951.
NextBioi 20805158.

Family and domain databases

Gene3Di 1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view ]
PIRSFi PIRSF002290. Clathrin_H_chain. 1 hit.
SMARTi SM00299. CLH. 7 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEi PS50236. CHCR. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs."
    Liu S.-H., Wong M.L., Craik C.S., Brodsky F.M.
    Cell 83:257-267(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
    Marat A.L., McPherson P.S.
    J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C.

Entry informationi

Entry nameiCLH1_BOVIN
AccessioniPrimary (citable) accession number: P49951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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