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Q00610

- CLH1_HUMAN

UniProt

Q00610 - CLH1_HUMAN

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Protein

Clathrin heavy chain 1

Gene

CLTC

Organism
Homo sapiens (Human)
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. clathrin light chain binding Source: FlyBase
  2. double-stranded RNA binding Source: MGI
  3. poly(A) RNA binding Source: UniProtKB
  4. protein kinase binding Source: ParkinsonsUK-UCL
  5. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. intracellular protein transport Source: UniProtKB
  3. membrane organization Source: Reactome
  4. mitotic nuclear division Source: UniProtKB
  5. negative regulation of hyaluronan biosynthetic process Source: UniProtKB
  6. negative regulation of protein localization to plasma membrane Source: UniProtKB
  7. osteoblast differentiation Source: UniProt
  8. post-Golgi vesicle-mediated transport Source: Reactome
  9. receptor internalization Source: BHF-UCL
  10. receptor-mediated endocytosis Source: UniProtKB
  11. transferrin transport Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_121399. MHC class II antigen presentation.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiQ00610.

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 1
Alternative name(s):
Clathrin heavy chain on chromosome 17
Short name:
CLH-17
Gene namesi
Name:CLTC
Synonyms:CLH17, CLTCL2, KIAA0034
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2092. CLTC.

Subcellular locationi

Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Membranecoated pit 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Melanosome 1 Publication
Note: Cytoplasmic face of coated pits and vesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. clathrin coat Source: UniProtKB
  2. clathrin-coated endocytic vesicle membrane Source: Reactome
  3. clathrin-coated vesicle Source: UniProtKB
  4. clathrin coat of coated pit Source: InterPro
  5. clathrin coat of trans-Golgi network vesicle Source: InterPro
  6. clathrin complex Source: FlyBase
  7. cytosol Source: Reactome
  8. extracellular vesicular exosome Source: UniProtKB
  9. focal adhesion Source: UniProtKB
  10. membrane Source: UniProtKB
  11. mitochondrion Source: Ensembl
  12. plasma membrane Source: Reactome
  13. protein complex Source: MGI
  14. spindle Source: UniProtKB
  15. trans-Golgi network membrane Source: Reactome
  16. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti178342. Inflammatory myofibroblastic tumor.
319308. Translocation renal cell carcinoma.
PharmGKBiPA26618.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 16751674Clathrin heavy chain 1PRO_0000205778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei184 – 1841PhosphotyrosineBy similarity
Modified residuei394 – 3941Phosphothreonine1 Publication
Modified residuei634 – 6341Phosphotyrosine1 Publication
Modified residuei737 – 7371N6-succinyllysineBy similarity
Modified residuei856 – 8561N6-acetyllysine1 Publication
Modified residuei899 – 8991PhosphotyrosineBy similarity
Modified residuei1206 – 12061PhosphotyrosineBy similarity
Modified residuei1441 – 14411N6-acetyllysine; alternate1 Publication
Modified residuei1441 – 14411N6-succinyllysine; alternateBy similarity
Modified residuei1477 – 14771Phosphotyrosine1 Publication
Modified residuei1487 – 14871PhosphotyrosineBy similarity
Modified residuei1494 – 14941Phosphoserine1 Publication
Modified residuei1501 – 15011N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00610.
PaxDbiQ00610.
PRIDEiQ00610.

PTM databases

PhosphoSiteiQ00610.

Expressioni

Gene expression databases

BgeeiQ00610.
CleanExiHS_CLTC.
ExpressionAtlasiQ00610. baseline and differential.
GenevestigatoriQ00610.

Organism-specific databases

HPAiCAB010389.
CAB011571.
CAB017155.

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 (By similarity). May interact with OCRL. Interacts with ERBB2 (By similarity). Interacts with FKBP6.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MYBP102424EBI-354967,EBI-298355
OCRLQ019684EBI-354967,EBI-6148898
TOM1L1O756744EBI-354967,EBI-712991

Protein-protein interaction databases

BioGridi107623. 125 interactions.
IntActiQ00610. 49 interactions.
MINTiMINT-4998595.
STRINGi9606.ENSP00000269122.

Structurei

Secondary structure

1
1675
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 – 448
Beta strandi47 – 548
Beta strandi62 – 654
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 – 17310
Beta strandi176 – 18510
Turni186 – 1894
Beta strandi190 – 1945
Beta strandi197 – 2048
Beta strandi213 – 22210
Beta strandi225 – 2328
Beta strandi246 – 2505
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 strandi323 – 3297
Turni331 – 3333
Helixi334 – 3407
Helixi345 – 35410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZGX-ray1.70A1-364[»]
4G55X-ray1.69A1-364[»]
ProteinModelPortaliQ00610.
SMRiQ00610. Positions 1-493, 1077-1630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati537 – 683147CHCR 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati686 – 828143CHCR 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati833 – 972140CHCR 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati979 – 1124146CHCR 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati1128 – 1269142CHCR 51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati1274 – 1420147CHCR 61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati1423 – 1566144CHCR 71 PublicationPROSITE-ProRule annotationAdd
BLAST

Region

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

Domaini

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.

Sequence similaritiesi

Belongs to the clathrin heavy chain family.Curated
Contains 7 CHCR (clathrin heavy-chain) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG314149.
GeneTreeiENSGT00400000022107.
HOGENOMiHOG000188877.
HOVERGENiHBG005344.
InParanoidiQ00610.
KOiK04646.
OMAiWKWFSEK.
OrthoDBiEOG7Z0JVM.
PhylomeDBiQ00610.
TreeFamiTF300059.

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_dom.
[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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00610-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV
60 70 80 90 100
VIIDMNDPSN PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK
110 120 130 140 150
AHTMTDDVTF WKWISLNTVA LVTDNAVYHW SMEGESQPVK MFDRHSSLAG
160 170 180 190 200
CQIINYRTDA KQKWLLLTGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAS
210 220 230 240 250
FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN QPFPKKAVDV
260 270 280 290 300
FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
310 320 330 340 350
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR
360 370 380 390 400
MAVRNNLAGA EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR
410 420 430 440 450
FQSVPAQPGQ TSPLLQYFGI LLDQGQLNKY ESLELCRPVL QQGRKQLLEK
460 470 480 490 500
WLKEDKLECS EELGDLVKSV DPTLALSVYL RANVPNKVIQ CFAETGQVQK
510 520 530 540 550
IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE EPLADITQIV
560 570 580 590 600
DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
610 620 630 640 650
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW
660 670 680 690 700
LVNYFGSLSV EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE
710 720 730 740 750
LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE
760 770 780 790 800
SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNNLQKYI
810 820 830 840 850
EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF STDELVAEVE
860 870 880 890 900
KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
910 920 930 940 950
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR
960 970 980 990 1000
KDPELWGSVL LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL
1010 1020 1030 1040 1050
PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYINRLDNY
1060 1070 1080 1090 1100
DAPDIANIAI SNELFEEAFA IFRKFDVNTS AVQVLIEHIG NLDRAYEFAE
1110 1120 1130 1140 1150
RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV VQAANTSGNW
1160 1170 1180 1190 1200
EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
1210 1220 1230 1240 1250
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST
1260 1270 1280 1290 1300
RTWKEVCFAC VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI
1310 1320 1330 1340 1350
TMLEAALGLE RAHMGMFTEL AILYSKFKPQ KMREHLELFW SRVNIPKVLR
1360 1370 1380 1390 1400
AAEQAHLWAE LVFLYDKYEE YDNAIITMMN HPTDAWKEGQ FKDIITKVAN
1410 1420 1430 1440 1450
VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS KVKQLPLVKP
1460 1470 1480 1490 1500
YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
1510 1520 1530 1540 1550
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA
1560 1570 1580 1590 1600
EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI
1610 1620 1630 1640 1650
QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP
1660 1670
PQAPFGYGYT APPYGQPQPG FGYSM
Length:1,675
Mass (Da):191,615
Last modified:January 23, 2007 - v5
Checksum:i6C4F2D54950079E2
GO
Isoform 2 (identifier: Q00610-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1636-1639: QPQL → NLSL
     1640-1675: Missing.

Note: No experimental confirmation available.

Show »
Length:1,639
Mass (Da):187,890
Checksum:i9CE5237A31C9B0C6
GO

Sequence cautioni

The sequence BAA04801.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 5601Q → R in CAA39363. (PubMed:1765375)Curated
Sequence conflicti817 – 8171G → V in CAA39363. (PubMed:1765375)Curated
Sequence conflicti923 – 9231R → H in CAE45761. (PubMed:17974005)Curated
Sequence conflicti1563 – 15631R → G in CAE45761. (PubMed:17974005)Curated
Sequence conflicti1652 – 16521Q → R in CAE45761. (PubMed:17974005)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1636 – 16394QPQL → NLSL in isoform 2. 1 PublicationVSP_011570
Alternative sequencei1640 – 167536Missing in isoform 2. 1 PublicationVSP_011571Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21260 mRNA. Translation: BAA04801.2. Different initiation.
BX640615 mRNA. Translation: CAE45761.1.
CH471109 Genomic DNA. Translation: EAW94396.1.
CH471109 Genomic DNA. Translation: EAW94399.1.
BC051800 mRNA. Translation: AAH51800.1.
BC054489 mRNA. Translation: AAH54489.1.
X55878 mRNA. Translation: CAA39363.1.
CCDSiCCDS32696.1. [Q00610-1]
PIRiA40573.
RefSeqiNP_004850.1. NM_004859.3. [Q00610-1]
UniGeneiHs.491351.

Genome annotation databases

EnsembliENST00000269122; ENSP00000269122; ENSG00000141367. [Q00610-1]
ENST00000393043; ENSP00000376763; ENSG00000141367. [Q00610-2]
GeneIDi1213.
KEGGihsa:1213.
UCSCiuc002ixp.3. human. [Q00610-2]
uc002ixq.1. human. [Q00610-1]

Polymorphism databases

DMDMi1705916.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Clathrin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21260 mRNA. Translation: BAA04801.2 . Different initiation.
BX640615 mRNA. Translation: CAE45761.1 .
CH471109 Genomic DNA. Translation: EAW94396.1 .
CH471109 Genomic DNA. Translation: EAW94399.1 .
BC051800 mRNA. Translation: AAH51800.1 .
BC054489 mRNA. Translation: AAH54489.1 .
X55878 mRNA. Translation: CAA39363.1 .
CCDSi CCDS32696.1. [Q00610-1 ]
PIRi A40573.
RefSeqi NP_004850.1. NM_004859.3. [Q00610-1 ]
UniGenei Hs.491351.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XZG X-ray 1.70 A 1-364 [» ]
4G55 X-ray 1.69 A 1-364 [» ]
ProteinModelPortali Q00610.
SMRi Q00610. Positions 1-493, 1077-1630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107623. 125 interactions.
IntActi Q00610. 49 interactions.
MINTi MINT-4998595.
STRINGi 9606.ENSP00000269122.

Chemistry

ChEMBLi CHEMBL3108634.

PTM databases

PhosphoSitei Q00610.

Polymorphism databases

DMDMi 1705916.

Proteomic databases

MaxQBi Q00610.
PaxDbi Q00610.
PRIDEi Q00610.

Protocols and materials databases

DNASUi 1213.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269122 ; ENSP00000269122 ; ENSG00000141367 . [Q00610-1 ]
ENST00000393043 ; ENSP00000376763 ; ENSG00000141367 . [Q00610-2 ]
GeneIDi 1213.
KEGGi hsa:1213.
UCSCi uc002ixp.3. human. [Q00610-2 ]
uc002ixq.1. human. [Q00610-1 ]

Organism-specific databases

CTDi 1213.
GeneCardsi GC17P057697.
H-InvDB HIX0039315.
HGNCi HGNC:2092. CLTC.
HPAi CAB010389.
CAB011571.
CAB017155.
MIMi 118955. gene.
neXtProti NX_Q00610.
Orphaneti 178342. Inflammatory myofibroblastic tumor.
319308. Translocation renal cell carcinoma.
PharmGKBi PA26618.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314149.
GeneTreei ENSGT00400000022107.
HOGENOMi HOG000188877.
HOVERGENi HBG005344.
InParanoidi Q00610.
KOi K04646.
OMAi WKWFSEK.
OrthoDBi EOG7Z0JVM.
PhylomeDBi Q00610.
TreeFami TF300059.

Enzyme and pathway databases

Reactomei REACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_121399. MHC class II antigen presentation.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinki Q00610.

Miscellaneous databases

ChiTaRSi CLTC. human.
EvolutionaryTracei Q00610.
GeneWikii CLTC.
GenomeRNAii 1213.
NextBioi 4999.
PROi Q00610.
SOURCEi Search...

Gene expression databases

Bgeei Q00610.
CleanExi HS_CLTC.
ExpressionAtlasi Q00610. baseline and differential.
Genevestigatori Q00610.

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_dom.
[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

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: PNS and Testis.
  5. "Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter."
    Dodge G.R., Kovalszky I., McBride O.W., Yi H.F., Chu M.-L., Saitta B., Stokes D.G., Iozzo R.V.
    Genomics 11:174-178(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 560-864 (ISOFORMS 1/2).
    Tissue: Colon.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Tissue: Platelet.
  7. Cited for: PROTEIN SEQUENCE OF 2-8; 64-78; 87-96; 164-205; 228-245; 270-278; 298-320; 355-382; 469-481; 507-519; 572-610; 626-638; 799-806; 831-852; 855-865; 882-903; 1011-1037; 1074-1101; 1123-1130; 1166-1179; 1183-1204; 1216-1245; 1312-1326; 1398-1406; 1435-1453; 1482-1498; 1502-1508; 1510-1516 AND 1610-1620, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Hepatoma and Mammary carcinoma.
  8. "The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis."
    Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E.
    Hum. Mol. Genet. 10:1807-1817(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIP1.
  9. "Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
    Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
    Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB2.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  11. "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes."
    Jarczowski F., Fischer G., Edlich F.
    Biochemistry 47:6946-6952(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP6.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-634 AND TYR-1477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-856; LYS-1441 AND LYS-1501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-364 IN COMPLEX WITH INHIBITORS, WD40-LIKE REPEATS.

Entry informationi

Entry nameiCLH1_HUMAN
AccessioniPrimary (citable) accession number: Q00610
Secondary accession number(s): D3DU00, Q6N0A0, Q86TF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 150 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3