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Q00610 (CLH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Clathrin heavy chain 1
Alternative name(s):
Clathrin heavy chain on chromosome 17
Short name=CLH-17
Gene names
Name:CLTC
Synonyms:CLH17, CLTCL2, KIAA0034
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1675 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side. Melanosome. Note: Cytoplasmic face of coated pits and vesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10

Domain

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 similarities

Belongs to the clathrin heavy chain family.

Contains 7 CHCR (clathrin heavy-chain) repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCoated pit
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

intracellular protein transport

Non-traceable author statement Ref.5. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from mutant phenotype PubMed 15858577. Source: UniProtKB

negative regulation of hyaluronan biosynthetic process

Inferred from direct assay PubMed 24251095. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

receptor internalization

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

receptor-mediated endocytosis

Inferred from mutant phenotype PubMed 15858577. Source: UniProtKB

transferrin transport

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

   Cellular_componentclathrin coat

Non-traceable author statement Ref.5. Source: UniProtKB

clathrin coat of coated pit

Inferred from electronic annotation. Source: InterPro

clathrin coat of trans-Golgi network vesicle

Inferred from electronic annotation. Source: InterPro

clathrin complex

Inferred from direct assay PubMed 4066749. Source: FlyBase

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

clathrin-coated vesicle

Inferred from direct assay PubMed 19478182. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from direct assay PubMed 21266579. Source: MGI

spindle

Inferred from direct assay PubMed 15858577. Source: UniProtKB

trans-Golgi network membrane

Traceable author statement. Source: Reactome

   Molecular_functionclathrin light chain binding

Inferred from physical interaction PubMed 4066749. Source: FlyBase

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19478182. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: ParkinsonsUK-UCL

structural molecule activity

Non-traceable author statement Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q00610-1)

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.
Isoform 2 (identifier: Q00610-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1636-1639: QPQL → NLSL
     1640-1675: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 16751674Clathrin heavy chain 1
PRO_0000205778

Regions

Repeat537 – 683147CHCR 1
Repeat686 – 828143CHCR 2
Repeat833 – 972140CHCR 3
Repeat979 – 1124146CHCR 4
Repeat1128 – 1269142CHCR 5
Repeat1274 – 1420147CHCR 6
Repeat1423 – 1566144CHCR 7
Region2 – 479478Globular terminal domain
Region24 – 6744WD40-like repeat 1
Region68 – 10740WD40-like repeat 2
Region108 – 14942WD40-like repeat 3
Region150 – 19546WD40-like repeat 4
Region196 – 25762WD40-like repeat 5
Region258 – 30144WD40-like repeat 6
Region302 – 33029WD40-like repeat 7
Region449 – 46517Binding site for the uncoating ATPase, involved in lattice disassembly Potential
Region480 – 52344Flexible linker
Region524 – 16751152Heavy chain arm
Region524 – 634111Distal segment
Region639 – 16751037Proximal segment
Region1213 – 1522310Involved in binding clathrin light chain By similarity
Region1550 – 1675126Trimerization By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.19 Ref.20
Modified residue1841Phosphotyrosine By similarity
Modified residue3941Phosphothreonine Ref.13
Modified residue6341Phosphotyrosine Ref.15
Modified residue7371N6-succinyllysine By similarity
Modified residue8561N6-acetyllysine Ref.16
Modified residue8991Phosphotyrosine By similarity
Modified residue12061Phosphotyrosine By similarity
Modified residue14411N6-acetyllysine; alternate Ref.16
Modified residue14411N6-succinyllysine; alternate By similarity
Modified residue14771Phosphotyrosine Ref.15
Modified residue14871Phosphotyrosine By similarity
Modified residue14941Phosphoserine Ref.14
Modified residue15011N6-acetyllysine Ref.16

Natural variations

Alternative sequence1636 – 16394QPQL → NLSL in isoform 2.
VSP_011570
Alternative sequence1640 – 167536Missing in isoform 2.
VSP_011571

Experimental info

Sequence conflict5601Q → R in CAA39363. Ref.5
Sequence conflict8171G → V in CAA39363. Ref.5
Sequence conflict9231R → H in CAE45761. Ref.2
Sequence conflict15631R → G in CAE45761. Ref.2
Sequence conflict16521Q → R in CAE45761. Ref.2

Secondary structure

.................................................................... 1675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 6C4F2D54950079E2

FASTA1,675191,615
        10         20         30         40         50         60 
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN 

        70         80         90        100        110        120 
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA 

       130        140        150        160        170        180 
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA 

       190        200        210        220        230        240 
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN 

       250        260        270        280        290        300 
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG 

       310        320        330        340        350        360 
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA 

       370        380        390        400        410        420 
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI 

       430        440        450        460        470        480 
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL 

       490        500        510        520        530        540 
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE 

       550        560        570        580        590        600 
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL 

       610        620        630        640        650        660 
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV 

       670        680        690        700        710        720 
EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN 

       730        740        750        760        770        780 
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR 

       790        800        810        820        830        840 
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF 

       850        860        870        880        890        900 
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY 

       910        920        930        940        950        960 
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL 

       970        980        990       1000       1010       1020 
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE 

      1030       1040       1050       1060       1070       1080 
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS 

      1090       1100       1110       1120       1130       1140 
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV 

      1150       1160       1170       1180       1190       1200 
VQAANTSGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ 

      1210       1220       1230       1240       1250       1260 
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC 

      1270       1280       1290       1300       1310       1320 
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL 

      1330       1340       1350       1360       1370       1380 
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN 

      1390       1400       1410       1420       1430       1440 
HPTDAWKEGQ FKDIITKVAN VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS 

      1450       1460       1470       1480       1490       1500 
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE 

      1510       1520       1530       1540       1550       1560 
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE 

      1570       1580       1590       1600       1610       1620 
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR 

      1630       1640       1650       1660       1670 
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM 

« Hide

Isoform 2 [UniParc].

Checksum: 9CE5237A31C9B0C6
Show »

FASTA1,639187,890

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal kidney.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (FEB-2008) to UniProtKB
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition."
von Kleist L., Stahlschmidt W., Bulut H., Gromova K., Puchkov D., Robertson M.J., MacGregor K.A., Tomilin N., Pechstein A., Chau N., Chircop M., Sakoff J., von Kries J.P., Saenger W., Krausslich H.G., Shupliakov O., Robinson P.J., McCluskey A., Haucke V.
Cell 146:471-484(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-364 IN COMPLEX WITH INHIBITORS, WD40-LIKE REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32696.1. [Q00610-1]
PIRA40573.
RefSeqNP_004850.1. NM_004859.3. [Q00610-1]
UniGeneHs.491351.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZGX-ray1.70A1-364[»]
4G55X-ray1.69A1-364[»]
ProteinModelPortalQ00610.
SMRQ00610. Positions 1-493, 1077-1630.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107623. 121 interactions.
IntActQ00610. 46 interactions.
MINTMINT-4998595.
STRING9606.ENSP00000269122.

PTM databases

PhosphoSiteQ00610.

Polymorphism databases

DMDM1705916.

Proteomic databases

MaxQBQ00610.
PaxDbQ00610.
PRIDEQ00610.

Protocols and materials databases

DNASU1213.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269122; ENSP00000269122; ENSG00000141367. [Q00610-1]
ENST00000393043; ENSP00000376763; ENSG00000141367. [Q00610-2]
GeneID1213.
KEGGhsa:1213.
UCSCuc002ixp.3. human. [Q00610-2]
uc002ixq.1. human. [Q00610-1]

Organism-specific databases

CTD1213.
GeneCardsGC17P057697.
H-InvDBHIX0039315.
HGNCHGNC:2092. CLTC.
HPACAB010389.
CAB011571.
CAB017155.
MIM118955. gene.
neXtProtNX_Q00610.
Orphanet178342. Inflammatory myofibroblastic tumor.
319308. Translocation renal cell carcinoma.
PharmGKBPA26618.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314149.
HOGENOMHOG000188877.
HOVERGENHBG005344.
InParanoidQ00610.
KOK04646.
OMAWKWFSEK.
OrthoDBEOG7Z0JVM.
PhylomeDBQ00610.
TreeFamTF300059.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.
SignaLinkQ00610.

Gene expression databases

ArrayExpressQ00610.
BgeeQ00610.
CleanExHS_CLTC.
GenevestigatorQ00610.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProIPR016024. 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]
PfamPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view]
PIRSFPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEPS50236. CHCR. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLTC. human.
EvolutionaryTraceQ00610.
GeneWikiCLTC.
GenomeRNAi1213.
NextBio4999.
PROQ00610.
SOURCESearch...

Entry information

Entry nameCLH1_HUMAN
AccessionPrimary (citable) accession number: Q00610
Secondary accession number(s): D3DU00, Q6N0A0, Q86TF2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM