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UniProtKB - Q00610 (CLH1_HUMAN)

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Protein

Clathrin heavy chain 1

Gene

CLTC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872).5 Publications

GO - Molecular functioni

  • clathrin light chain binding Source: FlyBase
  • disordered domain specific binding Source: CAFA
  • double-stranded RNA binding Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL
  • RNA binding Source: UniProtKB
  • structural molecule activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  • autophagy Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • clathrin coat assembly Source: CAFA
  • intracellular protein transport Source: UniProtKB
  • low-density lipoprotein particle clearance Source: Reactome
  • low-density lipoprotein particle receptor catabolic process Source: Reactome
  • membrane organization Source: Reactome
  • microtubule-based movement Source: Reactome
  • mitotic cell cycle Source: UniProtKB
  • negative regulation of hyaluronan biosynthetic process Source: UniProtKB
  • negative regulation of protein localization to plasma membrane Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • receptor internalization Source: BHF-UCL
  • receptor-mediated endocytosis Source: UniProtKB
  • regulation of mitotic spindle organization Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • transferrin transport Source: BHF-UCL
  • Wnt signaling pathway, planar cell polarity pathway Source: Reactome
Complete GO annotation...

Keywordsi

Biological processAutophagy, Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-168275. Entry of Influenza Virion into Host Cell via Endocytosis.
R-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-432720. Lysosome Vesicle Biogenesis.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5140745. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8866427. VLDLR internalisation and degradation.
R-HSA-8964038. LDL clearance.
SignaLinkiQ00610.
SIGNORiQ00610.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:2092. CLTC.

Subcellular locationi

GO - Cellular componenti

  • clathrin coat Source: CAFA
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • clathrin-coated vesicle Source: UniProtKB
  • clathrin coat of coated pit Source: InterPro
  • clathrin coat of trans-Golgi network vesicle Source: InterPro
  • clathrin complex Source: FlyBase
  • cytosol Source: Reactome
  • endolysosome membrane Source: Reactome
  • endosome Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular vesicle Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lysosome Source: HPA
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • mitotic spindle microtubule Source: UniProtKB
  • plasma membrane Source: Reactome
  • protein complex Source: MGI
  • spindle Source: UniProtKB
  • trans-Golgi network membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65P → N: Disrupts spindle localization. 1 Publication1
Mutagenesisi67S → G: Disrupts spindle localization. 1 Publication1
Mutagenesisi87T → A: Disrupts spindle localization. 1 Publication1
Mutagenesisi89Q → A: Disrupts spindle localization. 1 Publication1
Mutagenesisi96K → E: Disrupts spindle localization. 1 Publication1
Mutagenesisi98K → E: Disrupts spindle localization. 1 Publication1
Mutagenesisi444R → E: Disrupts spindle localization; when associated with E-445, E-500 E-506 and E-507. 1 Publication1
Mutagenesisi445K → E: Disrupts spindle localization; when associated with E-444, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi480 – 484LRANV → ERGQC: Disrupts spindle localization and interaction with TACC3. 1 Publication5
Mutagenesisi481R → E: Disrupts spindle localization; when associated with E-487, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi487K → E: Disrupts spindle localization; when associated with E-481, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi500K → E: Disrupts spindle localization; when associated with E-444, E-445, E-506 and E-507. 1 Publication1
Mutagenesisi500K → E: Disrupts spindle localization; when associated with E-481, E-487, E-506 and E-507. 1 Publication1
Mutagenesisi506K → E: Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-507. 1 Publication1
Mutagenesisi506K → E: Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-507. 1 Publication1
Mutagenesisi507K → E: Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-506. 1 Publication1
Mutagenesisi507K → E: Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-506. 1 Publication1

Organism-specific databases

DisGeNETi1213.
MalaCardsiCLTC.
OpenTargetsiENSG00000141367.
Orphaneti178342. Inflammatory myofibroblastic tumor.
319308. Translocation renal cell carcinoma.
PharmGKBiPA26618.

Chemistry databases

ChEMBLiCHEMBL3108634.

Polymorphism and mutation databases

BioMutaiCLTC.
DMDMi1705916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00002057782 – 1675Clathrin heavy chain 1Add BLAST1674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei67PhosphoserineCombined sources1
Modified residuei105PhosphothreonineBy similarity1
Modified residuei184PhosphotyrosineBy similarity1
Modified residuei394PhosphothreonineCombined sources1
Modified residuei634PhosphotyrosineCombined sources1
Modified residuei737N6-succinyllysineBy similarity1
Modified residuei856N6-acetyllysineCombined sources1
Modified residuei899PhosphotyrosineBy similarity1
Modified residuei1167PhosphoserineBy similarity1
Modified residuei1206PhosphotyrosineBy similarity1
Modified residuei1229PhosphoserineCombined sources1
Modified residuei1441N6-acetyllysine; alternateCombined sources1
Modified residuei1441N6-succinyllysine; alternateBy similarity1
Modified residuei1477PhosphotyrosineCombined sources1
Modified residuei1487PhosphotyrosineBy similarity1
Modified residuei1494PhosphoserineCombined sources1
Modified residuei1501N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ00610.
MaxQBiQ00610.
PaxDbiQ00610.
PeptideAtlasiQ00610.
PRIDEiQ00610.

PTM databases

iPTMnetiQ00610.
PhosphoSitePlusiQ00610.
SwissPalmiQ00610.

Expressioni

Gene expression databases

BgeeiENSG00000141367.
CleanExiHS_CLTC.
ExpressionAtlasiQ00610. baseline and differential.
GenevisibleiQ00610. HS.

Organism-specific databases

HPAiCAB010389.
CAB011571.
CAB017155.
HPA059143.

Interactioni

Subunit structurei

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (PubMed:16968737). In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1 (PubMed:11532990). Interacts with DENND1A, DENND1B and DENND1C (By similarity). May interact with OCRL (By similarity). Interacts with ERBB2 (PubMed:16314522). Interacts with FKBP6 (PubMed:18529014). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions; TACC3 and CLTC are proposed to form a composite microtubule interaction surface (PubMed:21297582). Interacts with ATG16L1 (via N-terminus) (PubMed:20639872).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • clathrin light chain binding Source: FlyBase
  • disordered domain specific binding Source: CAFA
  • protein kinase binding Source: ParkinsonsUK-UCL
Complete GO annotation...

Protein-protein interaction databases

BioGridi107623. 311 interactors.
IntActiQ00610. 195 interactors.
MINTiMINT-4998595.
STRINGi9606.ENSP00000269122.

Chemistry databases

BindingDBiQ00610.

Structurei

Secondary structure

11675
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 14Combined sources9
Helixi15 – 18Combined sources4
Helixi22 – 24Combined sources3
Turni27 – 29Combined sources3
Beta strandi30 – 34Combined sources5
Beta strandi37 – 44Combined sources8
Beta strandi47 – 54Combined sources8
Beta strandi62 – 65Combined sources4
Beta strandi69 – 73Combined sources5
Beta strandi75 – 84Combined sources10
Beta strandi87 – 92Combined sources6
Turni93 – 96Combined sources4
Beta strandi97 – 103Combined sources7
Beta strandi108 – 113Combined sources6
Beta strandi115 – 133Combined sources19
Beta strandi139 – 143Combined sources5
Helixi146 – 148Combined sources3
Beta strandi152 – 158Combined sources7
Beta strandi164 – 173Combined sources10
Beta strandi176 – 185Combined sources10
Turni186 – 189Combined sources4
Beta strandi190 – 194Combined sources5
Beta strandi197 – 204Combined sources8
Beta strandi213 – 222Combined sources10
Beta strandi225 – 232Combined sources8
Beta strandi246 – 250Combined sources5
Beta strandi261 – 267Combined sources7
Turni268 – 271Combined sources4
Beta strandi272 – 277Combined sources6
Beta strandi280 – 286Combined sources7
Turni287 – 289Combined sources3
Beta strandi292 – 297Combined sources6
Beta strandi303 – 309Combined sources7
Helixi310 – 312Combined sources3
Beta strandi314 – 319Combined sources6
Beta strandi323 – 329Combined sources7
Turni331 – 333Combined sources3
Helixi334 – 340Combined sources7
Helixi345 – 354Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XZGX-ray1.70A1-364[»]
4G55X-ray1.69A1-364[»]
ProteinModelPortaliQ00610.
SMRiQ00610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati537 – 683CHCR 1PROSITE-ProRule annotation1 PublicationAdd BLAST147
Repeati686 – 828CHCR 2PROSITE-ProRule annotation1 PublicationAdd BLAST143
Repeati833 – 972CHCR 3PROSITE-ProRule annotation1 PublicationAdd BLAST140
Repeati979 – 1124CHCR 4PROSITE-ProRule annotation1 PublicationAdd BLAST146
Repeati1128 – 1269CHCR 5PROSITE-ProRule annotation1 PublicationAdd BLAST142
Repeati1274 – 1420CHCR 6PROSITE-ProRule annotation1 PublicationAdd BLAST147
Repeati1423 – 1566CHCR 7PROSITE-ProRule annotation1 PublicationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 479Globular terminal domainAdd BLAST478
Regioni24 – 67WD40-like repeat 1Add BLAST44
Regioni68 – 107WD40-like repeat 2Add BLAST40
Regioni108 – 149WD40-like repeat 3Add BLAST42
Regioni150 – 195WD40-like repeat 4Add BLAST46
Regioni196 – 257WD40-like repeat 5Add BLAST62
Regioni258 – 301WD40-like repeat 6Add BLAST44
Regioni302 – 330WD40-like repeat 7Add BLAST29
Regioni449 – 465Binding site for the uncoating ATPase, involved in lattice disassemblySequence analysisAdd BLAST17
Regioni457 – 507Involved in spindle localization and interaction with TACC31 PublicationAdd BLAST51
Regioni480 – 523Flexible linkerAdd BLAST44
Regioni524 – 1675Heavy chain armAdd BLAST1152
Regioni524 – 634Distal segmentAdd BLAST111
Regioni639 – 1675Proximal segmentAdd BLAST1037
Regioni1213 – 1522Involved in binding clathrin light chainBy similarityAdd BLAST310
Regioni1550 – 1675TrimerizationBy similarityAdd BLAST126

Domaini

The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It constitutes a major protein-protein interaction node.

Sequence similaritiesi

Belongs to the clathrin heavy chain family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0985. Eukaryota.
ENOG410XPH1. LUCA.
GeneTreeiENSGT00400000022107.
HOGENOMiHOG000188877.
HOVERGENiHBG005344.
InParanoidiQ00610.
KOiK04646.
PhylomeDBiQ00610.
TreeFamiTF300059.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
1.25.40.30. 1 hit.
InterProiView protein in InterPro
IPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR012331. Clathrin_H-chain_linker.
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.
PfamiView protein in Pfam
PF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 5 hits.
PIRSFiPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTiView protein in SMART
SM00299. CLH. 7 hits.
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEiView protein in PROSITE
PS50236. CHCR. 7 hits.

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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti560Q → R in CAA39363 (PubMed:1765375).Curated1
Sequence conflicti817G → V in CAA39363 (PubMed:1765375).Curated1
Sequence conflicti923R → H in CAE45761 (PubMed:17974005).Curated1
Sequence conflicti1563R → G in CAE45761 (PubMed:17974005).Curated1
Sequence conflicti1652Q → R in CAE45761 (PubMed:17974005).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0115701636 – 1639QPQL → NLSL in isoform 2. 1 Publication4
Alternative sequenceiVSP_0115711640 – 1675Missing in isoform 2. 1 PublicationAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q00610-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCLH1_HUMAN
AccessioniPrimary (citable) accession number: Q00610
Secondary accession number(s): D3DU00, Q6N0A0, Q86TF2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 181 of the entry and version 5 of the sequence. See 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