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Protein

Clathrin heavy chain 2

Gene

CLTCL1

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 (By similarity).By similarity

GO - Molecular functioni

  • signal transducer activity Source: ProtInc
  • structural molecule activity Source: InterPro

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • intracellular protein transport Source: InterPro
  • mitotic nuclear division Source: UniProtKB
  • positive regulation of glucose import Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB
  • signal transduction Source: GOC
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_264198. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 2
Alternative name(s):
Clathrin heavy chain on chromosome 22
Short name:
CLH-22
Gene namesi
Name:CLTCL1
Synonyms:CLH22, CLTCL, CLTD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2093. CLTCL1.

Subcellular locationi

GO - Cellular componenti

  • clathrin-coated vesicle Source: UniProtKB
  • clathrin coat of coated pit Source: InterPro
  • clathrin coat of trans-Golgi network vesicle Source: InterPro
  • coated pit Source: UniProtKB
  • coated vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • spindle Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26619.

Polymorphism and mutation databases

BioMutaiCLTCL1.
DMDMi2506298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 16401639Clathrin heavy chain 2PRO_0000205786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei184 – 1841PhosphotyrosineBy similarity
Modified residuei394 – 3941PhosphothreonineBy similarity
Modified residuei634 – 6341PhosphotyrosineBy similarity
Modified residuei737 – 7371N6-succinyllysineBy similarity
Modified residuei856 – 8561N6-acetyllysineBy similarity
Modified residuei899 – 8991PhosphotyrosineBy similarity
Modified residuei1206 – 12061PhosphotyrosineBy similarity
Modified residuei1441 – 14411N6-acetyllysine; alternateBy similarity
Modified residuei1441 – 14411N6-succinyllysine; alternateBy similarity
Modified residuei1477 – 14771PhosphotyrosineBy similarity
Modified residuei1487 – 14871PhosphotyrosineBy similarity
Modified residuei1494 – 14941PhosphoserineBy similarity
Modified residuei1501 – 15011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53675.
PaxDbiP53675.
PRIDEiP53675.

PTM databases

PhosphoSiteiP53675.

Expressioni

Tissue specificityi

Maximal levels in skeletal muscle. High levels in heart and testis. Low expression detected in all other tissues.

Gene expression databases

BgeeiP53675.
CleanExiHS_CLTCL1.
ExpressionAtlasiP53675. baseline and differential.
GenevestigatoriP53675.

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 (By similarity). May interact with OCRL (By similarity).By similarity

Protein-protein interaction databases

BioGridi113854. 33 interactions.
IntActiP53675. 9 interactions.
MINTiMINT-208273.
STRINGi9606.ENSP00000263200.

Structurei

3D structure databases

ProteinModelPortaliP53675.
SMRiP53675. Positions 1-493, 1077-1628.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati537 – 683147CHCR 1Add
BLAST
Repeati686 – 828143CHCR 2Add
BLAST
Repeati833 – 972140CHCR 3Add
BLAST
Repeati979 – 1124146CHCR 4Add
BLAST
Repeati1128 – 1269142CHCR 5Add
BLAST
Repeati1274 – 1420147CHCR 6Add
BLAST
Repeati1423 – 1566144CHCR 7Add
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 – 16401117Heavy chain armAdd
BLAST
Regioni524 – 634111Distal segmentAdd
BLAST
Regioni639 – 16401002Proximal segmentAdd
BLAST
Regioni1213 – 1522310Involved in binding clathrin light chainBy similarityAdd
BLAST
Regioni1551 – 164090TrimerizationBy similarityAdd
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).By similarity

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.
InParanoidiP53675.
KOiK04646.
OMAiYYQXVAN.
OrthoDBiEOG7Z0JVM.
PhylomeDBiP53675.
TreeFamiTF300059.

Family and domain databases

Gene3Di1.25.40.10. 3 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. 2 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. AlignAdd to basket

Isoform 1 (identifier: P53675-1) [UniParc]FASTAAdd to basket

Also known as: Long, Brain

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
MAQILPVRFQ EHFQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV
60 70 80 90 100
TIIDMSDPMA PIRRPISAES AIMNPASKVI ALKAGKTLQI FNIEMKSKMK
110 120 130 140 150
AHTMAEEVIF WKWVSVNTVA LVTETAVYHW SMEGDSQPMK MFDRHTSLVG
160 170 180 190 200
CQVIHYRTDE YQKWLLLVGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAA
210 220 230 240 250
FAEFKMEGNA KPATLFCFAV RNPTGGKLHI IEVGQPAAGN QPFVKKAVDV
260 270 280 290 300
FFPPEAQNDF PVAMQIGAKH GVIYLITKYG YLHLYDLESG VCICMNRISA
310 320 330 340 350
DTIFVTAPHK PTSGIIGVNK KGQVLSVCVE EDNIVNYATN VLQNPDLGLR
360 370 380 390 400
LAVRSNLAGA EKLFVRKFNT LFAQGSYAEA AKVAASAPKG ILRTRETVQK
410 420 430 440 450
FQSIPAQSGQ ASPLLQYFGI LLDQGQLNKL ESLELCHLVL QQGRKQLLEK
460 470 480 490 500
WLKEDKLECS EELGDLVKTT DPMLALSVYL RANVPSKVIQ CFAETGQFQK
510 520 530 540 550
IVLYAKKVGY TPDWIFLLRG VMKISPEQGL QFSRMLVQDE EPLANISQIV
560 570 580 590 600
DIFMENSLIQ QCTSFLLDAL KNNRPAEGLL QTWLLEMNLV HAPQVADAIL
610 620 630 640 650
GNKMFTHYDR AHIAQLCEKA GLLQQALEHY TDLYDIKRAV VHTHLLNPEW
660 670 680 690 700
LVNFFGSLSV EDSVECLHAM LSANIRQNLQ LCVQVASKYH EQLGTQALVE
710 720 730 740 750
LFESFKSYKG LFYFLGSIVN FSQDPDVHLK YIQAACKTGQ IKEVERICRE
760 770 780 790 800
SSCYNPERVK NFLKEAKLTD QLPLIIVCDR FGFVHDLVLY LYRNNLQRYI
810 820 830 840 850
EIYVQKVNPS RTPAVIGGLL DVDCSEEVIK HLIMAVRGQF STDELVAEVE
860 870 880 890 900
KRNRLKLLLP WLESQIQEGC EEPATHNALA KIYIDSNNSP ECFLRENAYY
910 920 930 940 950
DSSVVGRYCE KRDPHLACVA YERGQCDLEL IKVCNENSLF KSEARYLVCR
960 970 980 990 1000
KDPELWAHVL EETNPSRRQL IDQVVQTALS ETRDPEEISV TVKAFMTADL
1010 1020 1030 1040 1050
PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYISRLDNY
1060 1070 1080 1090 1100
DALDIASIAV SSALYEEAFT VFHKFDMNAS AIQVLIEHIG NLDRAYEFAE
1110 1120 1130 1140 1150
RCNEPAVWSQ LAQAQLQKDL VKEAINSYIR GDDPSSYLEV VQSASRSNNW
1160 1170 1180 1190 1200
EDLVKFLQMA RKKGRESYIE TELIFALAKT SRVSELEDFI NGPNNAHIQQ
1210 1220 1230 1240 1250
VGDRCYEEGM YEAAKLLYSN VSNFARLAST LVHLGEYQAA VDNSRKASST
1260 1270 1280 1290 1300
RTWKEVCFAC MDGQEFRFAQ LCGLHIVIHA DELEELMCYY QDRGYFEELI
1310 1320 1330 1340 1350
LLLEAALGLE RAHMGMFTEL AILYSKFKPQ KMLEHLELFW SRVNIPKVLR
1360 1370 1380 1390 1400
AAEQAHLWAE LVFLYDKYEE YDNAVLTMMS HPTEAWKEGQ FKDIITKVAN
1410 1420 1430 1440 1450
VELCYRALQF YLDYKPLLIN DLLLVLSPRL DHTWTVSFFS KAGQLPLVKP
1460 1470 1480 1490 1500
YLRSVQSHNN KSVNEALNHL LTEEEDYQGL RASIDAYDNF DNISLAQQLE
1510 1520 1530 1540 1550
KHQLMEFRCI AAYLYKGNNW WAQSVELCKK DHLYKDAMQH AAESRDAELA
1560 1570 1580 1590 1600
QKLLQWFLEE GKRECFAACL FTCYDLLRPD MVLELAWRHN LVDLAMPYFI
1610 1620 1630 1640
QVMREYLSKV DKLDALESLR KQEEHVTEPA PLVFDFDGHE
Length:1,640
Mass (Da):187,030
Last modified:November 1, 1997 - v2
Checksum:iC661E1AB989D8E7F
GO
Isoform 2 (identifier: P53675-2) [UniParc]FASTAAdd to basket

Also known as: Short, Muscle

The sequence of this isoform differs from the canonical sequence as follows:
     1479-1535: Missing.

Show »
Length:1,583
Mass (Da):180,296
Checksum:i5DB1E3D4A77607D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931P → H in AAC50494 (PubMed:8733128).Curated
Sequence conflicti215 – 2151L → H in AAC50494 (PubMed:8733128).Curated
Sequence conflicti320 – 3201K → T in CAA64752 (PubMed:8733129).Curated
Sequence conflicti530 – 5301L → Q in AAC50494 (PubMed:8733128).Curated
Sequence conflicti1474 – 14741E → K in AAB40908 (PubMed:8844170).Curated
Sequence conflicti1474 – 14741E → K in AAB40909 (PubMed:8844170).Curated
Sequence conflicti1620 – 164021RKQEE…FDGHE → PPSKRSM in AAB40908 (PubMed:8844170).CuratedAdd
BLAST
Sequence conflicti1620 – 164021RKQEE…FDGHE → PPSKRSM in AAB40909 (PubMed:8844170).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611P → L.
Corresponds to variant rs3747059 [ dbSNP | Ensembl ].
VAR_055653
Natural varianti205 – 2051K → R.
Corresponds to variant rs5746697 [ dbSNP | Ensembl ].
VAR_055654
Natural varianti279 – 2791Y → C.
Corresponds to variant rs807459 [ dbSNP | Ensembl ].
VAR_055655
Natural varianti691 – 6911E → K.1 Publication
Corresponds to variant rs1060374 [ dbSNP | Ensembl ].
VAR_055656
Natural varianti941 – 9411K → R.
Corresponds to variant rs35398725 [ dbSNP | Ensembl ].
VAR_055657
Natural varianti945 – 9451R → H.
Corresponds to variant rs36077768 [ dbSNP | Ensembl ].
VAR_055658
Natural varianti1046 – 10461R → C.
Corresponds to variant rs712952 [ dbSNP | Ensembl ].
VAR_055659
Natural varianti1195 – 11951N → S.
Corresponds to variant rs807547 [ dbSNP | Ensembl ].
VAR_059214
Natural varianti1316 – 13161M → V.
Corresponds to variant rs1061325 [ dbSNP | Ensembl ].
VAR_059215
Natural varianti1394 – 13941I → T.
Corresponds to variant rs1633399 [ dbSNP | Ensembl ].
VAR_059216
Natural varianti1592 – 15921V → M.
Corresponds to variant rs2073738 [ dbSNP | Ensembl ].
VAR_059217
Natural varianti1620 – 16201R → H.
Corresponds to variant rs5748024 [ dbSNP | Ensembl ].
VAR_059218

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1479 – 153557Missing in isoform 2. 3 PublicationsVSP_001100Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41763 mRNA. Translation: AAC50494.1.
X95486 mRNA. Translation: CAA64752.1.
X95487 mRNA. Translation: CAA64753.1.
U60802 mRNA. Translation: AAB40908.1.
U60803 mRNA. Translation: AAB40909.1.
AK302506 mRNA. Translation: BAH13731.1.
CH471176 Genomic DNA. Translation: EAX03047.1.
CCDSiCCDS46662.2. [P53675-1]
CCDS54497.2. [P53675-2]
PIRiG02757.
T09522.
RefSeqiNP_001826.3. NM_001835.3. [P53675-2]
NP_009029.3. NM_007098.3. [P53675-1]
UniGeneiHs.368266.

Genome annotation databases

EnsembliENST00000427926; ENSP00000441158; ENSG00000070371. [P53675-1]
ENST00000621271; ENSP00000485020; ENSG00000070371. [P53675-2]
GeneIDi8218.
KEGGihsa:8218.
UCSCiuc011agw.1. human. [P53675-1]
uc021wld.1. human. [P53675-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41763 mRNA. Translation: AAC50494.1.
X95486 mRNA. Translation: CAA64752.1.
X95487 mRNA. Translation: CAA64753.1.
U60802 mRNA. Translation: AAB40908.1.
U60803 mRNA. Translation: AAB40909.1.
AK302506 mRNA. Translation: BAH13731.1.
CH471176 Genomic DNA. Translation: EAX03047.1.
CCDSiCCDS46662.2. [P53675-1]
CCDS54497.2. [P53675-2]
PIRiG02757.
T09522.
RefSeqiNP_001826.3. NM_001835.3. [P53675-2]
NP_009029.3. NM_007098.3. [P53675-1]
UniGeneiHs.368266.

3D structure databases

ProteinModelPortaliP53675.
SMRiP53675. Positions 1-493, 1077-1628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113854. 33 interactions.
IntActiP53675. 9 interactions.
MINTiMINT-208273.
STRINGi9606.ENSP00000263200.

PTM databases

PhosphoSiteiP53675.

Polymorphism and mutation databases

BioMutaiCLTCL1.
DMDMi2506298.

Proteomic databases

MaxQBiP53675.
PaxDbiP53675.
PRIDEiP53675.

Protocols and materials databases

DNASUi8218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000427926; ENSP00000441158; ENSG00000070371. [P53675-1]
ENST00000621271; ENSP00000485020; ENSG00000070371. [P53675-2]
GeneIDi8218.
KEGGihsa:8218.
UCSCiuc011agw.1. human. [P53675-1]
uc021wld.1. human. [P53675-2]

Organism-specific databases

CTDi8218.
GeneCardsiGC22M019171.
H-InvDBHIX0016234.
HGNCiHGNC:2093. CLTCL1.
MIMi601273. gene.
neXtProtiNX_P53675.
PharmGKBiPA26619.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314149.
GeneTreeiENSGT00400000022107.
HOGENOMiHOG000188877.
HOVERGENiHBG005344.
InParanoidiP53675.
KOiK04646.
OMAiYYQXVAN.
OrthoDBiEOG7Z0JVM.
PhylomeDBiP53675.
TreeFamiTF300059.

Enzyme and pathway databases

ReactomeiREACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_264198. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSiCLTCL1. human.
GenomeRNAii8218.
NextBioi30943.
PROiP53675.
SOURCEiSearch...

Gene expression databases

BgeeiP53675.
CleanExiHS_CLTCL1.
ExpressionAtlasiP53675. baseline and differential.
GenevestigatoriP53675.

Family and domain databases

Gene3Di1.25.40.10. 3 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. 2 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a new clathrin heavy chain gene with muscle-specific expression from the region commonly deleted in velo-cardio-facial syndrome."
    Sirotkin H., Morrow B., Dasgupta R., Goldberg R., Patangali S.R., Shi G., Cannizzaro L., Shprintzen R., Weissman S., Kucherlapati R.
    Hum. Mol. Genet. 5:617-624(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11."
    Kedra D., Peyrard M., Fransson I., Collins J.E., Dunham I., Roe B.A., Dumanski J.P.
    Hum. Mol. Genet. 5:625-631(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1640 (ISOFORM 2).
    Tissue: Fetal brain and Skeletal muscle.
  3. "Cloning and characterization of a novel human clathrin heavy chain gene (CLTCL)."
    Long K.R., Trofatter J.A., Ramesh V., McCormick M.K., Buckler A.J.
    Genomics 35:466-472(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT LYS-691.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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.

Entry informationi

Entry nameiCLH2_HUMAN
AccessioniPrimary (citable) accession number: P53675
Secondary accession number(s): B7Z7U5
, Q14017, Q15808, Q15809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: May 27, 2015
This is version 140 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.