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Q14019

- COTL1_HUMAN

UniProt

Q14019 - COTL1_HUMAN

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Protein

Coactosin-like protein

Gene
COTL1, CLP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis.2 Publications

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. protein binding Source: IntAct

GO - Biological processi

  1. defense response to fungus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coactosin-like protein
Gene namesi
Name:COTL1
Synonyms:CLP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:18304. COTL1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Nucleus membrane; Peripheral membrane protein 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProt
  4. nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751K → A: Abolishes actin-binding activity. 1 Publication
Mutagenesisi130 – 1301K → A: No effect on 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → A: Abolishes 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → E: Abolishes 5LO-binding activity. 1 Publication
Mutagenesisi131 – 1311K → R: No effect on 5LO-binding activity. 1 Publication

Organism-specific databases

PharmGKBiPA38522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 142141Coactosin-like proteinPRO_0000214954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei126 – 1261N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ14019.
PaxDbiQ14019.
PeptideAtlasiQ14019.
PRIDEiQ14019.

2D gel databases

OGPiQ14019.
REPRODUCTION-2DPAGEIPI00017704.

PTM databases

PhosphoSiteiQ14019.

Expressioni

Tissue specificityi

Widely expressed with highest levels in placenta, lung, kidney and peripheral blood leukocytes and lower levels in brain, liver and pancreas.1 Publication

Gene expression databases

ArrayExpressiQ14019.
BgeeiQ14019.
CleanExiHS_COTL1.
GenevestigatoriQ14019.

Organism-specific databases

HPAiHPA008918.

Interactioni

Subunit structurei

Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-independent manner. Binds to F-actin with a stoichiometry of 1:2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALOX5P099174EBI-79926,EBI-79934

Protein-protein interaction databases

BioGridi116979. 8 interactions.
IntActiQ14019. 1 interaction.
STRINGi9606.ENSP00000262428.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1812
Beta strandi20 – 234
Beta strandi26 – 327
Beta strandi35 – 4410
Helixi45 – 517
Beta strandi54 – 563
Beta strandi57 – 6610
Helixi69 – 713
Beta strandi73 – 8210
Beta strandi84 – 863
Helixi88 – 10114
Turni102 – 1043
Beta strandi109 – 1146
Helixi117 – 1204
Helixi122 – 13110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2LX-ray2.80A/B2-142[»]
1T3XX-ray2.00A2-142[»]
1T3YX-ray1.15A2-142[»]
1TMWNMR-A2-142[»]
1VFQX-ray1.90A1-142[»]
1WNJNMR-A1-142[»]
ProteinModelPortaliQ14019.
SMRiQ14019. Positions 1-131.

Miscellaneous databases

EvolutionaryTraceiQ14019.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 130129ADF-HAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 7510Flexible and important for F-actin binding

Sequence similaritiesi

Contains 1 ADF-H domain.

Phylogenomic databases

eggNOGiNOG253317.
HOGENOMiHOG000007758.
HOVERGENiHBG051082.
InParanoidiQ14019.
OMAiEYANDKE.
OrthoDBiEOG7R56V4.
PhylomeDBiQ14019.
TreeFamiTF324318.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q14019-1 [UniParc]FASTAAdd to Basket

« Hide

MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ    50
QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL 100
VKEVVQNFAK EFVISDRKEL EEDFIKSELK KAGGANYDAQ TE 142
Length:142
Mass (Da):15,945
Last modified:January 23, 2007 - v3
Checksum:iA4B881DD8E89A35D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381P → H in AAH42970. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L54057 mRNA. Translation: AAA88022.1.
BT006968 mRNA. Translation: AAP35614.1.
AK315675 mRNA. Translation: BAG38040.1.
CH471114 Genomic DNA. Translation: EAW95476.1.
CH471114 Genomic DNA. Translation: EAW95477.1.
BC010039 mRNA. Translation: AAH10039.1.
BC010884 mRNA. Translation: AAH10884.1.
BC016702 mRNA. Translation: AAH16702.1.
BC042970 mRNA. Translation: AAH42970.1.
BC053682 mRNA. Translation: AAH53682.1.
CCDSiCCDS10947.1.
RefSeqiNP_066972.1. NM_021149.3.
UniGeneiHs.289092.

Genome annotation databases

EnsembliENST00000262428; ENSP00000262428; ENSG00000103187.
GeneIDi23406.
KEGGihsa:23406.
UCSCiuc002fid.3. human.

Polymorphism databases

DMDMi21759076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L54057 mRNA. Translation: AAA88022.1 .
BT006968 mRNA. Translation: AAP35614.1 .
AK315675 mRNA. Translation: BAG38040.1 .
CH471114 Genomic DNA. Translation: EAW95476.1 .
CH471114 Genomic DNA. Translation: EAW95477.1 .
BC010039 mRNA. Translation: AAH10039.1 .
BC010884 mRNA. Translation: AAH10884.1 .
BC016702 mRNA. Translation: AAH16702.1 .
BC042970 mRNA. Translation: AAH42970.1 .
BC053682 mRNA. Translation: AAH53682.1 .
CCDSi CCDS10947.1.
RefSeqi NP_066972.1. NM_021149.3.
UniGenei Hs.289092.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T2L X-ray 2.80 A/B 2-142 [» ]
1T3X X-ray 2.00 A 2-142 [» ]
1T3Y X-ray 1.15 A 2-142 [» ]
1TMW NMR - A 2-142 [» ]
1VFQ X-ray 1.90 A 1-142 [» ]
1WNJ NMR - A 1-142 [» ]
ProteinModelPortali Q14019.
SMRi Q14019. Positions 1-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116979. 8 interactions.
IntActi Q14019. 1 interaction.
STRINGi 9606.ENSP00000262428.

PTM databases

PhosphoSitei Q14019.

Polymorphism databases

DMDMi 21759076.

2D gel databases

OGPi Q14019.
REPRODUCTION-2DPAGE IPI00017704.

Proteomic databases

MaxQBi Q14019.
PaxDbi Q14019.
PeptideAtlasi Q14019.
PRIDEi Q14019.

Protocols and materials databases

DNASUi 23406.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262428 ; ENSP00000262428 ; ENSG00000103187 .
GeneIDi 23406.
KEGGi hsa:23406.
UCSCi uc002fid.3. human.

Organism-specific databases

CTDi 23406.
GeneCardsi GC16M084599.
H-InvDB HIX0134273.
HGNCi HGNC:18304. COTL1.
HPAi HPA008918.
MIMi 606748. gene.
neXtProti NX_Q14019.
PharmGKBi PA38522.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253317.
HOGENOMi HOG000007758.
HOVERGENi HBG051082.
InParanoidi Q14019.
OMAi EYANDKE.
OrthoDBi EOG7R56V4.
PhylomeDBi Q14019.
TreeFami TF324318.

Miscellaneous databases

ChiTaRSi COTL1. human.
EvolutionaryTracei Q14019.
GeneWikii COTL1.
GenomeRNAii 23406.
NextBioi 45583.
PROi Q14019.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14019.
Bgeei Q14019.
CleanExi HS_COTL1.
Genevestigatori Q14019.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
[Graphical view ]
Pfami PF00241. Cofilin_ADF. 1 hit.
[Graphical view ]
SMARTi SM00102. ADF. 1 hit.
[Graphical view ]
PROSITEi PS51263. ADF_H. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homologous recombination of a flanking repeat gene cluster is a mechanism for a common contiguous gene deletion syndrome."
    Chen K.-S., Manian P., Koeuth T., Potocki L., Zhao Q., Chinault A.C., Lee C.-C., Lupski J.R.
    Nat. Genet. 17:154-163(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain, Cervix, Kidney, Lung and Uterus.
  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 2-11.
    Tissue: Platelet.
  7. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 76-91, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75."
    Provost P., Doucet J., Stock A., Gerisch G., Samuelsson B., Radmark O.
    Biochem. J. 359:255-263(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-75.
  9. Cited for: INTERACTION WITH 5-LIPOXYGENASE, MUTAGENESIS OF LYS-130 AND LYS-131.
  10. "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-102 AND LYS-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102."
    Esser J., Rakonjac M., Hofmann B., Fischer L., Provost P., Schneider G., Steinhilber D., Samuelsson B., Radmark O.
    Biochem. J. 425:265-274(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: STRUCTURE BY NMR.
  15. "Crystal structure of human coactosin-like protein at 1.9 A resolution."
    Li X., Liu X., Lou Z., Duan X., Wu H., Liu Y., Rao Z.
    Protein Sci. 13:2845-2851(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
  16. "Binding model of human coactosin-like protein with filament actin revealed by mutagenesis."
    Dai H., Huang W., Xu J., Yao B., Xiong S., Ding H., Tang Y., Liu H., Wu J., Shi Y.
    Biochim. Biophys. Acta 1764:1688-1700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT, F-ACTIN BINDING REGION.

Entry informationi

Entry nameiCOTL1_HUMAN
AccessioniPrimary (citable) accession number: Q14019
Secondary accession number(s): B2RDU3, D3DUL9, Q86XM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 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 16
    Human chromosome 16: 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

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