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Protein

C-type lectin domain family 1 member B

Gene

CLEC1B

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

Functioni

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • cell surface receptor signaling pathway Source: ProtInc
  • defense response Source: ProtInc
  • platelet activation Source: Reactome
  • platelet formation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165682-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 1 member B
Alternative name(s):
C-type lectin-like receptor 2
Short name:
CLEC-2
Gene namesi
Name:CLEC1B
Synonyms:CLEC2
ORF Names:UNQ721/PRO1384
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24356. CLEC1B.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 33CytoplasmicSequence analysisAdd BLAST33
Transmembranei34 – 54Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini55 – 229ExtracellularSequence analysisAdd BLAST175

GO - Cellular componenti

  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150K → A: Substantial reduction in rhodocytin binding. 1 Publication1
Mutagenesisi171K → A: Significant reduction in rhodocytin binding. 1 Publication1
Mutagenesisi184E → A: Significant reduction in rhodocytin binding. 1 Publication1
Mutagenesisi187E → A: Significant reduction in rhodocytin binding. 1 Publication1
Mutagenesisi188D → A: Significant reduction in rhodocytin binding. 1 Publication1
Mutagenesisi190K → A: Significant reduction in rhodocytin binding. 1 Publication1
Mutagenesisi192N → A: Significant reduction in rhodocytin binding. 1 Publication1

Organism-specific databases

DisGeNETi51266.
OpenTargetsiENSG00000165682.
PharmGKBiPA142672098.

Polymorphism and mutation databases

BioMutaiCLEC1B.
DMDMi134035066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002800431 – 229C-type lectin domain family 1 member BAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphotyrosine1 Publication1
Glycosylationi68N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi102 ↔ 113PROSITE-ProRule annotation1 Publication
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi130 ↔ 216PROSITE-ProRule annotation1 Publication
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi195 ↔ 208PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Glycosylated.1 Publication
Phosphorylated on tyrosine residue in response to rhodocytin binding.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9P126.
PeptideAtlasiQ9P126.
PRIDEiQ9P126.

PTM databases

iPTMnetiQ9P126.
PhosphoSitePlusiQ9P126.

Expressioni

Tissue specificityi

Expressed preferentially in the liver. Also expressed in immune cells of myeloid origin and on the surface of platelets.3 Publications

Gene expression databases

BgeeiENSG00000165682.
CleanExiHS_CLEC1B.
ExpressionAtlasiQ9P126. baseline and differential.
GenevisibleiQ9P126. HS.

Interactioni

Subunit structurei

Homodimer. Interacts (via cytoplasmic domain) with RACK1; promotes CLEC1B ubiquitination and proteasome-mediated degradation. Interacts (dimer) with SYK (via SH2 domains).4 Publications

Protein-protein interaction databases

BioGridi119420. 1 interactor.
DIPiDIP-61332N.
IntActiQ9P126. 1 interactor.
MINTiMINT-1453946.
STRINGi9606.ENSP00000298527.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi106 – 109Combined sources4
Beta strandi112 – 121Combined sources10
Helixi123 – 132Combined sources10
Helixi143 – 150Combined sources8
Beta strandi157 – 162Combined sources6
Helixi180 – 185Combined sources6
Beta strandi195 – 199Combined sources5
Beta strandi202 – 206Combined sources5
Beta strandi212 – 219Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C6UX-ray1.60A100-221[»]
3WSRX-ray1.91A/B96-221[»]
3WWKX-ray2.98C/F/I/L96-221[»]
ProteinModelPortaliQ9P126.
SMRiQ9P126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P126.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 217C-type lectinPROSITE-ProRule annotationAdd BLAST109

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000111777.
HOVERGENiHBG094936.
InParanoidiQ9P126.
KOiK10070.
OMAiKGHKCSP.
OrthoDBiEOG091G0OAQ.
PhylomeDBiQ9P126.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P126-1) [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
MQDEDGYITL NIKTRKPALI SVGSASSSWW RVMALILLIL CVGMVVGLVA
60 70 80 90 100
LGIWSVMQRN YLQGENENRT GTLQQLAKRF CQYVVKQSEL KGTFKGHKCS
110 120 130 140 150
PCDTNWRYYG DSCYGFFRHN LTWEESKQYC TDMNATLLKI DNRNIVEYIK
160 170 180 190 200
ARTHLIRWVG LSRQKSNEVW KWEDGSVISE NMFEFLEDGK GNMNCAYFHN
210 220
GKMHPTFCEN KHYLMCERKA GMTKVDQLP
Length:229
Mass (Da):26,596
Last modified:March 6, 2007 - v2
Checksum:iB39BF202AAE6DDD9
GO
Isoform 2 (identifier: Q9P126-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-55: VGSASSSWWRVMALILLILCVGMVVGLVALGIWS → A

Show »
Length:196
Mass (Da):23,096
Checksum:i0BFA3D427640C3F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41C → Y in AAF36777 (PubMed:10671229).Curated1
Sequence conflicti41C → Y (PubMed:16940507).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03104720I → V.4 PublicationsCorresponds to variant rs612593dbSNPEnsembl.1
Natural variantiVAR_03104824S → P.1 PublicationCorresponds to variant rs2273986dbSNPEnsembl.1
Natural variantiVAR_03104928S → F.Corresponds to variant rs2273987dbSNPEnsembl.1
Natural variantiVAR_03105064G → D.4 PublicationsCorresponds to variant rs583903dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02351522 – 55VGSAS…LGIWS → A in isoform 2. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124841 mRNA. Translation: AAF36777.1.
AY358599 mRNA. Translation: AAQ88962.1.
AC091814 Genomic DNA. No translation available.
BC029554 mRNA. Translation: AAH29554.1.
CCDSiCCDS41751.1. [Q9P126-2]
CCDS41752.1. [Q9P126-1]
RefSeqiNP_001092901.1. NM_001099431.1. [Q9P126-2]
NP_057593.3. NM_016509.3. [Q9P126-1]
XP_005253439.1. XM_005253382.4. [Q9P126-1]
XP_011518987.1. XM_011520685.2. [Q9P126-2]
XP_016874884.1. XM_017019395.1. [Q9P126-1]
UniGeneiHs.409794.

Genome annotation databases

EnsembliENST00000298527; ENSP00000298527; ENSG00000165682. [Q9P126-1]
ENST00000348658; ENSP00000327169; ENSG00000165682. [Q9P126-2]
ENST00000428126; ENSP00000406338; ENSG00000165682. [Q9P126-2]
GeneIDi51266.
KEGGihsa:51266.
UCSCiuc001qwu.5. human. [Q9P126-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

CLEC-2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124841 mRNA. Translation: AAF36777.1.
AY358599 mRNA. Translation: AAQ88962.1.
AC091814 Genomic DNA. No translation available.
BC029554 mRNA. Translation: AAH29554.1.
CCDSiCCDS41751.1. [Q9P126-2]
CCDS41752.1. [Q9P126-1]
RefSeqiNP_001092901.1. NM_001099431.1. [Q9P126-2]
NP_057593.3. NM_016509.3. [Q9P126-1]
XP_005253439.1. XM_005253382.4. [Q9P126-1]
XP_011518987.1. XM_011520685.2. [Q9P126-2]
XP_016874884.1. XM_017019395.1. [Q9P126-1]
UniGeneiHs.409794.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C6UX-ray1.60A100-221[»]
3WSRX-ray1.91A/B96-221[»]
3WWKX-ray2.98C/F/I/L96-221[»]
ProteinModelPortaliQ9P126.
SMRiQ9P126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119420. 1 interactor.
DIPiDIP-61332N.
IntActiQ9P126. 1 interactor.
MINTiMINT-1453946.
STRINGi9606.ENSP00000298527.

PTM databases

iPTMnetiQ9P126.
PhosphoSitePlusiQ9P126.

Polymorphism and mutation databases

BioMutaiCLEC1B.
DMDMi134035066.

Proteomic databases

PaxDbiQ9P126.
PeptideAtlasiQ9P126.
PRIDEiQ9P126.

Protocols and materials databases

DNASUi51266.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298527; ENSP00000298527; ENSG00000165682. [Q9P126-1]
ENST00000348658; ENSP00000327169; ENSG00000165682. [Q9P126-2]
ENST00000428126; ENSP00000406338; ENSG00000165682. [Q9P126-2]
GeneIDi51266.
KEGGihsa:51266.
UCSCiuc001qwu.5. human. [Q9P126-1]

Organism-specific databases

CTDi51266.
DisGeNETi51266.
GeneCardsiCLEC1B.
HGNCiHGNC:24356. CLEC1B.
MIMi606783. gene.
neXtProtiNX_Q9P126.
OpenTargetsiENSG00000165682.
PharmGKBiPA142672098.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000111777.
HOVERGENiHBG094936.
InParanoidiQ9P126.
KOiK10070.
OMAiKGHKCSP.
OrthoDBiEOG091G0OAQ.
PhylomeDBiQ9P126.
TreeFamiTF336674.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165682-MONOMER.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.

Miscellaneous databases

EvolutionaryTraceiQ9P126.
GeneWikiiCLEC1B.
GenomeRNAii51266.
PROiQ9P126.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165682.
CleanExiHS_CLEC1B.
ExpressionAtlasiQ9P126. baseline and differential.
GenevisibleiQ9P126. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLC1B_HUMAN
AccessioniPrimary (citable) accession number: Q9P126
Secondary accession number(s): Q6UWX7, Q8NHR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: November 30, 2016
This is version 114 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

Miscellaneous

Acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (Syk) and initiation of downstream tyrosine phosphorylation events and activation of PLC-gamma-2 (PubMed:16174766). Acts as an attachment factor for human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets (PubMed:16940507).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.