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O44326 (HMP2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein humpback-2
Gene names
Name:hmp-2
ORF Names:K05C4.6
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length678 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cell migration during body enclosure and cell shape changes during body elongation. Ref.1

Subunit structure

Interacts with hmr-1. May interact with hmp-1. Ref.3 Ref.4

Subcellular location

Cell junctionadherens junction Ref.1.

Tissue specificity

Epidermal cells. Ref.1

Developmental stage

Present in all embryonic blastomeres at early stages of development (at protein level). Ref.1

Disruption phenotype

Worms have strong elongation defects. Ref.1

Sequence similarities

Belongs to the beta-catenin family.

Contains 5 ARM repeats.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
   DomainRepeat
   Molecular functionDevelopmental protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from mutant phenotype Ref.1. Source: WormBase

cell migration involved in gastrulation

Inferred from genetic interaction PubMed 20515680. Source: WormBase

cell morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryo development ending in birth or egg hatching

Inferred from mutant phenotype Ref.1. Source: WormBase

embryonic body morphogenesis

Inferred from mutant phenotype Ref.1. Source: WormBase

morphogenesis of embryonic epithelium

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

nervous system development

Inferred from Biological aspect of Ancestor. Source: RefGenome

oocyte development

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4. Source: WormBase

regulation of actin cytoskeleton organization by cell-cell adhesion

Inferred from mutant phenotype Ref.1. Source: WormBase

regulation of protein localization

Inferred from mutant phenotype PubMed 15958510. Source: WormBase

   Cellular_componentZ disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

basolateral plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

catenin complex

Inferred from physical interaction Ref.3. Source: WormBase

cell-cell adherens junction

Inferred from direct assay PubMed 21575624Ref.1. Source: WormBase

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

desmosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 21575624. Source: WormBase

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

zonula adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-catenin binding

Inferred from physical interaction Ref.4. Source: WormBase

cadherin binding

Inferred from physical interaction Ref.3PubMed 12847081. Source: WormBase

protein domain specific binding

Inferred from physical interaction PubMed 19551147. Source: WormBase

protein kinase binding

Inferred from physical interaction PubMed 15958510. Source: WormBase

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from direct assay Ref.4. Source: WormBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hmr-1Q967F45EBI-317320,EBI-2528888

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 678678Protein humpback-2
PRO_0000268647

Regions

Repeat153 – 19240ARM 1
Repeat280 – 31940ARM 2
Repeat320 – 35940ARM 3
Repeat362 – 40342ARM 4
Repeat409 – 44840ARM 5

Sequences

Sequence LengthMass (Da)Tools
O44326 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E6C7ED51F6241232

FASTA67874,511
        10         20         30         40         50         60 
MLLHSTNSYS IFTDHEVETR TSRIRSAMFP DWIPPTSAAE ATNSTTSIVE MMQMPTQQLK 

        70         80         90        100        110        120 
QSVMDLLTYE GSNDMSGLSL PDLVKLMCDH DESVVARAVH RAYMLSREDP NFFNAPGFDH 

       130        140        150        160        170        180 
RSFVEALMAA SKSSNVNVRR NAIGALSHMS EQRGGPLLIF RSGGLAEIIR MLYDSLESVV 

       190        200        210        220        230        240 
HYAVTTLRNL LMHVSDSRAQ ARALNAVEAL TPHLHKTNPK LLAQVADGLY FLLIDDAPSK 

       250        260        270        280        290        300 
ITFLSLLGPQ ILVSILREYS DHRKLIYTVV RCIRSLSVCP SNKPALISLG CLPALYVELC 

       310        320        330        340        350        360 
TAKDERSQTA ILVAMRNLSD SATNEENLTQ LIIKLLEIIR VANDGMTACA CGTLSNLTCN 

       370        380        390        400        410        420 
NTRNKQTVCS HGGIDALVTA IRRLPEVEEV TEPALCALRH CTARHSLAEE AQSELRFCQA 

       430        440        450        460        470        480 
FPVILDQLET LRTPVIKAAL GVIRNSALLQ TNLIELTQEQ TANGHTAVSL TMDILRRAIT 

       490        500        510        520        530        540 
AIEENPDIAV DGVPMWGVIE GAVSALHQLA NHPAVAAACC DDIGQVGNPE CPPFLDLLHR 

       550        560        570        580        590        600 
LLAHPRLGSM DDEVLEREIL GLLYQLSKRP DGARAVESTG VSALLMESRG SQYKSVVTYA 

       610        620        630        640        650        660 
NGVLSNLKRG DSAAIMNMSN SYDYEMSGSA ADWQRDGLER ELFAEMYPTN DGGHSESINM 

       670 
ALNNSQMRPN HNWYDTDL 

« Hide

References

« Hide 'large scale' references
[1]"A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo."
Costa M., Raich W., Agbunag C., Leung B., Hardin J., Priess J.R.
J. Cell Biol. 141:297-308(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Distinct beta-catenins mediate adhesion and signalling functions in C. elegans."
Korswagen H.C., Herman M.A., Clevers H.C.
Nature 406:527-532(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HMR-1.
[4]"The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1 and HMP-2 make distinct protein interactions but retain functional redundancy in vivo."
Natarajan L., Witwer N.E., Eisenmann D.M.
Genetics 159:159-172(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH HMP-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF016853 mRNA. Translation: AAB94552.1.
Z81564 Genomic DNA. Translation: CAB04572.1.
PIRT23341.
RefSeqNP_001252426.1. NM_001265497.1.
UniGeneCel.7074.

3D structure databases

ProteinModelPortalO44326.
SMRO44326. Positions 69-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid38723. 19 interactions.
DIPDIP-27261N.
IntActO44326. 4 interactions.
MINTMINT-1079247.
STRING6239.K05C4.6.

Proteomic databases

PaxDbO44326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaK05C4.6a.1; K05C4.6a.1; K05C4.6.
K05C4.6a.2; K05C4.6a.2; K05C4.6.
K05C4.6a.3; K05C4.6a.3; K05C4.6.
GeneID173338.
KEGGcel:CELE_K05C4.6.
UCSCK05C4.6. c. elegans.

Organism-specific databases

CTD173338.
WormBaseK05C4.6a; CE19974; WBGene00001979; hmp-2.

Phylogenomic databases

eggNOGNOG297695.
HOGENOMHOG000021706.
InParanoidO44326.
PhylomeDBO44326.

Enzyme and pathway databases

SignaLinkO44326.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 1 hit.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 5 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio879233.
PROO44326.

Entry information

Entry nameHMP2_CAEEL
AccessionPrimary (citable) accession number: O44326
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase