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Protein

Protein humpback-2

Gene

hmp-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. alpha-catenin binding Source: WormBase
  2. cadherin binding Source: WormBase
  3. nuclear hormone receptor binding Source: GO_Central
  4. protein domain specific binding Source: WormBase
  5. protein kinase binding Source: WormBase
  6. protein phosphatase binding Source: GO_Central
  7. signal transducer activity Source: InterPro
  8. transcription coactivator activity Source: WormBase

GO - Biological processi

  1. adherens junction assembly Source: InterPro
  2. cell migration Source: WormBase
  3. cell migration involved in gastrulation Source: WormBase
  4. embryo development ending in birth or egg hatching Source: WormBase
  5. embryonic body morphogenesis Source: WormBase
  6. positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  7. regulation of actin cytoskeleton organization by cell-cell adhesion Source: WormBase
  8. regulation of cell fate specification Source: GO_Central
  9. regulation of protein localization Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_281351. TCF dependent signaling in response to WNT.
REACT_285408. formation of the beta-catenin:TCF transactivating complex.
REACT_292612. deactivation of the beta-catenin transactivating complex.
REACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_308298. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_309764. S37 mutants of beta-catenin aren't phosphorylated.
REACT_310088. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_313786. S45 mutants of beta-catenin aren't phosphorylated.
REACT_326630. VEGFR2 mediated vascular permeability.
REACT_333395. T41 mutants of beta-catenin aren't phosphorylated.
REACT_333609. Beta-catenin phosphorylation cascade.
REACT_347258. S33 mutants of beta-catenin aren't phosphorylated.
REACT_350223. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_352745. Ca2+ pathway.
SignaLinkiO44326.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein humpback-2
Gene namesi
Name:hmp-2
ORF Names:K05C4.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiK05C4.6a; CE19974; WBGene00001979; hmp-2.

Subcellular locationi

Cell junctionadherens junction 1 Publication

GO - Cellular componenti

  1. catenin complex Source: WormBase
  2. cell-cell adherens junction Source: WormBase
  3. cytoplasm Source: GO_Central
  4. nucleus Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

Worms have strong elongation defects.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 678678Protein humpback-2PRO_0000268647Add
BLAST

Proteomic databases

PaxDbiO44326.

Expressioni

Tissue specificityi

Epidermal cells.1 Publication

Developmental stagei

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

Gene expression databases

ExpressionAtlasiO44326. baseline.

Interactioni

Subunit structurei

Interacts with hmr-1. May interact with hmp-1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
hmr-1Q967F45EBI-317320,EBI-2528888

Protein-protein interaction databases

BioGridi38723. 20 interactions.
DIPiDIP-27261N.
IntActiO44326. 4 interactions.
MINTiMINT-1079247.
STRINGi6239.K05C4.6.

Structurei

3D structure databases

ProteinModelPortaliO44326.
SMRiO44326. Positions 69-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati153 – 19240ARM 1Add
BLAST
Repeati280 – 31940ARM 2Add
BLAST
Repeati320 – 35940ARM 3Add
BLAST
Repeati362 – 40342ARM 4Add
BLAST
Repeati409 – 44840ARM 5Add
BLAST

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 5 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000021706.
InParanoidiO44326.
PhylomeDBiO44326.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 1 hit.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 5 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50176. ARM_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O44326-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLHSTNSYS IFTDHEVETR TSRIRSAMFP DWIPPTSAAE ATNSTTSIVE
60 70 80 90 100
MMQMPTQQLK QSVMDLLTYE GSNDMSGLSL PDLVKLMCDH DESVVARAVH
110 120 130 140 150
RAYMLSREDP NFFNAPGFDH RSFVEALMAA SKSSNVNVRR NAIGALSHMS
160 170 180 190 200
EQRGGPLLIF RSGGLAEIIR MLYDSLESVV HYAVTTLRNL LMHVSDSRAQ
210 220 230 240 250
ARALNAVEAL TPHLHKTNPK LLAQVADGLY FLLIDDAPSK ITFLSLLGPQ
260 270 280 290 300
ILVSILREYS DHRKLIYTVV RCIRSLSVCP SNKPALISLG CLPALYVELC
310 320 330 340 350
TAKDERSQTA ILVAMRNLSD SATNEENLTQ LIIKLLEIIR VANDGMTACA
360 370 380 390 400
CGTLSNLTCN NTRNKQTVCS HGGIDALVTA IRRLPEVEEV TEPALCALRH
410 420 430 440 450
CTARHSLAEE AQSELRFCQA FPVILDQLET LRTPVIKAAL GVIRNSALLQ
460 470 480 490 500
TNLIELTQEQ TANGHTAVSL TMDILRRAIT AIEENPDIAV DGVPMWGVIE
510 520 530 540 550
GAVSALHQLA NHPAVAAACC DDIGQVGNPE CPPFLDLLHR LLAHPRLGSM
560 570 580 590 600
DDEVLEREIL GLLYQLSKRP DGARAVESTG VSALLMESRG SQYKSVVTYA
610 620 630 640 650
NGVLSNLKRG DSAAIMNMSN SYDYEMSGSA ADWQRDGLER ELFAEMYPTN
660 670
DGGHSESINM ALNNSQMRPN HNWYDTDL
Length:678
Mass (Da):74,511
Last modified:May 31, 1998 - v1
Checksum:iE6C7ED51F6241232
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016853 mRNA. Translation: AAB94552.1.
Z81564 Genomic DNA. Translation: CAB04572.1.
PIRiT23341.
RefSeqiNP_001252426.1. NM_001265497.1.
UniGeneiCel.7074.

Genome annotation databases

EnsemblMetazoaiK05C4.6a.1; K05C4.6a.1; WBGene00001979.
K05C4.6a.2; K05C4.6a.2; WBGene00001979.
GeneIDi173338.
KEGGicel:CELE_K05C4.6.
UCSCiK05C4.6. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016853 mRNA. Translation: AAB94552.1.
Z81564 Genomic DNA. Translation: CAB04572.1.
PIRiT23341.
RefSeqiNP_001252426.1. NM_001265497.1.
UniGeneiCel.7074.

3D structure databases

ProteinModelPortaliO44326.
SMRiO44326. Positions 69-604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38723. 20 interactions.
DIPiDIP-27261N.
IntActiO44326. 4 interactions.
MINTiMINT-1079247.
STRINGi6239.K05C4.6.

Proteomic databases

PaxDbiO44326.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK05C4.6a.1; K05C4.6a.1; WBGene00001979.
K05C4.6a.2; K05C4.6a.2; WBGene00001979.
GeneIDi173338.
KEGGicel:CELE_K05C4.6.
UCSCiK05C4.6. c. elegans.

Organism-specific databases

CTDi173338.
WormBaseiK05C4.6a; CE19974; WBGene00001979; hmp-2.

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000021706.
InParanoidiO44326.
PhylomeDBiO44326.

Enzyme and pathway databases

ReactomeiREACT_281351. TCF dependent signaling in response to WNT.
REACT_285408. formation of the beta-catenin:TCF transactivating complex.
REACT_292612. deactivation of the beta-catenin transactivating complex.
REACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_308298. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_309764. S37 mutants of beta-catenin aren't phosphorylated.
REACT_310088. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_313786. S45 mutants of beta-catenin aren't phosphorylated.
REACT_326630. VEGFR2 mediated vascular permeability.
REACT_333395. T41 mutants of beta-catenin aren't phosphorylated.
REACT_333609. Beta-catenin phosphorylation cascade.
REACT_347258. S33 mutants of beta-catenin aren't phosphorylated.
REACT_350223. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_352745. Ca2+ pathway.
SignaLinkiO44326.

Miscellaneous databases

NextBioi879233.
PROiO44326.

Gene expression databases

ExpressionAtlasiO44326. baseline.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 1 hit.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 5 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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(1997) [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(1999) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH HMP-1.

Entry informationi

Entry nameiHMP2_CAEEL
AccessioniPrimary (citable) accession number: O44326
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2006
Last sequence update: May 31, 1998
Last modified: March 31, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. 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.