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Protein

Beta-catenin-like protein hmp-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 (PubMed:9531567). Plays a role in recruitment of the cadherin protein hmr-1 to adherens junctions (PubMed:26412237).2 Publications

GO - Molecular functioni

  • alpha-catenin binding Source: WormBase
  • cadherin binding Source: WormBase
  • protein domain specific binding Source: WormBase
  • protein kinase binding Source: WormBase
  • signal transducer activity Source: InterPro
  • structural molecule activity Source: InterPro
  • transcription coactivator activity Source: WormBase

GO - Biological processi

  • adherens junction assembly Source: InterPro
  • cell migration Source: WormBase
  • cell migration involved in gastrulation Source: WormBase
  • desmosome assembly Source: InterPro
  • embryo development ending in birth or egg hatching Source: WormBase
  • embryonic body morphogenesis Source: WormBase
  • negative regulation of cell division Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  • regulation of actin cytoskeleton organization by cell-cell adhesion Source: WormBase
  • regulation of protein localization Source: WormBase
  • Wnt signaling pathway involved in digestive tract morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-CEL-5218920. VEGFR2 mediated vascular permeability.
SignaLinkiO44326.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-catenin-like protein hmp-2Curated
Alternative name(s):
Protein humpback-2Imported
Gene namesi
Name:hmp-2
ORF Names:K05C4.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

  • catenin complex Source: WormBase
  • cell-cell adherens junction Source: WormBase
  • nucleus Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

Worms have strong elongation defects (PubMed:9531567). RNAi-mediated knockdown results in failure of cadherin protein hmr-1 to localize to adherens junctions, but results in its accumulation along the basolateral membrane of the cell (PubMed:26412237).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi271 – 2711R → C in zu364; embryonic lethal with embryos failing to elongate and displaying a humpback phenotype in which embryos contain a dorsal hump. Localizes exclusively to the cytoplasm rather than adherens junctions. 1 Publication
Mutagenesisi599 – 5991Y → E: Phosphomimetic mutation. Initially localizes to adherens junctions, but the distribution at the junctions becomes punctate during late embryonic elongation with excursions forming orthogonal to the junctions between lateral seam cells and the dorsal and ventral neighboring cells. Defects in F-actin filament organization that include wavy and irregularly spaced filaments and the occasional aggregation of multiple bundles at single points along the adherens junction. 1 Publication
Mutagenesisi599 – 5991Y → F: Phospho-null mutation. No obvious phenotype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 678678Beta-catenin-like protein hmp-2CuratedPRO_0000268647Add
BLAST

Proteomic databases

EPDiO44326.
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

Component of a core catenin-cadherin complex consisting of hmr-1, hmp-1 and hmp-2; the complex localizes to adherens junctions (PubMed:25850673). Interacts with hmr-1; the interaction is direct (PubMed:10952315, PubMed:25850673, PubMed:26412237). May interact with hmp-1 (PubMed:11560894). Interacts with frk-1 (PubMed:20805471).5 Publications

Binary interactionsi

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

GO - Molecular functioni

  • alpha-catenin binding Source: WormBase
  • cadherin binding Source: WormBase
  • protein domain specific binding Source: WormBase
  • protein kinase binding Source: WormBase

Protein-protein interaction databases

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

Structurei

Secondary structure

1
678
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 7014Combined sources
Helixi80 – 8910Combined sources
Helixi92 – 10817Combined sources
Helixi110 – 1145Combined sources
Helixi120 – 13011Combined sources
Helixi136 – 14914Combined sources
Helixi155 – 1628Combined sources
Helixi165 – 1706Combined sources
Helixi171 – 1733Combined sources
Helixi177 – 19317Combined sources
Helixi197 – 2037Combined sources
Helixi206 – 2105Combined sources
Helixi211 – 2155Combined sources
Helixi219 – 23315Combined sources
Helixi237 – 2459Combined sources
Helixi248 – 25811Combined sources
Helixi263 – 27614Combined sources
Helixi282 – 2887Combined sources
Helixi291 – 30111Combined sources
Helixi305 – 31814Combined sources
Helixi319 – 3213Combined sources
Helixi329 – 33810Combined sources
Turni339 – 3413Combined sources
Helixi344 – 35815Combined sources
Helixi362 – 3709Combined sources
Helixi373 – 38311Combined sources
Helixi388 – 40114Combined sources
Beta strandi403 – 4053Combined sources
Helixi408 – 41710Combined sources
Helixi421 – 4288Combined sources
Helixi433 – 44614Combined sources
Helixi452 – 4587Combined sources
Helixi467 – 48418Combined sources
Helixi495 – 50915Combined sources
Helixi513 – 5219Combined sources
Helixi534 – 5429Combined sources
Helixi545 – 5484Combined sources
Helixi554 – 56613Combined sources
Helixi570 – 5778Combined sources
Turni578 – 5803Combined sources
Helixi582 – 5887Combined sources
Helixi594 – 61118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R0ZX-ray2.00A53-678[»]
4R10X-ray2.30A53-621[»]
4R11X-ray2.79A/C/E53-621[»]
ProteinModelPortaliO44326.
SMRiO44326. Positions 56-612.
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

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
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.
IPR030461. Plakoglobin/HMP-2.
[Graphical view]
PANTHERiPTHR23315:SF12. PTHR23315:SF12. 1 hit.
PfamiPF00514. Arm. 1 hit.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 8 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:June 1, 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.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R0ZX-ray2.00A53-678[»]
4R10X-ray2.30A53-621[»]
4R11X-ray2.79A/C/E53-621[»]
ProteinModelPortaliO44326.
SMRiO44326. Positions 56-612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiO44326.
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.
UCSCiK05C4.6. c. elegans.

Organism-specific databases

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

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000021706.
InParanoidiO44326.
PhylomeDBiO44326.

Enzyme and pathway databases

ReactomeiR-CEL-5218920. VEGFR2 mediated vascular permeability.
SignaLinkiO44326.

Miscellaneous databases

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.
IPR030461. Plakoglobin/HMP-2.
[Graphical view]
PANTHERiPTHR23315:SF12. PTHR23315:SF12. 1 hit.
PfamiPF00514. Arm. 1 hit.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 8 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(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.
  5. "Repression of Wnt signaling by a Fer-type nonreceptor tyrosine kinase."
    Putzke A.P., Rothman J.H.
    Proc. Natl. Acad. Sci. U.S.A. 107:16154-16159(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRK-1.
  6. "ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens Junctions."
    Tsur A., Bening Abu-Shach U., Broday L.
    Dev. Cell 35:63-77(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HMR-1, DISRUPTION PHENOTYPE.
  7. "A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo."
    Choi H.J., Loveless T., Lynch A.M., Bang I., Hardin J., Weis W.I.
    Dev. Cell 33:82-93(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 54-678 IN COMPLEX WITH HMR-1, IDENTIFICATION IN CATENIN-CADHERIN COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-271 AND TYR-599.

Entry informationi

Entry nameiHMP2_CAEEL
AccessioniPrimary (citable) accession number: O44326
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.