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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
  • protein phosphatase binding Source: GO_Central
  • 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
  • establishment of mitotic spindle orientation Source: UniProtKB
  • left/right axis specification Source: UniProtKB
  • 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.
R-CEL-6798695. Neutrophil degranulation.
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
  • cytoplasm Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi271R → 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 Publication1
Mutagenesisi599Y → 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 Publication1
Mutagenesisi599Y → F: Phospho-null mutation. No obvious phenotype. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002686471 – 678Beta-catenin-like protein hmp-2CuratedAdd BLAST678

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

BgeeiWBGene00001979.
ExpressionAtlasiO44326. differential.

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 phosphatase binding Source: GO_Central

Protein-protein interaction databases

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

Structurei

Secondary structure

1678
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi57 – 70Combined sources14
Helixi80 – 89Combined sources10
Helixi92 – 108Combined sources17
Helixi110 – 114Combined sources5
Helixi120 – 130Combined sources11
Helixi136 – 149Combined sources14
Helixi155 – 162Combined sources8
Helixi165 – 170Combined sources6
Helixi171 – 173Combined sources3
Helixi177 – 193Combined sources17
Helixi197 – 203Combined sources7
Helixi206 – 210Combined sources5
Helixi211 – 215Combined sources5
Helixi219 – 233Combined sources15
Helixi237 – 245Combined sources9
Helixi248 – 258Combined sources11
Helixi263 – 276Combined sources14
Helixi282 – 288Combined sources7
Helixi291 – 301Combined sources11
Helixi305 – 318Combined sources14
Helixi319 – 321Combined sources3
Helixi329 – 338Combined sources10
Turni339 – 341Combined sources3
Helixi344 – 358Combined sources15
Helixi362 – 370Combined sources9
Helixi373 – 383Combined sources11
Helixi388 – 401Combined sources14
Beta strandi403 – 405Combined sources3
Helixi408 – 417Combined sources10
Helixi421 – 428Combined sources8
Helixi433 – 446Combined sources14
Helixi452 – 458Combined sources7
Helixi467 – 484Combined sources18
Helixi495 – 509Combined sources15
Helixi513 – 521Combined sources9
Helixi534 – 542Combined sources9
Helixi545 – 548Combined sources4
Helixi554 – 566Combined sources13
Helixi570 – 577Combined sources8
Turni578 – 580Combined sources3
Helixi582 – 588Combined sources7
Helixi594 – 611Combined sources18

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati153 – 192ARM 1Add BLAST40
Repeati280 – 319ARM 2Add BLAST40
Repeati320 – 359ARM 3Add BLAST40
Repeati362 – 403ARM 4Add BLAST42
Repeati409 – 448ARM 5Add BLAST40

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R0ZX-ray2.00A53-678[»]
4R10X-ray2.30A53-621[»]
4R11X-ray2.79A/C/E53-621[»]
ProteinModelPortaliO44326.
SMRiO44326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38723. 20 interactors.
DIPiDIP-27261N.
IntActiO44326. 4 interactors.
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.
R-CEL-6798695. Neutrophil degranulation.
SignaLinkiO44326.

Miscellaneous databases

PROiO44326.

Gene expression databases

BgeeiWBGene00001979.
ExpressionAtlasiO44326. differential.

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...

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: November 30, 2016
This is version 140 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.