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O44326

- HMP2_CAEEL

UniProt

O44326 - HMP2_CAEEL

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Protein

Protein humpback-2

Gene

hmp-2

Organism
Caenorhabditis elegans
Status
Reviewed - 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. protein domain specific binding Source: WormBase
  4. protein kinase binding Source: WormBase
  5. structural molecule activity Source: RefGenome
  6. transcription coactivator activity Source: WormBase

GO - Biological processi

  1. cell migration Source: WormBase
  2. cell migration involved in gastrulation Source: WormBase
  3. cell morphogenesis Source: RefGenome
  4. cytoskeletal anchoring at plasma membrane Source: RefGenome
  5. embryo development ending in birth or egg hatching Source: WormBase
  6. embryonic body morphogenesis Source: WormBase
  7. morphogenesis of embryonic epithelium Source: RefGenome
  8. negative regulation of heart induction by canonical Wnt signaling pathway Source: RefGenome
  9. negative regulation of transcription from RNA polymerase II promoter Source: RefGenome
  10. nervous system development Source: RefGenome
  11. oocyte development Source: RefGenome
  12. positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  13. regulation of actin cytoskeleton organization by cell-cell adhesion Source: WormBase
  14. regulation of protein localization Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_184336. Ca2+ pathway.
REACT_229949. deactivation of the beta-catenin transactivating complex.
REACT_232673. VEGFR2 mediated vascular permeability.
REACT_239816. CDO in myogenesis.
REACT_240735. S45 mutants of beta-catenin aren't phosphorylated.
REACT_242531. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_245438. Beta-catenin phosphorylation cascade.
REACT_245811. formation of the beta-catenin:TCF transactivating complex.
REACT_245964. T41 mutants of beta-catenin aren't phosphorylated.
REACT_248099. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_248818. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249017. S33 mutants of beta-catenin aren't phosphorylated.
REACT_249811. Degradation of beta-catenin by the destruction complex.
REACT_249843. TCF dependent signaling in response to WNT.
REACT_250752. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_253559. Adherens junctions interactions.
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: Chromosome I

Organism-specific databases

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

Subcellular locationi

Cell junctionadherens junction 1 Publication

GO - Cellular componenti

  1. basolateral plasma membrane Source: RefGenome
  2. catenin complex Source: WormBase
  3. cell-cell adherens junction Source: WormBase
  4. cytoplasmic side of plasma membrane Source: RefGenome
  5. cytosol Source: RefGenome
  6. desmosome Source: RefGenome
  7. fascia adherens Source: RefGenome
  8. nucleus Source: WormBase
  9. transcription factor complex Source: RefGenome
  10. Z disc Source: RefGenome
  11. zonula adherens Source: RefGenome
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: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.
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 .
PIRi T23341.
RefSeqi NP_001252426.1. NM_001265497.1.
UniGenei Cel.7074.

3D structure databases

ProteinModelPortali O44326.
SMRi O44326. Positions 69-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 38723. 20 interactions.
DIPi DIP-27261N.
IntActi O44326. 4 interactions.
MINTi MINT-1079247.
STRINGi 6239.K05C4.6.

Proteomic databases

PaxDbi O44326.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai K05C4.6a.1 ; K05C4.6a.1 ; WBGene00001979 .
K05C4.6a.2 ; K05C4.6a.2 ; WBGene00001979 .
GeneIDi 173338.
KEGGi cel:CELE_K05C4.6.
UCSCi K05C4.6. c. elegans.

Organism-specific databases

CTDi 173338.
WormBasei K05C4.6a ; CE19974 ; WBGene00001979 ; hmp-2.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000021706.
InParanoidi O44326.
PhylomeDBi O44326.

Enzyme and pathway databases

Reactomei REACT_184336. Ca2+ pathway.
REACT_229949. deactivation of the beta-catenin transactivating complex.
REACT_232673. VEGFR2 mediated vascular permeability.
REACT_239816. CDO in myogenesis.
REACT_240735. S45 mutants of beta-catenin aren't phosphorylated.
REACT_242531. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_245438. Beta-catenin phosphorylation cascade.
REACT_245811. formation of the beta-catenin:TCF transactivating complex.
REACT_245964. T41 mutants of beta-catenin aren't phosphorylated.
REACT_248099. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_248818. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249017. S33 mutants of beta-catenin aren't phosphorylated.
REACT_249811. Degradation of beta-catenin by the destruction complex.
REACT_249843. TCF dependent signaling in response to WNT.
REACT_250752. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_253559. Adherens junctions interactions.
SignaLinki O44326.

Miscellaneous databases

NextBioi 879233.
PROi O44326.

Gene expression databases

ExpressionAtlasi O44326. baseline.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view ]
Pfami PF00514. Arm. 1 hit.
[Graphical view ]
PRINTSi PR01869. BCATNINFAMLY.
SMARTi SM00185. ARM. 5 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
PROSITEi PS50176. ARM_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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 26, 2014
This is version 120 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