wanglab/gogpt-training-data huggingface dataset:
Protein: Probable 2-ketoarginine decarboxylase AruI (EC 4.1.1.75) (2-oxo-5-guanidinopentanoate decarboxylase) (5-guanidino-2-oxopentanoate decarboxylase) (Q9HUI8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the decarboxylation of 2-ketoarginine, leading to the formation of 4-guanidinobutyraldehyde.
Interaction partners:
- Arginine--pyruvate transaminase AruH
- Probable aldehyde dehydrogenase
- Acetolactate synthase small subunit
- Ketol-acid reductoisomerase
- ATP-grasp domain-containing protein
- 2-isopropylmalate synthase
- Dihydroxy-acid dehydratase
- 3-isopropylmalate dehydrogenase
- Benzoylformate decarboxylase
- Probable decarboxylase
Sequence:
MGARALRRERRLRWSPNWTRILPMQPQKTLTAGQALVRLLANYGVDTVFGIPGVHTLELYRGLPGSGIRHVLTRHEQGAGFMADGYARVSGKPGVCFVITGPGVTNVATAIGQAYADSVPLLVISSVNHSASLGKGWGCLHETQDQRAMTAPITAFSALALSPEQLPELIARAYAVFDSERPRPVHISIPLDVLAAPVAHDWSAAVARRPGRGVPCSEALRAAAERLAAARRPMLIAGGGALAAGEALAALSERLAAPLFTSVAGKGLLPPDAPLNAGASLCVAPGWEMIAEADLVLAVGTEMADTDFWRERLPLSGELIRVDIDPRKFNDFYPSAVALRGDARQTLEALLVRLPQEARDSAPAAARVARLRAEIRAAHAPLQALHQAILDRIAAALPADAFVSTDMTQLAYTGNYAFASRAPRSWLHPTGYGTLGYGLPAGIGAKLGAPQRPGLVLVGDGGFLYTAQELATASEELDSPLVVLLWNNDALGQIRDDMLGLDIEPVGVLPRNPDFALLGRAYGCAVRQPQDLDELERDLRAGFGQSGVTLIELRHACAR
Protein: Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain] (P0A790)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:6767707}.
Interaction partners:
- Pantothenate synthetase
- PanD regulatory factor
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- 4-aminobutyrate aminotransferase GabT
- Glutamate decarboxylase beta
- 4-aminobutyrate aminotransferase PuuE
- Glutamate decarboxylase alpha
- 2-dehydropantoate 2-reductase
- L-aspartate oxidase
- Aspartate aminotransferase
Sequence:
MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAIAAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKAIPVQVA
Protein: High mobility group protein hmg-12 (High mobility group AT-hook protein hmg-12) (High mobility group protein I beta) (G5EDQ2)
Organism: Caenorhabditis elegans
Function: Transcriptional regulator. Binds to specific sequence motifs in regulatory elements. May recruit transcription factors, or may induce structural changes in chromatin, to thereby modulate embryonic expression of ATP-dependent chaperone cdc-48.1.
Subcellular location: Nucleus {ECO:0000305|PubMed:18430416}.
Interaction partners:
- Piwi domain-containing protein
- Transcription initiation factor TFIID subunit 11
Sequence:
MSDVAEEKAEFLVIRTYGSESFRKECADLIEKELHKLNATIARVPVGEFVAYAENAVKNETDSEAVGSSSVKRENSANDSPANTNDVDIVSSPVKRGRGRKAKNPSADADVNDTGSSPVKKGRGRPIKNPSADAGSPLVKKGRGRRAQTPAADTDAIDTASSPVKKGRGRPAKNPSADAGSPLVKKGRGRQAKNLAADTDAIDTASSPVKKGRGRPLKKTAAEADVNGLGSPSANRITGCPPSTKVSNQSSPPEPAVNESEEADEPVLKRGRSVKQPKDESESDDEDAEKAPAAIPKKRGRPGKSAIDAFFDGSD
Protein: Present in the outer mitochondrial membrane proteome 8 (Q38DA9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDLDATKISIISVKKANPKLLAEVGDEANELPVTVKEKRAHEKRCNFCCMSIGLLFSAFMVVMVASIGTGMAVYTEKRARYTVNGVMRQVGWISLPGLLVGTTLHYFLSEAMWSGRRNSWGQAWMKAFATNTAIWSVAIGTGTLLWRKGLLINAAGRRLYYRYPIPSDPLEYRLVRSEAQFFTGMGWSYWLSGVVSGQVGLVSCVGFCVWNDRPYFMMNPHGGYARRCMPNWRREQLARQANVSLSE
Protein: Elongation factor Tu, chloroplastic (EF-Tu) (O24310)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15219860}.
Interaction partners:
Sequence:
MALSSTAATTSSKLKLSNPPSLSHTFTASASASVSNSTSFRPKLTLTRLSSSFLNPSTILHLTPSQRTNRPSSSPFTVRAARGKFERKKPHLNIGTIGHVDHGKTTLTAALTMALACLGNSAPKKYDEIDAAPEERARGITINTATVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPSVVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIVSGSALLALEALMANPTLKRGNNQWVDKIYQLMDEVDKYIPIPQRQTELPFLLAIEDVFSITXRGTVATGRIERGLVKVGDVVDLVGLRETRNTTVTGVEMFQKILDDAMAGDNVGLLLRGIQKIDIQRGMVLAKPGTITPHSKFSAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSIMNDKDEESKMVMPGDRVKIVVELIVPVAIEQGMRFAIREGGKTVGAGVIGAIIE
Protein: LD42724p (Phosphatidylinositol 3-kinase regulatory subunit) (p60 protein) (O18683)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQPSPLHYSTMRPQAPGSLVDPNEDELRMAPWYWGRISREEAKSILHGKPDGSFLVRDALSMKGEYTLTLMKDGCEKLIKICHMDRKYGFIETDLFNSVVEMINYYKENSLSMYNKTLDITLSNPIVRAREDEESQPHGDLCLLSNEFIRTCQLLQNLEQNLENKRNSFNAIREELQEKKLHQSVFGNTEKIFRNQIKLNESFMKAPADAPSTEAGGAGDGANAAASAAANANARRSLQEHKQTLLNLLDALQAKGQVLNHYMENKKKEELLLERQINALKPELQILQLRKDKYIERLKGFNLKDDDLKMILQMGFDKWQQLYETVSNQPHSNEALWLLKDAKRRNAEEMLKGAPSGTFLIRARDAGHYALSIACKNIVQHCLIYETSTGFGFAAPYNIYATLKSLVEHYANNSLEEHNDTLTTTLRWPVLYWKNNPLQVQMIQLQEEMDLEYEQAATLRPPPMMGSSAPIPTSRSREHDVVDGTGSLEAEAAPASISPSNFSTSQ
Protein: Ectonucleoside triphosphate diphosphohydrolase 6 (Q5QPJ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKKGIRYETSRKTSYIFQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYIKWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQFTRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLKATAGLRLLP
Protein: Serine-arginine repetitive matrix 2/3/4, isoform H (X2J8K5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQGKTDLAKDEFGRVAARDTHQIAEAQQQKNARLREAFNISEYFVEGSSFDGDRKAKEDLAKSVALQKELDAQRESLAAAAAAAAAGKDKETGKRYALVRTPSRERDRDAGDAAANGDERDHVSKTDKKKRKKRARESSASPERKKKKKSKKHKKERDSYEKESKKKRKATYK
Protein: RE02747p (Q8SZF0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNQTQVNNFLKCFLQIDEPSNRWTSRHDGEDLDDNDHDHDHDDDNDDDESGVLVAKVTAMVVLFCASAICGSIPFLLNRCYRWTENQTNARSAIVVKCLLYFGGGVLLATTFLHLLPEVQEVVEELQECGIIGELTFPLAELLMCCGFFLMYFIEEAMHTYVHHHQKDEAGAAFERGHSIRNSHLLKPTEGNATTPTAPPAPLAGTAELGTLSVQNLLQNDLEQQKFATKPQQQANGHGHSHGHGHGHSHLSVIADDADAGDMLASSLRGLFIVSALSLHELFEGMAIGLESSASSVWFMFGAVSAHKLVLAFCVGVELIVARTRMLLAVLYVLTFAVVSPLGIGIGILINHGEETSGPSLVSAILQGFACGTLIYVVFFEILSKNRSGLRAYLALFVGFLVMFGLQQLTSIGGHGHSHSHSSCSTSEHTHNHQETETETRSASGHTHGHQHDHDHPHHHNHAEELATVHNYEQQLQLLRQVTQKLLEAHPKKDA
Protein: T-cell immunomodulatory protein (Protein TIP) (Integrin-alpha FG-GAP repeat-containing protein 1) (Linkin) (Q8TB96)
Organism: Homo sapiens (Human)
Function: Modulator of T-cell function. Has a protective effect in graft versus host disease model (By similarity).
Subcellular location: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- TIMELESS-interacting protein
Sequence:
MAAAGRLPSSWALFSPLLAGLALLGVGPVPARALHNVTAELFGAEAWGTLAAFGDLNSDKQTDLFVLRERNDLIVFLADQNAPYFKPKVKVSFKNHSALITSVVPGDYDGDSQMDVLLTYLPKNYAKSELGAVIFWGQNQTLDPNNMTILNRTFQDEPLIMDFNGDLIPDIFGITNESNQPQILLGGNLSWHPALTTTSKMRIPHSHAFIDLTEDFTADLFLTTLNATTSTFQFEIWENLDGNFSVSTILEKPQNMMVVGQSAFADFDGDGHMDHLLPGCEDKNCQKSTIYLVRSGMKQWVPVLQDFSNKGTLWGFVPFVDEQQPTEIPIPITLHIGDYNMDGYPDALVILKNTSGSNQQAFLLENVPCNNASCEEARRMFKVYWELTDLNQIKDAMVATFFDIYEDGILDIVVLSKGYTKNDFAIHTLKNNFEADAYFVKVIVLSGLCSNDCPRKITPFGVNQPGPYIMYTTVDANGYLKNGSAGQLSQSAHLALQLPYNVLGLGRSANFLDHLYVGIPRPSGEKSIRKQEWTAIIPNSQLIVIPYPHNVPRSWSAKLYLTPSNIVLLTAIALIGVCVFILAIIGILHWQEKKADDREKRQEAHRFHFDAM
Protein: Dual specificity protein phosphatase 26 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP3) (Low-molecular-mass dual-specificity phosphatase 4) (DSP-4) (LDP-4) (Mitogen-activated protein kinase phosphatase 8) (MAP kinase phosphatase 8) (MKP-8) (Novel amplified gene in thyroid anaplastic cancer) (Q9BV47)
Organism: Homo sapiens (Human)
Function: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity. Inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. Can also induce activation of MAP kinase p38 and c-Jun N-terminal kinase (JNK).
Subcellular location: Cytoplasm. Nucleus. Golgi apparatus.
Interaction partners:
Sequence:
MCPGNWLWASMTFMARFSRSSSRSPVRTRGTLEEMPTVQHPFLNVFELERLLYTGKTACNHADEVWPGLYLGDQDMANNRRELRRLGITHVLNASHSRWRGTPEAYEGLGIRYLGVEAHDSPAFDMSIHFQTAADFIHRALSQPGGKILVHCAVGVSRSATLVLAYLMLYHHLTLVEAIKKVKDHRGIIPNRGFLRQLLALDRRLRQGLEA
Protein: Protein ECERIFERUM 16 (RST1-intearcting protein) (F4K8S5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with RST1, acts as cofactor of the cytoplasmic exosome and connects the cytosolic RNA exosome to the SKI complex. Acts as post-transcriptional gene silencing (PTGS) suppressor. CER16/RIPR can, like RST1 suppress the production of small interfering RNAs (siRNAs) from the CER3 locus, which is involved in cuticule membrane and wax production, and in the typhine and sporopollenin biosynthesis of pollen.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:31455787}. Endoplasmic reticulum {ECO:0000269|PubMed:31941670}.
Interaction partners:
- N-alpha-acetyltransferase MAK3
- Exosome complex exonuclease RRP46 homolog
- Maternal effect embryo arrest protein
- Protein RST1
- DExH-box ATP-dependent RNA helicase DExH9
- Tetratricopeptide repeat protein SKI3
- Polyadenylate-binding protein 2
- Coiled-coil protein
- DExH-box ATP-dependent RNA helicase DExH10
- Exosome complex component RRP45B
Sequence:
MDSKSLAKSKRAHTLHHSKKSHSVHKPKVPGVSEKNPEKLQGNQTKSPVQSRRVSALPSNWDRYDDELDAAEDSSISLHSDVIVPKSKGADYLHLISEAQAESNSKIENNLDCLSSLDDLLHDEFSRVVGSMISARGEGILSWMEDDNFVVEEDGSGSYQEPGFLSLNLNVLAKTLENVDLHERLYIDPDLLPLPELNTSQTKVSRNEEPSHSHIAQNDPIVVPGESSVREAESLDQVKDILILTDESEKSSAIEADLDLLLNSFSEAHTQPNPVASASGKSSAFETELDSLLKSHSSTEQFNKPGNPSDQKIHMTGFNDVLDDLLESTPVSIIPQSNQTSSKVLDDFDSWLDTI
Protein: Tumor necrosis factor ligand superfamily member 8 (CD30 ligand) (CD30-L) (CD antigen CD153) (P32971)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to TNFRSF8/CD30. Induces proliferation of T-cells.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 8
- Tumor necrosis factor receptor superfamily member 4
- CD27 antigen
- Tumor necrosis factor ligand superfamily member 15
- Tumor necrosis factor receptor superfamily member 5
- Tumor necrosis factor ligand superfamily member 4
- Tumor necrosis factor receptor superfamily member 9
- CD40 ligand
- Tumor necrosis factor
- Interleukin-8
Sequence:
MDPGLQQALNGMAPPGDTAMHVPAGSVASHLGTTSRSYFYLTTATLALCLVFTVATIMVLVVQRTDSIPNSPDNVPLKGGNCSEDLLCILKRAPFKKSWAYLQVAKHLNKTKLSWNKDGILHGVRYQDGNLVIQFPGLYFIICQLQFLVQCPNNSVDLKLELLINKHIKKQALVTVCESGMQTKHVYQNLSQFLLDYLQVNTTISVNVDTFQYIDTSTFPLENVLSIFLYSNSD
Protein: RNI-like superfamily protein (Q9FHI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alpha-galactosidase 2
Sequence:
MDSGTQPEGLQAAQPAGLQAAGLQAAQPAGLQAAQPAGLQAAGKRKPPTTTEDPNDPQHIIHDFLTIVNKLEKEVDLPGAITRARTYDAEVDGLITADQPQTNLGRAESAPIPNAKPEGPDDHHIPKLQRNLRLLKEDVAKLQYLRSEVAEEVWKHIRPLELLLENVAKEQKKNPTKPPLTLGMKKDLDDINKKIFNLMCQVPLLPNKRKKAKGLDDDDGDGDNNNGKGIVCLPGIHANKADLRSRAVFRYVLREFEELSDQRKICLLTFAVFPENQEVNRTMLMYWWMGEGILSTKDISSQEGTEEVILKPEDVVKVILKDFTDRNLIEPVEIKRKVEPSSYKMAPFVHASVVLISKEIGLFDMYDIKDKPVMKKSGMHKVCLVEGSSSQQEAKAKKMEDVDHIETVFNVSERFPDFTFKWFSEDKPTRNKLTLSKVTYQKLKVFYLGRWERTAKRHIEVENPELMKNLKRMIKLKLLSFQGISRIERLDDAVCKLRDLIILDLRACYNLEKLPDKIDSLKALIYLDITDCYMIDRMPKRLSWLDNLEVLKGFVVSDATDEETVCTLAELVHLKKLRKLSISINKENFSIDDVFVAVKSFKKLEKLKVAWGGINTHPQGKGVDSEKGDENVKPKENIGILERAATMFRKEKDPTAPELPKTLKKLDLQCFPGEHLPEWLEPDNLLNVEKLYIKGGIKLTGFGKSLPSQNSKCKVTVLRLKFLPKLKVEWRDLSKRYFPELKFLEKYQCPQVSLCPCDGIGIWRKPEEDEV
Protein: Taxoid 7-beta-hydroxylase (EC 1.14.14.182) (Q6JTJ0)
Organism: Taxus cuspidata (Japanese yew)
Function: Catalyzes the conversion of taxusin to 7-beta-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 2-alpha-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:15157877}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDALSLVNSTVAKFNEVTQLQASPAILSTALTAIAGIIVLLVITSKRRSSLKLPPGKLGLPFIGETLEFVKALRSDTLRQFVEEREGKFGRVFKTSLLGKPTVILCGPAGNRLVLSNEEKLLHVSWSAQIARILGLNSVAVKRGDDHRVLRVALAGFLGSAGLQLYIGKMSALIRNHINEKWKGKDEVNVLSLVRDLVMDNSAILFFNIYDKERKQQLHEILKIILASHFGIPLNIPGFLYRKALKGSLKRKKILSALLEKRKDELRSRLASSNQDLLSVLLSFRDERGKPLSDEAVLDNCFAMLDASYDTTTSQMTLILKMLSSNPECFEKVVQEQLEIASNKKEGEEITMKDIKAMKYTWQVLQESLRMLSPVFGTLRKTMNDINHDGYTIPKGWQVVWTTYSTHQKDIYFKQPDKFMPSRFEEEDGHLDAYTFVPFGGGRRTCPGWEYAKVEILLFLHHFVKAFSGYTPTDPHERICGYPVPLVPVKGFPIKLIARS
Protein: GPEET2 procyclin (Q581F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MAPRSLYLLAILLFSANVFAGVGFAAAADESASNVIVKGGKGKEREDGPEEPEETGPEETGPEETGPEETGPEETGPEETGPEETEPEPEPGAATLKSVALPIAVAAAALVAAF
Protein: Vomeronasal type-1 receptor (B2RWV5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MSLFKNVLYFQAGLGVLANMFLLFFYIFIILGHRPKPTDLISCQLTFVHIMMFLAGGDIWLTDIFETLNIENDFKCKTIFYISRVMRGLSICNTCLPSVVQAVTISPSTSLLAKFKPRLKMYLIYAFFCIWSFNLLYSSNQILYVGGFTNLSETNQMKVTKSCTLLPKNYIIKGLILTVSISRDVFLVGVMLTTSTYMLNILFRHQRQCKHLHSISYLRASPEKRATQTILLLVVFFVVMYWVDFIISSTSVMLWMYDPVVLTVQKFVMCAYPTITPLVQITSDNRIIIMLENMQSKHRQNFF
Protein: Killer cell lectin-like receptor subfamily B member 1B allele B (CD161 antigen-like family member B) (Inhibitory receptor NKR-P1B) (Lymphocyte antigen 55d) (Ly-55d) (NKR-P1D) (Natural killer cell surface protein NKR-P1B allele B6) (CD antigen CD161b) (Q99JB4)
Organism: Mus musculus (Mouse)
Function: Receptor for CLEC2D/OCIL. Ligand-binding contributes to inhibition of cytotoxic natural killer (NK) cells. May mediate MHC class I-independent 'missing-self' recognition of allografts, tumor cells and virus-infected cells.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 2 member D
Sequence:
MDSTTLVYADLNLARIQEPKHDSPPSLSPDTCRCPRWHRLALKFGCAGLILLVLVVIGLCVLVLSVQKSSVQKICADVQENRTHTTGCSAKLECPQDWLSHRDKCFHVSQVSNTWKECRIDCDKKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLSYTLTDMNWKWINGTAFNSDVLKITGVTENGSCAAISGEKVTSEGCSSDNRWICQKELNHETPCNDS
Protein: Sorting nexin 6 (G3V5X9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMEGLDDGPDFLSEEDRGLKAINVDLQSDAALQVDISDALSERDKVKFTVHTKIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRRDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDIC
Protein: EG:118B3.2 (Q9U4H0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSLAAVPQASATGSSSNSNINNNNALAALQDGGAAAAAAADFYQQLAAAATATATATSANGSNTSADSPVSSFPAAAAAVAVAAVAASSYQQQQQQQQLLNNEQQQQQLLEANNKMQELHKQMERFRSEQMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQEPDLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADESESHYSSTSSLNSGTPDLGTTPIIFPPSSDWHESIRLPVLQSTNLHVNVGNEVGAGQGTNTSSGSGGDLASTTKATLPLRDQQQLAITSTQSQVQNVSQPSTPATPSSAGSSSSGGLPFGNVSKSFISGERKDPLNMLAKNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNINDMCQIERPDWMQVMSYVTAVYKYFET
Protein: Cadherin-1 (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3] (F1PAA9)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:P12830}. Cell membrane {ECO:0000250|UniProtKB:P12830}; Single-pass type I membrane protein {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000250|UniProtKB:P09803}. Cell junction, desmosome {ECO:0000250|UniProtKB:P12830}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane (By similarity). Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (By similarity). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:P12830}.
Interaction partners:
- Catenin beta-1
- Catenin delta 1.
- Uncharacterized protein.
- Catenin alpha 1.
- Matrix metalloproteinase-9
- Catenin alpha 2.
- Catenin alpha 3.
- Occludin
- Rap guanine nucleotide exchange factor 1.
- Uncharacterized protein.
Sequence:
MGPRYGGAPALLLPLLLLLQVSSGLCQEPEPCRPGFGADSYTFTVPRRHLERGRVLGRVSFEGCTGLPRTAYVSDDTRFKVGTDGVITVKRPLQLHKPEISFLVHAWDSSRRKLSTRVRLKAATHHHHHHHDAPSKTQTEVLTFPSSQHGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNRDKEIKVFYSITGQGADAPPVGVFIIERETGWLKVTEPLDREQIAKYILYSHAVSSNGNAVEDPMEIVITVTDQNDNKPEFTQAVFQGSVTEGALPGTSVMQVTATDADDDVNTYNAAIAYSILTQDPLLPSSMMFTINKDTGVISVLTTGLDREGVPMYTLVVQAADLQGEGLTTTATAVITVTDINDNPPIFNPTTYQGRVPENKANVEIAVLKVTDADVPDTPAWRAVYTILNNNNDQFVVTTDPVTNDGILKTTKGLDFEDKQQYVLYVTVVNVTPFEVILSTSTATVTVDVEDVNEAPIFIPCPKVVSIPEDFGVGQEITSYTAEDPDTYMEQRITYRIWRDAAGWLEVNPESGAIFTRAELDREDFEHVKNSTYEALIIAIDNGSPVATGTGTLLLVLSDVNDNGPIPEPRNMDFCQKNPQPHVINIIDPDLPPNTSPFTAELTHGASVNWTIEYNDPARESLILKPKKTLELGDYKINLKLTDNQNKDQVTTLDVFVCDCEGVVNSCKRTAPYAEAGLQVPAILGILGGILALLILILLLLLFVRRRRVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLLSVPQYRPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD
Protein: Ubiquitin-binding ESCRT-I subunit protein (Q59WF8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting-associated protein 28
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF7
- ESCRT-III subunit protein
- Vacuolar-sorting protein SNF8
- Polyubiquitin
- Ubiquitin-ribosomal protein eS31 fusion protein
- ESCRT-III subunit protein
- Vacuolar protein-sorting protein BRO1
Sequence:
MVSQQVSNWLFNVIQPSYEHKKEVYAHVFQFLQLHLKKNLNFKIRTQIYTSSGSGEPNLLINLFGTIQINEQIGTPIEIWVPFAYPYVDYENKGAPIVYIVPDHSKGWYLKPNNNVDTQGMFYHPYLTRWHRECLRSNPDSLNMFSLVELANVIYRSVTTDSPIASKPPGITNTPQKPAKVPLDFNSISTEQPLNLHQLNTEQPAVIPVQTTGPPLPAKPPKAQNDIHSSTPLKYQAPLPLPHEAEKFNYPQERTSSPLPPLGFINQQPSRSPAIASAVPHTMTPPQPSPPVDLIDGENPLSETNTGVTNLTHELYSKINHFLSEEEKTIKDVNEKTMKIKVLYEQLNHYYSSALKNSSFLDDIVSQLTSKVRDLTQLNQELGVVNELNHQSQDSIAISSTKKIPLDEIVIADSPMIDTLYKVSAEINSITDTINLISGNFHNEQEIVNEKSFDSCLKTTRKMGRELFWLHFIKSEIGNKLQ
Protein: Proline-rich receptor-like protein kinase PERK8 (EC 2.7.11.1) (Proline-rich extensin-like receptor kinase 8) (AtPERK8) (Q9FFW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Could be involved in the negative regulation of root growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}; Single-pass membrane protein {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}.
Interaction partners:
- Serine/threonine-protein kinase KIPK1
- Serine/threonine-protein kinase KIPK2
- Kinesin-like protein KIN-14E
- Nuclear pore complex protein NUP62
- Protein transport protein SEC31 homolog B
- Small ribosomal subunit protein uS4m
Sequence:
MSLVPPLPILSPPSSNSSTTAPPPLQTQPTTPSAPPPVTPPPSPPQSPPPVVSSSPPPPVVSSPPPSSSPPPSPPVITSPPPTVASSPPPPVVIASPPPSTPATTPPAPPQTVSPPPPPDASPSPPAPTTTNPPPKPSPSPPGETPSPPGETPSPPKPSPSTPTPTTTTSPPPPPATSASPPSSNPTDPSTLAPPPTPLPVVPREKPIAKPTGPASNNGNNTLPSSSPGKSEVGTGGIVAIGVIVGLVFLSLFVMGVWFTRKRKRKDPGTFVGYTMPPSAYSSPQGSDVVLFNSRSSAPPKMRSHSGSDYMYASSDSGMVSNQRSWFSYDELSQVTSGFSEKNLLGEGGFGCVYKGVLSDGREVAVKQLKIGGSQGEREFKAEVEIISRVHHRHLVTLVGYCISEQHRLLVYDYVPNNTLHYHLHAPGRPVMTWETRVRVAAGAARGIAYLHEDCHPRIIHRDIKSSNILLDNSFEALVADFGLAKIAQELDLNTHVSTRVMGTFGYMAPEYATSGKLSEKADVYSYGVILLELITGRKPVDTSQPLGDESLVEWARPLLGQAIENEEFDELVDPRLGKNFIPGEMFRMVEAAAACVRHSAAKRPKMSQVVRALDTLEEATDITNGMRPGQSQVFDSRQQSAQIRMFQRMAFGSQDYSSDFFDRSQSHSSWGSRDQSRFVP
Protein: Early endosome antigen 1 (Q8BL66)
Organism: Mus musculus (Mouse)
Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
Subcellular location: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-5A
- Ras-related protein Rab-5B
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Rab GTPase-binding effector protein 1
- Syntaxin-12
- Rab5 GDP/GTP exchange factor
- Lysosome-associated membrane glycoprotein 1
- Ras-related protein Rab-5C
- Transferrin receptor protein 1
- Ras-related protein Rab-11A
Sequence:
MFRRILQRTPGRVGSQGSDLDSSATPINTVDVNNESSSEGFICPQCMKSLGSADELFKHYQAVHDAGNDSGHGGEAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDLQG
Protein: Tetratricopeptide repeat protein 38 (TPR repeat protein 38) (Q5R3I4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAASPLRDCQAWKDARLPLSTTSNEACKLFDATLTQYVKWTNDKSLGGIEGCLSKLKAADPTFVMGHAMATGLVLIGTGSSVKLDKELDLAVKTMVEISRTQPLTRREQLHVSAVETFANGNFPKACELWEQILQDHPTDMLALKFSHDAYFYLGYQEQMRDSVARIYPFWTPDIPLSSYVKGIYSFGLMETNFYDQAEKLAKEALSINPTDAWSVHTVAHIHEMKAEIKDGLEFMQHSETFWKDSDMLACHNYWHWALYLIEKGEYEAALTIYDTHILPSLQANDAMLDVVDSCSMLYRLQMEGVSVGQRWQDVLPVARKHSRDHILLFNDAHFLMASLGAHDPQTTQELLTTLRDASESPGENCQHLLARDVGLPLCQALVEAEDGNPDRVLELLLPIRYRIVQLGGSNAQRDVFNQLLIHAALNCTSSVHKNVARSLLMERDALKPNSPLTERLIRKAATVHLMQ