wanglab/gogpt-training-data huggingface dataset:
Protein: Putative oxidoreductase SadH (EC 1.-.-.-) (P9WGP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH.
Interaction partners:
- Putative acetyl-hydrolase LipR
- Putative FAD-containing monooxygenase MymA
- Putative alcohol dehydrogenase D
- Probable diacyglycerol O-acyltransferase Tgs4
- Long-chain-fatty-acid--CoA ligase FadD13
- Putative diacyglycerol O-acyltransferase Rv3087
Sequence:
MSSFEGKVAVITGAGSGIGRALALNLSEKRAKLALSDVDTDGLAKTVRLAQALGAQVKSDRLDVAEREAVLAHADAVVAHFGTVHQVYNNAGIAYNGNVDKSEFKDIERIIDVDFWGVVNGTKAFLPHVIASGDGHIVNISSLFGLIAVPGQSAYNAAKFAVRGFTEALRQEMLVARHPVKVTCVHPGGIKTAVARNATVADGEDQQTFAEFFDRRLALHSPEMAAKTIVNGVAKGQARVVVGLEAKAVDVLARIMGSSYQRLVAAGVAKFFPWAK
Protein: Plasmepsin III (EC 3.4.23.39) (Histo-aspartic protease) (PfHAP) (Plasmepsin 3) (Q8IM15)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Vacuole lumen {ECO:0000269|PubMed:23471987}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:23471987}.
Interaction partners:
Sequence:
MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL
Protein: Rifin (Q8I3E0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFVIPLNILIYNQRNHNSTTPHHPPNTRLLCECDIYTSIYDNDPQMKAVMENYNRQTSDRFKEYDERMQGKRQKCKEQCDKEIQKIVLKDKIDKELTEKFATLQTDIQSDSIPTCVCEKSLADKTEKFCHNCGYGLGSVAPSIGLLGGPGIYGWKTAALAAATKDAITKGLAAGEAARIKEGINAVIAGIKSTFSIDKLGGEALKSVITAQKYNKVALISESIYSEFSRSGCGDITSSSFLKNPFCTSVYEGIDAISGGNGVSPEDFIKRTVQSMVSDANGVANAAAEIAEATEKAKAIKTSTDAIEAASTQLYGAIGYSILAILIIVLIMLIIYLILRYRRKKKMKKKLQYIKLLKE
Protein: Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1) (P20456)
Organism: Bos taurus (Bovine)
Function: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates (By similarity). Is equally active with myo-inositol monophosphate and D-galactose 1-phosphate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol polyphosphate 1-phosphatase
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol monophosphatase 2
- Myotubularin
- Inositol polyphosphate-4-phosphatase type I A
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- Transcription termination factor 2
- Glucose-6-phosphate isomerase
Sequence:
MADPWQECMDYAVTLAGQAGEVVREALKNEMNIMVKSSPADLVTATDQKVEKMLITSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHGFPFVAVSIGFVVNKKMEFGIVYSCLEDKMYTGRKGKGAFCNGQKLQVSHQEDITKSLLVTELGSSRTPETVRIILSNIERLLCLPIHGIRGVGTAALNMCLVAAGAADAYYEMGIHCWDVAGAGIIVTEAGGVLLDVTGGPFDLMSRRVIASSNKTLAERIAKEIQIIPLQRDDED
Protein: Uncharacterized protein (O53954)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- PE family protein PE20
Sequence:
MTASVVATSRERHSHKAAKQRACEITDFEPEGRFRVRKRRRGRIGTKRSSISDTDYRRDSFRSHLLTAGAHGDADAQHKGMTAQQTTELGTPLVRALAPHGVSGRSSRKPLGLNP
Protein: Protein MLN51 homolog (Protein CASC3 homolog) (Protein barentsz) (Btz) (Q93ZJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15234}. Cytoplasm {ECO:0000250|UniProtKB:O15234}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:O15234}.
Interaction partners:
- Eukaryotic initiation factor 4A-III homolog
- RNA-binding protein Y14
- Protein mago nashi homolog
- Partner of Y14 and mago
- Eukaryotic initiation factor 4A-3
- Transcription initiation factor TFIID subunit
Sequence:
MAPDGVEDSDYESDPDELNRSLATRRREASDDDEDDEEADDHDKLRAAIQIHSDEHSGVVVVDSDDNEGLHIEDSYGDDDDEEEDGDYGQVDDHVEYIADNNDKTIVAGNGTDDSAATDLVDGEEQKKKEPFAVPTAGAFYMHDDRFQELDAASNRRMRGGRRLWQSRDERKWGHDKFEEMNTQKQQYDRRTSRGRGRGRGQGRGQDRGQSRGNNSKEFTGNGHQNQFPKAVTRGRGARRYEVALRNGNQAPSVQTKQSQNSSVEVSHVDLGRPPTETATLETEAIQAKKNVFASSLNSASPPFYPSRSNNNLAQKDVQAGMGRLHINENPNPTGKKFGNTKSSSLWGRTAQTTSHGRGVPPHGQVLYQQSPNQGDKVSSPMQIRGMPKGTDQSCTQLPGQVFNQHSAVISLLPSSPPKTGSSENPYLSGEIESAVETGALVAKGKGSLQPSGRGSFMYGGTQFMGPAGMAAGHGNPNFPAFLPVMQFGGQHGGVPTFGMALPGYFQPEHGTGNPEMTWLPILAGPGALGGSYCPPYTVLDGSYQADKPGLPSSAGSSSQENSSNNPNDEEPMERPEVTNNGNSQRSNSNPNKQPRRYSEMSFSK
Protein: Profilin-2 (Profilin II) (P35080)
Organism: Homo sapiens (Human)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Protein enabled homolog
- Ena/VASP-like protein
- Actin-related protein 2/3 complex subunit 1A
- Histone deacetylase 1
- Actin, cytoplasmic 1
- N-alpha-acetyltransferase 80
- Actin, cytoplasmic 2
- Protein diaphanous homolog 1
- Formin-like protein 1
Sequence:
MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPIEIDMIVGKDREGFFTNGLTLGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYNVAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF
Protein: Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26) (P11274)
Organism: Homo sapiens (Human)
Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. The amino terminus contains an intrinsic kinase activity. Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity. Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation.
Subcellular location: Postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000250|UniProtKB:F1LXF1}.
Interaction partners:
- Tyrosine-protein kinase ABL1
- Growth factor receptor-bound protein 2
- Crk-like protein
- E3 ubiquitin-protein ligase CBL
- Adapter molecule crk
- Signal transducer and activator of transcription 5B
- SHC-transforming protein 1
- Signal transducer and activator of transcription 5A
- SHC-transforming protein 3
- SHC-transforming protein 2
Sequence:
MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV
Protein: Hematopoietic death receptor (F1QD95)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Tumor necrosis factor receptor superfamily, member a.
- Interleukin
- Tumor necrosis factor ligand superfamily member 10
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor ligand superfamily member 10
Sequence:
MRYITLLVLLLLNVINAARSHGDLAWAHRSVKNRLSRDVSCREGLEYPHENICCLNCPAGTYVKKACAAAAEKGVCAPCEFDTYTEHDHGLLKCISCDKCRIDQETIEKCTSTQNTRCKCRNGSFCLPDQACEVCKKCSRCKEDEETEKSCTAISNTVCRKRSSPGSSTSMTFIVIMPLIVLLACVLCIVYWTKSKQNKTAVTSRSPREMVKICMGDSEEVREEKQNDHNSRIDDSSQLQPFLEQNYVVGTSVPHPSEAEKDKGLGDSLPNTANSSQTSLAICAVPSDLQSCHTNQSSSSVLAWQPPALESESSRRLVPLSGEESLKKTFDFFEEIDVHYHNRFFRLIGLSDNAIKSAESLFPEDRVYELLKIWMEKEGLKADFNSLIDALIYLDQRLSAENIIAKAINNSCFKYEEE
Protein: Small ribosomal subunit protein mS29 (28S ribosomal protein S29, mitochondrial) (MRP-S29) (S29mt) (Death-associated protein 3) (DAP-3) (Ionizing radiation resistance conferring protein) (P51398)
Organism: Homo sapiens (Human)
Function: Involved in mediating interferon-gamma-induced cell death.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11162496, ECO:0000269|PubMed:20563667}.
Interaction partners:
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS12m
Sequence:
MMLKGITRLISRIHKLDPGRFLHMGTQARQSIAAHLDNQVPVESPRAISRTNENDPAKHGDQHEGQHYNISPQDLETVFPHGLPPRFVMQVKTFSEACLMVRKPALELLHYLKNTSFAYPAIRYLLYGEKGTGKTLSLCHVIHFCAKQDWLILHIPDAHLWVKNCRDLLQSSYNKQRFDQPLEASTWLKNFKTTNERFLNQIKVQEKYVWNKRESTEKGSPLGEVVEQGITRVRNATDAVGIVLKELKRQSSLGMFHLLVAVDGINALWGRTTLKREDKSPIAPEELALVHNLRKMMKNDWHGGAIVSALSQTGSLFKPRKAYLPQELLGKEGFDALDPFIPILVSNYNPKEFESCIQYYLENNWLQHEKAPTEEGKKELLFLSNANPSLLERHCAYL
Protein: ES/130 (Q07718)
Organism: Gallus gallus (Chicken)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
KIPEQQVTQEVTDSSKDVVVEPAVVPEPIAVESPIAAVSVPPQEKEKPALSPKEKRKKEKKVAKVEPAPSPALASPPASVPKGSPVLEVTPKEVPVVAVPPVGTQQSAPVVSSVPIKKPEALPTHEEQKHDGPVKKKSASKKKAEPAPADSDGPLYLPYKTLVSTISSMAFSEGEAQQLIEILTERAGIVQDTWHTATQKGDPVAVLKRQLEEKEKQLTAEQEDAAAARNKLRELSKELAAEKAKAAASESKLKEQLVTREREITAVQARMQASYQDHVNETQQLQGKIRALQEQLENGPNTQLARLQQENSILRDALNQATSQTESKQNAELAKLRQECNKLMKELSEKSEVLQQEEQQKKSWEIKAAASEKQIEQLQTSQREMEATLQKRLDEVSDELRKTQTSYRSLVADAEKAKGQQQSIAELQAKLLSSETEVKSKLLELDSLKGKLQEASSENTRLLERIKSIEALLEAGRMREAEEDRDLQAANEAEMKQLQLRLQEKTDQLLSLEREAAELREAMEQQKTKNNDLREKNWKAVEALTTVEKACEEKLLAATKAKEELAHQLDVLQTRTKETLLSALPEVTVSQQDYEAWLQEFKEKAVNVLKQHTVMTEPVDSALKLKEAEEAQSTLQAECEQYRAILAETEGMLRDLQKSVEEEEQVWKAKLTVSEEELQKSQLQLKSLEDMIEKLKAELQSTDQLKEYISLLEAQLDKSLADSQL
Protein: Uncharacterized protein (Q587G9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongation factor 2
Sequence:
MVSTRRIAEYKSTATCNCLLSGGISGGWGQFDVVVGCYELSEGSDSSSSHQHQHQNGESNIHVGSLTGLMCERREANQNDTNFVLRERTDGAFKLPSASSLPGIFDLTYSNNNNCLMASCTDGALWVLELRDAAVHESVFPVFDTMLTSCSPFNSETGDQNKWFCTAHKGDVALYDAGMKRIIRRLDGHEYDAWCSATTGAETGVSGGDDGLLRWHDVRMGGKSTVAKMQFDAGVVSISPISTCGTSATTYSLVGSYDEHLYLVDLRSAKRPLSSVHLGGGVWRCSRQLLEEKLTPEAKKAMNYYRWVQECNALAIPVMQNGVALVRYDITSNAEGNFTLLGHLQSSAGSAASDEELPNNALFYDCAVLPGNICSDAVTGDVIGRTIAACDFYNRTVSLWNINDV
Protein: Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 7.1.1.2) (Complex I-23kD) (CI-23kD) (NADH-ubiquinone oxidoreductase 23 kDa subunit) (Q22619)
Organism: Caenorhabditis elegans
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Probable NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 7, mitochondrial
Sequence:
MAMKSVAVLTKGMFGRIPAQLAVSSVPSNTIQKRSNYKFVGMPNETDGTLAGDLNYGLHNVFFTELFRGFGVMLGHVFMEPATINYPFEKGPLSSRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAETRPDGSRRTTRYDIDMTKCIYCGLCQEACPVDAIVEGPNFEYSTETHEELLYNKEKLLLNGDRWEPELASNLQAEYLYR
Protein: Cytoplasmic envelopment protein 3 (O41955)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Subcellular location: Virion tegument {ECO:0000256|HAMAP-Rule:MF_04042}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}. Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}. Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000256|HAMAP-Rule:MF_04042}.
Interaction partners:
Sequence:
MGAAFGCCKKTHNPLKDVRGQLIDLTKDFELISENTGLLVEDPSVGEGHLELKPKPYGSDTDSDTDIEYERGKHA
Protein: CAP, isoform G (CAP, isoform H) (LP11629p) (Q7K1M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Aquaporin-5 (AQP-5) (Q9WTY4)
Organism: Mus musculus (Mouse)
Function: Forms a water-specific channel (By similarity). Plays an important role in fluid secretion in salivary glands. Required for TRPV4 activation by hypotonicity. Together with TRPV4, controls regulatory volume decrease in salivary epithelial cells. Seems to play a redundant role in water transport in the eye, lung and in sweat glands.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:10400615, ECO:0000269|PubMed:12042359, ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18027168, ECO:0000269|PubMed:23473857}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55064}. Cell membrane {ECO:0000250|UniProtKB:P55064}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55064}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23473857}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55064}. Note=Hypotonicity increases location at the cell membrane. Phosphorylation decreases location at the cell membrane. {ECO:0000250|UniProtKB:P55064}.
Interaction partners:
- Aquaporin-12
- Aquaporin-11
- Surfactant protein C
- Uteroglobin
- Keratin, type II cytoskeletal 5
- Aquaporin-7
- Aquaporin-1
- Aquaporin-3
- Pulmonary surfactant-associated protein B
- Aquaporin-9
Sequence:
MKKEVCSVAFFKAVFAEFLATLIFVFFGLGSALKWPSALPTILQISIAFGLAIGTLAQALGPVSGGHINPAITLALLIGNQISLLRAIFYVAAQLVGAIAGAGILYWLAPGNARGNLAVNALSNNTTPGKAVVVELILTFQLALCIFSSTDSRRTSPVGSPALSIGLSVTLGHLVGIYFTGCSMNPARSFGPAVVMNRFSPSHWVFWVGPIVGAVLAAILYFYLLFPSSLSLHDRVAVVKGTYEPEEDWEDHREERKKTIELTAH
Protein: T. brucei spp.-specific protein (Q582K1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MERPADEPQSFLFFFFLCAHLILLTNHRVRETSKKKNSSNPNRRFINGPHVLLFSSPYYNFLCCRCCCFFLYALGKRVISETVCVFFCLFAVSFFFSHINTNLLFILCACFVGLSHIHARKGDIIFLNLKYGCFIVVFFFNHMLTPHRRHVLPLYLLSIFFFFKKPCKIFTYDVCLKIEVKKKTGVVFVGGV
Protein: Cyclin-A2 (Q91ZX8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPGIARQAGSALLSQQEDQENVNPEKVAPAQQPRAQAVLKAGKVRGPAPQQRLKTRRVAPLKDLPINDEHVPTVPSWKAVSKQPAFTIHVDEAEETQKRPAERKETQCEDALAFSAAVSLPGARKPLVPLDYPMDGSFESPHAMDISIVLEDEKPVNVNEVPDYHEDIHTYLGEMEVKCKPKVSYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLFSMSALRGKLQLVGTAAMLLASKFEEIYPPEVAEFV
Protein: UDP-glycosyltransferase 76G1 (EC 2.4.1.-) (Q6VAB4)
Organism: Stevia rebaudiana (Stevia) (Eupatorium rebaudianum)
Function: Involved in the biosynthesis of steviol glycosides in leaves. Converts the di-glycoside steviolbioside to the tri-glycoside rebaudioside B. Converts the tri-glycoside stevioside to the tetra-glycoside rebaudioside A. Converts the tetra-glycoside rebaudioside E to the penta-glycoside rebaudioside D. Converts the penta-glycoside rebaudioside D to the hexa-glycoside rebaudioside M. Can glucosylate rubusoside and rebaudioside A in vitro.
Interaction partners:
Sequence:
MENKTETTVRRRRRIILFPVPFQGHINPILQLANVLYSKGFSITIFHTNFNKPKTSNYPHFTFRFILDNDPQDERISNLPTHGPLAGMRIPIINEHGADELRRELELLMLASEEDEEVSCLITDALWYFAQSVADSLNLRRLVLMTSSLFNFHAHVSLPQFDELGYLDPDDKTRLEEQASGFPMLKVKDIKSAYSNWQILKEILGKMIKQTKASSGVIWNSFKELEESELETVIREIPAPSFLIPLPKHLTASSSSLLDHDRTVFQWLDQQPPSSVLYVSFGSTSEVDEKDFLEIARGLVDSKQSFLWVVRPGFVKGSTWVEPLPDGFLGERGRIVKWVPQQEVLAHGAIGAFWTHSGWNSTLESVCEGVPMIFSDFGLDQPLNARYMSDVLKVGVYLENGWERGEIANAIRRVMVDEEGEYIRQNARVLKQKADVSLMKGGSSYESLESLVSYISSL
Protein: Mas-related G-protein coupled receptor member A3 (Q91WW3)
Organism: Mus musculus (Mouse)
Function: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). Activated by the antimalarial drug chloroquine. Mediates chloroquine-induced itch, in a histamine-independent manner.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Gastrin-releasing peptide receptor
- Transient receptor potential cation channel subfamily A member 1
- Transient receptor potential cation channel subfamily V member 1
- Gastrin-releasing peptide
Sequence:
MNETIPGSIDIETLIPDLMIIIFGLVGLTGNAIVFWLLGFRMHRTAFLVYILNLALADFLFLLCHIINSTVDLLKFTLPKGIFAFCFHTIKRVLYITGLSMLSAISTERCLSVLCPIWYHCRRPEHTSTVMCAVIWVLSLLICILDGYFCGYLDNHYFNYSVCQAWDIFIGAYLMFLFVVLCLSTLALLARLFCGARNMKFTRLFVTIMLTVLVFLLCGLPWGITWFLLFWIAPGVFVLDYSPLLVLTAINSCANPIIYFFVGSFRQRLNKQTLKMVLQKALQDTPETPENMVEMSRNKAEP
Protein: Proteasome assembly chaperone family protein (Q6LWU3)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Interaction partners:
- Proteasome subunit alpha
- Large ribosomal subunit protein eL42
- Phenylalanine--tRNA ligase beta subunit
- Diadenylate cyclase
- non-specific serine/threonine protein kinase
- Conserved hypothetical archaeal protein
- Translation initiation factor 5A
- Small ribosomal subunit protein eS24
Sequence:
MVKIIENKLIDAEPLKDAVLIEGLPGIGHVGRVAAEHIVEEFNGEKVLELYCDDFPPQIVVKNDGTIEYMKNEFYLVKEPVPMVIVLGNTQALSPKGQYVLSEKIVDIAMKYGATKTYTLGGFGIGKISDELKVYVASTSKELSEQHKELGAEFRTDGGSIIGAAGLMLKFSKLKGIEGICLMGETPGYLVDPKSAGNVLEMLSKAIGFEIDMKKLDERAKEMEKFIEKVQMQEQGMQAPQHQDDLSYIG
Protein: Coiled-coil and C2 domain-containing protein 1B (Five prime repressor element under dual repression-binding protein 2) (FRE under dual repression-binding protein 2) (Freud-2) (Q8BRN9)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:21155902}.
Interaction partners:
- Charged multivesicular body protein 7
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 4b
Sequence:
MPGPRPRKGPKTSGQGAETAKQLGLFVEFNPEDMLLGVDETEDDGDLEAELLALTGETASRSRKPAPKGQAPLPMAHIEKLAADCMRDVEEDEEEEGLEDDADLLTELQEVLGEDEEAGLLDGSEAASPDLCEEKTWDNTELPVEQAACQQAVPAAAQAGGPRGLQALLEERIRNYREAAASAKEAGEAAKARRCERGLKTLQSQLATVRKGGKICEDEIPPPVALGKRPPAPQERAIKNPEIDSPGPCAMEPGNLSQPESSLPAIAPLPDSDPDPQALLLARQREYKAAALDAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAPADLKALPQASKASSATQGLSPAVEQMQPVMASDLPATPVAPAEPTTVLDALQQRLNKYREAGIQARANGDERKARMHDRIAKQYQDAVRAHQAGQKVDFAELPVPPGFPPIPGLEPRKGSEQDSVAATLATAQKLASEDAALVDDDEESDTPAQAPLAKKPAQTLVSPSHLLTEPKASSSKESLSPSVREQVTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSPLTDEEGDFILIHHEDLRLSQKAEEVYAQLQKMLQEQQAKCLLFSKQYMHQGNVAETTRFERLAEDRKKQLEILQLAQAQGLDPPSHHFELKTFQTVRIFSELNSTEMHLIIVRGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQSKGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQTVTENWLVLEPRGL