wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication complex GINS protein PSF1 (GINS complex subunit 1) (Q7ZT47)
Organism: Xenopus laevis (African clawed frog)
Function: Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730133}. Chromosome {ECO:0000269|PubMed:12730133}. Note=Associates with chromatin. {ECO:0000269|PubMed:12730133}.
Interaction partners:
- DNA replication complex GINS protein PSF2
- DNA replication complex GINS protein SLD5
- DNA helicase
- DNA polymerase epsilon subunit
- DNA helicase
- Uncharacterized protein.
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- DNA helicase
- Uncharacterized protein.
Sequence:
MFCEKAIELIRELQRASDGQLPAFNEDGIRQILEEMKALYEQNQADVNEAKTEGRSDLIPTIKFRHCCLLRNRRCIVAYLYDRLLRIRALRWEYGSVLPSALRFHMSTEEMDWFNQYKRSLATYMRSLGGEEGLDITQDMKPPKSLYIEVRCLRDYGEFEIDDGTTILLKKNSQHFLPRWKCEQLIRQGVLEHVLS
Protein: Protein phosphatase 1L (EC 3.1.3.16) (Protein phosphatase 1-like) (Protein phosphatase 2C isoform epsilon) (PP2C-epsilon) (Q5SGD2)
Organism: Homo sapiens (Human)
Function: Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Serine beta-lactamase-like protein LACTB, mitochondrial
- Vesicle-associated membrane protein-associated protein A
- Vesicle-associated membrane protein-associated protein B/C
- Serotonin N-acetyltransferase
- Serine/threonine-protein phosphatase 5
- Mitogen-activated protein kinase kinase kinase 7
Sequence:
MIEDTMTLLSLLGRIMRYFLLRPETLFLLCISLALWSYFFHTDEVKTIVKSSRDAVKMVKGKVAEIMQNDRLGGLDVLEAEFSKTWEFKNHNVAVYSIQGRRDHMEDRFEVLTDLANKTHPSIFGIFDGHGGETAAEYVKSRLPEALKQHLQDYEKDKENSVLSYQTILEQQILSIDREMLEKLTVSYDEAGTTCLIALLSDKDLTVANVGDSRGVLCDKDGNAIPLSHDHKPYQLKERKRIKRAGGFISFNGSWRVQGILAMSRSLGDYPLKNLNVVIPDPDILTFDLDKLQPEFMILASDGLWDAFSNEEAVRFIKERLDEPHFGAKSIVLQSFYRGCPDNITVMVVKFRNSSKTEEQ
Protein: Small ribosomal subunit protein uS13m (Small ribosomal subunit protein S13, mitochondrial) (mS13) (Q9CA19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Located at the top of the head of the small subunit, it contacts several helices of the 18S rRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11919680, ECO:0000269|PubMed:11971146}.
Interaction partners:
- Small ribosomal subunit protein uS19m
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS2m
- 50S ribosomal protein L33
- Small ribosomal subunit protein uS12m
- Ribosomal protein S12
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
Sequence:
MLGLRRSATTLFDISQSLLRNVTFHGLRVQGIRVGNAEVPNNKPLKTGLQEVYGIGRRKSHQVLCHLGITNKLARDLTGKELIDLREEVGQHQHGDELRRRVGSEIQRLVEVDCYRGSRHRHGLPCRGQRTSTNARTKKGKAVAIAGKKKAPRK
Protein: 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) (A0A096MJY6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAPAAPAAEEKGSEAQLKAALADVPELGRLLEIDPYLKPYAADFQRRYKKFNQVLHDIGENEGGIDKFSRGYESFGIHRCSDGGIYCKEWAPGAEGVFLTGEFSGWNPFSHPYKKLEYGKWELYIPPKQNKSPPIPHGSKLKVVITSKSGEILYRISPWAKYVVRENNNVNYDWIHWDPENPYKFRHSRPKKPRSLRIYESHVGISSHEGKIASYKHFTSNVLPRIKDLGYNCIQLMAIMEHAYYASFGYQVTSFFAASSRYGTPEELKELVDTAHLMGIVVLLDVVHSHASKNSEDGLNMFDGTDSCYFHSGPRGTHDLWDSRLFIYSSWEVLRFLLSNIRWWLEEYCFDGFRFDGVTSMLYHHHGMGQGFSGDYSEYFGLQVDEDALVYLMLANHLTHTMYPDSITIAEDVSGMPALCSPTSQGGGGFDYRLAMAIPDKWIQLLKEFKDEDWNMGNIVYTLTNRRHLEKCVAYAESHDQALVGDKTLAFWLMDAEMYTNMSVLAPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGKYPEWLDFPRKGNNESYHYARRQFNLTDDDLLRYKFLNNFDRDMNRLEETCGWLSAPQAYVSEKHEGNKTITFERAGLLFIFNFHPSKSYTDYRVGTAMPGKYPFLCQ
Protein: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28) (Cold shock protein CSI14) (P39071)
Organism: Bacillus subtilis (strain 168)
Subcellular location: Cytoplasm.
Interaction partners:
- Isochorismate synthase DhbC
- Dimodular nonribosomal peptide synthase
- 2,3-dihydroxybenzoate-AMP ligase
- Isochorismatase
- Ferri-bacillibactin esterase BesA
- Uncharacterized protein YbdZ
- Probable flavodoxin 1
- D-alanine--D-alanyl carrier protein ligase
- Probable flavodoxin 2
- Iron-uptake system-binding protein
Sequence:
MNAKGIEGKIAFITGAAQGIGEAVARTLASQGAHIAAVDYNPEKLEKVVSSLKAEGRHAEAFPADVRDSAAIDEITARIEREMGPIDILVNVAGVLRPGLIHSLSDEEWEATFSVNSTGVFNASRSVSKYMMDRRSGSIVTVGSNAAGVPRTSMAAYASSKAAAVMFTKCLGLELAEYNIRCNIVSPGSTETDMQWSLWADENGAEQVIKGSLETFKTGIPLKKLAKPSDIADAVLFLVSGQAGHITMHNLCVDGGATLGV
Protein: Cruzioseptin-3 (CZS-3) (A0A193H2X2)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity against Gram-negative bacterium E.coli (MIC=13.32 uM), aginst Gram-positive bacterium S.aureus (MIC=13.32 uM) and against fungus C.albicans (MIC=13.32 uM). At higher concentrations also has a bactericidal and fungicidal effect. Has hemagglutinating activity against horse erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
KRGFLDVVKHIGKAALGAVTHLINQGEQ
Protein: Ovule protein (Q17786)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGHSQSYDLRNPEGGEKTPVRGVRRVSREHQTDAQFSTETAEPFDFREDELRDRIRREQLRKREVELETLRIRQHESREPIIDAYRQNQPAPQGNLYNEFNHYDSMKHASPSDPATYFALKPMTEVNEGRQFSIPTSSTRRYDQVPIDPSPELQRREVPSKQSPPNYPKRSSVFGGRVSPLPRQSEVDPHPMPRYIPPMSPSNPIDDVPPTHVSELHAEKRMIVGIDDELQPEKNNVTYVTVATAAIDNELLHRHPEVGRHPVYVLPAQTSYGASAKRRSSDDEAKNVLPPQNCTVEHCTHVAVNDGSPVVIRKRASQDSIRDKENRLTIPINEDDTENVGEGTNYQNVSKKCFEERLHYDSYMPTLSLRQRPVVSFYDKLH
Protein: Cyclic nucleotide-gated ion channel 4 (AtCNGC4) (Cyclic nucleotide- and calmodulin-regulated ion channel 4) (AtHLM1) (Q94AS9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and sodium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Might constitute a common downstream component of the signaling pathways leading to hypersensitive response (HR).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Calmodulin-7
- Serine/threonine-protein kinase BIK1
- Glutamate receptor 3.3
- Cyclic nucleotide-gated ion channel 2
Sequence:
MATEQEFTRASRFSRDSSSVGYYSEEDNTEEEDEEEEEMEEIEEEEEEEEEEDPRIGLTCGGRRNGSSNNNKWMMLGRILDPRSKWVREWNKVFLLVCATGLFVDPLFLYTLSVSDTCMCLLVDGWLALTVTALRSMTDLLHLWNIWIQFKIARRWPYPGGDSDGDTNKGGGTRGSTRVAPPYVKKNGFFFDLFVILPLPQVVLWVVIPSLLKRGSVTLVVSVLLVTFLFQYLPKIYHSIRHLRRNATLSGYIFGTVWWGIALNMIAYFVAAHAAGACWYLLGVQRSAKCLKEQCENTIGCDLRMLSCKEPVYYGTTVMVLDRARLAWAQNHQARSVCLDINTNYTYGAYQWTIQLVSSESRLEKILFPIFWGLMTLSTFGNLESTTEWSEVVFNIIVLTSGLLLVTMLIGNIKVFLHATTSKKQAMHLKMRNIEWWMKKRHLPIGFRQRVRNYERQRWAAMRGVDECEMVQNLPEGLRRDIKYHLCLDLVRQVPLFQHMDDLVLENICDRVKSLIFTKGETIQKEGDAVQRMLFVVRGHLQSSQLLRDGVKSCCMLGPGNFSGDELLSWCLRRPFVERLPPSSSTLVTLETTEAFGLDAEDVKYVTQHFRYTFVNEKVKRSARYYSPGWRTWAAVAVQLAWRRYKHRLTLTSLSFIRPRRPLSRCASLGEDKLRLYAAILTSPKPNPDDFDDY
Protein: Sphingolipid C4-hydroxylase SUR2 (EC 1.-.-.-) (Syringomycin response protein 2) (P38992)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Catalyzes the conversion of sphinganine to phytosphingosine in sphingolipid biosynthesis. Involved in the response to syringomycin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8868422}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Sphingoid long chain base kinase 4
- Ceramide synthase LAC1
- 3-ketodihydrosphingosine reductase TSC10
- Ceramide very long chain fatty acid hydroxylase SCS7
- Ceramide synthase LAG1
- Alkaline ceramidase YPC1
- Alkaline ceramidase YDC1
- Sphingoid long chain base kinase 5
- Dihydrosphingosine 1-phosphate phosphatase YSR3
Sequence:
MNVTSNATAAGSFPLAFGLKTSFGFMHYAKAPAINLRPKESLLPEMSDGVLALVAPVVAYWALSGIFHVIDTFHLAEKYRIHPSEEVAKRNKASRMHVFLEVILQHIIQTIVGLIFMHFEPIYMTGFEENAMWKLRADLPRIIPDAAIYYGYMYGMSALKIFAGFLFVDTWQYFLHRLMHMNKTLYKWFHSVHHELYVPYAYGALFNNPVEGFLLDTLGTGIAMTLTHLTHREQIILFTFATMKTVDDHCGYALPLDPFQWLFPNNAVYHDIHHQQFGIKTNFAQPFFTFWDNLFQTNFKGFEEYQKKQRRVTIDKYKEFLQERELEKKEKLKNFKAMNAAENEVKKEK
Protein: Vinexin (SH3-containing adapter molecule 1) (SCAM-1) (Sorbin and SH3 domain-containing protein 3) (O60504)
Organism: Homo sapiens (Human)
Function: Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain.
Subcellular location: [Isoform Alpha]: Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cell junction {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites, vinexin beta was also found in the nucleus. {ECO:0000250}.
Interaction partners:
- Vinculin
- Talin-1
- Disks large homolog 5
- Paxillin
- Scaffold attachment factor B2
- Sorbin and SH3 domain-containing protein 1
- Integrin alpha-1
- Integrin beta-5
- Vacuolar protein sorting-associated protein VTA1 homolog
- GTP cyclohydrolase 1
Sequence:
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVKYEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQQRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEESWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSPKSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPSSTRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEHICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSARHPSSPSALRSPADPIDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPLDLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
Protein: Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein) (Q9Z2Y8)
Organism: Mus musculus (Mouse)
Function: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Interaction partners:
- Purine nucleoside phosphorylase LACC1
- Pyridoxal kinase
- Pyridoxine-5'-phosphate oxidase
- Erlin-2
Sequence:
MLRGGSMTAELGVGFALRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYVQELLEKASNPKILSSCPEIKWHFIGHLQKQNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGSFGHDLSQGPNPDFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFGERDYSKKPALDKTADAKASVPLVQGH
Protein: 2'-5' oligoadenylate synthase (EC 2.7.7.84) (Q05BJ7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEHGLRSIPAWTLDKFIEDYLLPDTTFGADVKSAVNVVCDFLKERCFQGAAHPVRVSKVVKGGSSGKGTTLKGRSDADLVVFLNNLTSFEDQLNRRGEFIKEIKKQLYEVQHERRFRVKFEVQSSWWPNARSLSFKLSAPHLHQEVEFDVLPAFDVLGHGSINKKPNPLIYTILIWECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLVRHRPSHCGLHLYRV
Protein: YTH domain-containing family protein (Q9FPE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Octicosapeptide/Phox/Bem1p family protein
- FKBP12-interacting protein of 37 kDa
- E3 ubiquitin-protein ligase HAKAI homolog
- DNA oxidative demethylase ALKBH2
- DExH-box ATP-dependent RNA helicase DExH10
- Uncharacterized protein
- At1g67210
- Protein RECOGNITION OF PERONOSPORA PARASITICA 7
- DExH-box ATP-dependent RNA helicase DExH9
- Proline transporter 2
Sequence:
MTSHVPKHPRKSFEDMVKNLKVDPLAKVTASTTSMVSAKENKNQSEAEPSYYETLETYQGLPCPYGGYYGYYYPGLDGSVGEAKDNGYYGYGTEVQYPVMQGENGSVIYLMPGFQSYDASQTYMPINPVGVSSQALHSPMYAAQGYYQNQFGYADVSSPTYLWDPVGDRYVYGVASYTPPLKQNISSSSHNHNNYYSKSKNSFTGHGMGDRPKTPRKASQNSYAPPPLLNQEKGRIAYPMDPVKKKSGALNRDETEKAKARTKENGTSMNDLANGQDHITNGECESCSLDAEGNERSNGVGSVIRRDQYNLPSFQTKYEEAIFFVIKSYSEDDIHKSIKYNVWSSTLNGNKKLDSAYQESQKKAADKSGKCPVFLFFSVNASGQFCGVAEMIGRVDYEKSMEFWQQDKWTGYFPVKWHIIKDVPNPQLRHIILENNENKPVTNSRDTQEVRLPQGNEVLNIFKNYAAKTSILDDFDFYENREKVMVQKKLRFPPVLKKKEEDLVADFKTMEMSNTVEEGNTELTGTVS
Protein: Delta-type opioid receptor (D-OR-1) (DOR-1) (K56) (MSL-2) (P32300)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1334555, ECO:0000269|PubMed:1335167, ECO:0000269|PubMed:18836069, ECO:0000269|PubMed:22596164}; Multi-pass membrane protein {ECO:0000269|PubMed:10677041, ECO:0000269|PubMed:1334555, ECO:0000269|PubMed:1335167, ECO:0000269|PubMed:22596164}.
Interaction partners:
- Proenkephalin-A
- Pro-opiomelanocortin
- Proenkephalin-B
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Kininogen-1
- HMW kininogen-II
- Prepronociceptin
- Mu-type opioid receptor
Sequence:
MELVPSARAELQSSPLVNLSDAFPSAFPSAGANASGSPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKLKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTQPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDINRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRTPCGRQEPGSLRRPRQATTRERVTACTPSDGPGGGAAA
Protein: Conditioned medium factor (CMF) (Density-sensing factor) (P34090)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cell density sensing and might synchronize the onset of development by triggering aggregation when a majority of the cells in a given area have starved.
Interaction partners:
- Conditioned medium factor receptor 1
- Cyclic AMP receptor 1
Sequence:
MRLLLLLILIITINFSYGVLTPKNLAGEASEFGSFNIPNPMDVAQSSDSSLFGISMTQSQLKNSFEWSGVVPVDSEEEFTLTFFSSFPLSEFKVEASPKTSLSSSKSESEHKSKFYKVIKSIYQTPTVTNGSFGIDGATTPSFSLTWDKPVVGDWNVVITASSSLRKNEKFQKMVEDSTPQLLMLVQNPSDTHIYSYVSSYNNLFTGQKVSVLAMLHKKSEFIKKSSANRPLNWKPSPILLSDVSAEMILGLPDGSKETIPMFDDGLHDDEQANDGLFGGYINVSELGNYDLQVVYKGSQNGNGVIRSNQHLIPITSQYLELTGEVQSVQDGDANLNIYFIVNSPNQTTVDQTPVHVYSEVYGTDDDGKKVAIAWVAGVTSAQPIQGSTTTFALSAVLNERWIAKVGATAPFFVKNVQVSDLDTFIPLSNTTSTSNVKMVGEYKDVRTIVHSPPLHEITKEMRDGKMPKELADRIGKSTGNGKLILTHGYCSEGVWPIEDFENSVEFQDFNQNRGNDEFAQILANFGSQYTDGFSLVAHSQGGNAALHLVTFYFSGLDLSQKLEGRVIQSMGTPYQGTALAGTWASIGSAVGVGCSANDDLTVDGAALWLKSIPADKRALVYYTTTQYSTGSLINYCNLASNAVLEWPNDGVVDNEHTPLEGGVYLNNFKDWCHSDGMHSPQQTTNTEYNKEMSSNSVW
Protein: MCP-type signal transduction protein (Q0PB65)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- Chemotaxis protein
- histidine kinase
- DUF465 domain-containing protein
- Chemotaxis protein
- protein-glutamate methylesterase
- Chemotaxis protein methyltransferase
- Histidine phosphotransferase
- FIST domain-containing protein
Sequence:
MFGSKINHSDLQKLEEENKNLTHKIEKFQSENLELKNKITSLEQAALESKLKTDLLNVLLTGVLKNITIIQGDMLENVNKAEVISSYSKTSLAEMDELNHIANSINASLGNITESANKTRDVAGTLHRSVDEITNVINLIKDVSDQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEKTQKATTEVEMNINLLKQNANEMYTQSEQVEKISIDSNAHIMSFSEKFTHLVNEAHSTNSNAVGIASEAFVSLAKLDHIAFKLNGYKEIFSKSGKQLADHTSCRLGKWLASTGKERFGQNKSFLKINEPHEKVHENMNNAITIANTEDISKDITQHSIINKCEVAENASLDLFNVFKEMLDESDH
Protein: ATP-binding cassette sub-family B member 10, mitochondrial (ATP-binding cassette, sub-family B (MDR/TAP), member 10) (F1Q5K6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ferrochelatase
- Mitoferrin-1
- Mitoferrin-2
- Transmembrane protein 14C
- Protoheme IX farnesyltransferase, mitochondrial
- STEAP family member 3, metalloreductase.
- Mitochondrial glutathione transporter SLC25A39
- Transferrin receptor protein 1
Sequence:
MYGTMLRMTGFAIGKLQQCSITCCRSSTFHHWSTRTSRTWSRQVRKNGSFDICVLPVYKGRNISKLSCLRTEGLFSPKHSRHIVALYSTSTDSNQTSKSVVNQESSAKTTADSLPVPSEDVKKLLQLAHPQRWRLTAAVGFLVISSTVTMSAPFFLGKVIDTIYTSPTEDFSSSLTSLCLMLTGVFLCGGAANAARVYLMQISGQQIVRKLRESLFSSILKQELGFFDKTRTGELINRLSADTAIVGRCLTDNLSDGLRSLAQAGAGVGMMLYVSPSLAAFVLMVVPPIACLAVIFGRFLRSISRRTQDALAEATQLAEERISNLRTVRAFGKELTEVQKYSQKVDHIFELAKKEAVVSAGFYGVTGLSGNVIILSVLYKGGLLMASEAMTVGQLSSFLMYAFWVGISIAGFSSFYSELMKGLGAGTRLWELIDRKPEFPLNEGLVLTSELLKGELEFRNVSFAYPTRKDSPIFQDLSLHVPAGSVLAVVGSSGSGKSSLVSLLLRLYDPDSGIVSVDGHDIRDLNPYWLRSHIGTVSQEPVLFSCSIAENIAYGAPDPSQVTVEDIYRAAQIANAHDFIQEFPKGYDTVVGEKGVLLSGGQKQRVAIARALLKNPKILLLDEATSALDAENEFLVQEALERLMDGRTVLIIAHRLSTIQSADSVAVLDQHRVMEIGSHSQLLANDQGLFRKLMEKQAFLQAEQKQALLK
Protein: Endonuclease III homolog 1, chloroplastic (AtNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Q9SIC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:19372224}.
Interaction partners:
- N-glycosylase/DNA lyase OGG1
- Formamidopyrimidine-DNA glycosylase
- DNA-
- DNA-repair protein XRCC1
- Uridine 5'-monophosphate synthase
- Endonuclease III homolog 2, chloroplastic
- Transcription factor bHLH140
- Putative DNA glycosylase At3g47830
- Polynucleotide 3'-phosphatase ZDP
- DNA-
Sequence:
MILLVNGGAATSIHPNAARFYRIGTMSRQIHGAVSSSKHISLKTQHPLSDSNSELAYGASGSETRVYTRKKRLKQEPFEPLEKYSGKGVNTHKLCGLPDIEDFAYKKTIGSPSSSRSTETSITVTSVKTAGYPPENWVEVLEGIRQMRSSEDAPVDSMGCDKAGSFLPPTERRFAVLLGALLSSQTKDQVNNAAIHRLHQNGLLTPEAVDKADESTIKELIYPVGFYTRKATYMKKIARICLVKYDGDIPSSLDDLLSLPGIGPKMAHLILHIAWNDVQGICVDTHVHRICNRLGWVSRPGTKQKTTSPEETRVALQQWLPKEEWVAINPLLVGFGQMICTPIRPRCEACSVSKLCPAAFKETSSPSSKLKKSNRSKEP
Protein: Uncharacterized protein C354.08c (O43022)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as an osmosensitive calcium-permeable cation channel.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to the cell tip and the barrier septum.
Interaction partners:
- ATP synthase protein 8
- Cytochrome c oxidase subunit 1
Sequence:
MVIEKRESFIEVVINSLLNDNPAQAKFDKYSILVSLGFSSLLSVILLCIFTLLRTKFNTYDRCIPPMKKSLWGWIEPLWSIKVEDCLYNMGADAVISLLFSRFCRDVFLILAAICCTILIPINIVATNKTLANSDSQNAYAKLSIQNVTGNWTWAHVVICYVFNVLVLFLLARYYQIVMRIRQRYYRSPTYQQSMSSRSLLIMDIPTTMRSNNGLSILASRLKSSEAPMHVHICHAIKNLPKILKKHDNAVRSLEAVLAKFFKNPKKLPDDRPVRRVKQGLLTSEKVDAIDYYSAKIENYGLRVDAARESLYENEFEHYGFITYKSSYIAHDTARHNSRVAGASVSMAPEPSDFLWDNLSLAWSTRLFNRMIGNILFIILIIAWIIETALVAIFISNLYHLGSVWPWLQQQLTSRSGFWSIVQGILSPAVAGFTFMILEIIMRRISYWQGSFTKSSRERGVLNKLHIIFTLDNFIIYTLMAVFWRLGVIIAYKTKEEGNFAEGMSAFATFDTVGLSVSSFVQFSTFWIMFIAHSTCSFFVEIAQPITLTIRLIKTKFFSPTPRDLLEWTAPTKYVYSQVLNKLIYFFTIAICYACINPLVLLFASVLFCVNYLTQKYILMYVSNSSTESGGGYWRPVVNRILLGLELANIILFLCLWVQGGRVRAYCIIPNFSFAIAFKIWCMFALDPKSHYMIEDPYMKVVEPLENEISESEMCFGHPSTYAPLLVPMVRSDARALLPLFYSGRTETHNKFDFATDSDDASEKHLRGEEEPLENVDFVDIDNVDTAKEVHDQQQVQQLKKNLSRSYTRSRGVSLRARLNEEELPLTESITQDSQISIPETLESQSTEITPINVSEHYDKYYHIF
Protein: Chondroitin sulfate proteoglycan 5 (Acidic leucine-rich EGF-like domain-containing brain protein) (Neuroglycan C) (Q71M36)
Organism: Mus musculus (Mouse)
Function: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Synaptic cell membrane {ECO:0000269|PubMed:21183079}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:12885772}; Single-pass type I membrane protein {ECO:0000305}. Cell surface {ECO:0000269|PubMed:15331613}. Secreted {ECO:0000250|UniProtKB:O95196}. Note=Partially enriched in lipid rafts (By similarity). Also detected in the endoplasmic reticulum and the Golgi (PubMed:10617623). {ECO:0000250|UniProtKB:Q9ERQ6, ECO:0000269|PubMed:10617623}.
Interaction partners:
- Neurocan core protein
- Receptor-type tyrosine-protein phosphatase zeta
Sequence:
MGRAGGGGPDWGPPPVLLLLGVTLVLTAGAVPARETGSAIEAEELVRSSLAWESRANDTREEAGLPAAGEDETSWTERGSEMAAVGPGVGPEEALEASAAVTGTAWLEADGPGLGGVTAEAGSGDAQTLPATLQAPDEALGSSTMPPAIPEATETSGPPSPAVHDKPSVGPELPKEIPLEVRLNLGGSTPEPTFPLQGTLETQPASDIIDIDYFEGLDSEGRGADMGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLEEEEEEEEDKDTVGGGDLEDENDLLLPSQKPGVGPGTGQPTNRWHAVPPQHTLGMVPGSSISLRPRPGDPGKDLASGENGTECRVGFVRHNGSCRSVCDLFPSYCHNGGQCYLVENIGAFCRCNTQDYIWHKGMRCESIITDFQVMCVAVGSAALVLLLLFMMTVFFAKKLYLLKTENTKLRRTNKFRTPSELHNDNFSLSTIAEGSHPNVRKFCDTPRVSSPHARALAHYDNIVCQDDPSAPHKIQDPLKSRLKEEESFNIQNSMSPKLEGGKGDQDDLGVNCLQNNLT
Protein: BHLH transcription factor (Os09g0475400 protein) (Q69JI7)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Os03g0726900 protein
Sequence:
MGIQGNKATTREHDFLSLYTTAAKDPSLQLHDAKPPPPSQGFFLRTHDFLQPLEKPTPAPTPPPTSQLQQQQQQAFPGGIGTFSISHVAGARPVAAAVVKAEPTPFVLWGQPAAAAAAHPVAALGHHHHHHQWTLPFAGVGQVAATAARQQQEWKGRVGGGGFMDSGSRSSGGAGFDDDDGVAARREVSSSLKELTVRVDGKGGSCSGSGTDQRPSSPRSKHSATEQRRRSKINDRFQILRELLPHSDQKRDKATFLLEVIEYIRFLQEKVQKFEASVPEWNQENAKILPWSNIYFRSFWKNSQSKGQNPGDDLPDPSQFIRNGSSSGYNFTGKPDDNHNMVTSAAASGAQELVETDHAASVSYRSAETPTNITNNVTSQAQAQWASPAGVDDCAMNSEMLNNQQLAIDEGTISLSSQYSQQLLGTLTHALESSGVDLSQSSISVQINLGKRAVKRPGADGSSSSKELPSTSANNENMGHQLTMLGGGTEELPHPTKRHKSGNS