wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipase A1 EG1, chloroplastic/mitochondrial (EC 3.1.1.32) (Protein EXTRA GLUME 1) (Q8S1D9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Phospholipase that releases free fatty acids from phospholipids. Catalyzes the initial step of jasmonate (JA) biosynthesis. Required for the biosynthesis of endogenous JA in seedling, inflorescence and spikelets. Not essential for JA biosynthesis after wounding. Mediates spikelet development and specification of empty-glume identity. Functions in a high temperature-dependent manner to maintain floral developmental robustness under heat stress conditions. Functions by safeguarding the expression of several floral identity genes, such as MADS1, MADS6 and G1.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:27367609}. Plastid, chloroplast {ECO:0000269|PubMed:24647160}. Note=Localizes predominantly in mitochondrion. {ECO:0000269|PubMed:27367609}.
Interaction partners:
Sequence:
MTLPRQCAAACRTGGGGGGVVRCRAVAAAGGAVAVRDAVVAPVARRGAARKTAETVAGMWREVQGCGDWEGMLEPAPHPVLRGEVARYGELVGACYKAFDLDPASRRYLNCKYGRERMLEEVGMGGAGYEVTRYIYAAADVSVPTMEPSTSGRGRWIGYVAVSTDEMSRRLGRRDVLVSFRGTVTPAEWMANLMSSLEAARLDPCDPRPDVKVESGFLSLYTSADKTCRFGGAGSCREQLLREVSRLVAAYSGGGEDVSVTLAGHSMGSALALLSAYDLAELGLNRAAPVTVFSFGGPRVGNAAFKARCDELGVKALRVTNVHDPITKLPGVFLNEATAGVLRPWRHSCYTHVGVELPLDFFKVGDLASVHDLATYISLLRGADKKQPAAAAADAGGVLAKVMDFVGRRRGGGALPWHDAAMIQMGGLVQTLGLI
Protein: Lysine-specific demethylase JMJ703 (EC 1.14.11.67) (Jumonji domain-containing protein 703) (Lysine-specific histone demethylase JMJ703) (Protein JUMONJI 703) ([histone H3]-trimethyl-L-lysine(4) demethylase JMJ703) (Q53WJ1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3, H3K4me2 and H3K4me1. No activity on H3K9me3/2/1, H3K27me3/2/1 and H3K36me3/2/1. Involved in the control of stem elongation by regulating methylation states of H3K4me3 on cytokinin oxidase (CKX) gene family, which may cause increased expression of CKX genes and reduced cytokinin levels. Prevents ectopic retrotransposition by regulating the levels of H3K4me3 in two non-LTR retrotransposons KARMA and LINE-1 (L1) and reinforcing their repressed states.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:23319643, ECO:0000269|PubMed:23357881}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit alpha
- F-ATPase protein 6
- ATP synthase subunit a
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit d
- Os06g0646500 protein
- Os02g0750100 protein
- ATP synthase F1, delta subunit family protein, expressed
Sequence:
MMGVTTTLNEDTEPSIPPGFGPFATLPLWGIHNDAKPAVTHSTPVQALQSIRKDSEECQPSAAVSRSDTPCSTSGTQTCRKSLRNRPPIDYSRFEHISDEDSDVEIVEKDVSSTRRRQQLPKGVLRGCAECSDCQKVIAKWNPAGARRPVLDEAPVFYPTEEEFEDTLKYIESIRPMAEPYGICRIVPPSSWKPPCLLKDKSIWEGSKFSTRVQKVDKLQNRKSSKKGRRGGMMKRRKLAESEENSATAHTQTGMQQSPERFGFEPGPEFTLQTFQKYADDFSKQYFRKDTSMDSVPSVEDIEGEYWRIVEVPTEEIEVIYGADLETGTFGSGFPKLSPETKSDAEDKYAQSGWNLNNLPRLQGSVLSFEGGDISGVLVPWVYVGMCFSSFCWHVEDHHLYSLNYMHWGAPKLWYGVPGKDAVNLESAMRKHLPELFEEQPDLLHNLVTQFSPSLLKSEGVHVYRCVQHEGEFVLTFPRAYHAGFNCGFNCAEAVNVAPIDWLPIGHNAVELYREQARKITISHDKLLLGAAREAIRAQWDILFLKRNTADNMRWKSICGADSTIFKALKARIETELVQRKTLGVPAQSRKMDAEFDSIDRECALCYYDLHLSASGCPCCPEKYACLVHAKQLCSCDWDKRFFLFRYDVNELNILADALGGKLSAIHRWGVSDLGLSLSSCVKREKVQDSKTVRRLTDGPRRSYMSQASAVSLVSSSTSNEQKDEGNKIMKIASPQTNNVCPSVEQRKSENISPLKEPCVRNELSCTTNSDSNGLQYNGGLGGHKGSAPGLPVSSSPSFSSNVATRPISTSSVSMKIVQGLVASKSCIQASSRTGDSRSLLGEHHNRSPAMIHDGTNMKSSLESSNNSCRLIASDYNATPCHSSKDQVLVTPGTNASVVTLKDSSQVHSASSQQFVRTGPWTQSASHEASSPSTSALKPSLDPPAMKNLYGGFTQGSAHPGPPSFSNQQPNDGRLQRTSESLPGVEARARGHPTVTAQPALEIHSRNGGAQKGPRIANVVHRFKCSVEPLEIGVVLSGRLWSSSQAIFPKGFRSRVKYFSIVDPIQMAYYISEILDAGMQGPLFMVKLENCPGEVFINLSPTKCWNMVRERLNMEIRRQLNMGKSNLPTLQPPGSVDGLEMFGLLSPPIVQAIWARDRDHICTEYWRSRPHVLIEDPNNRHMLSQGPPLLALRGLIQRANRDELQVLRSLMTNSNNLDDSSRQQAAHIIEEEIAKQLC
Protein: Protein-L-histidine N-pros-methyltransferase (EC 2.1.1.-) (DORA reverse strand protein) (DREV) (DREV1) (Methyltransferase-like protein 9) (hMETTL9) (Q9H1A3)
Organism: Homo sapiens (Human)
Function: Protein-histidine N-methyltransferase that specifically catalyzes 1-methylhistidine (pros-methylhistidine) methylation of target proteins. Mediates methylation of proteins with a His-x-His (HxH) motif (where 'x' is preferably a small amino acid). Catalyzes methylation of target proteins such as S100A9, NDUFB3, SLC39A5, SLC39A7, ARMC6 and DNAJB12; 1-methylhistidine modification may affect the binding of zinc and other metals to its target proteins. Constitutes the main methyltransferase for the 1-methylhistidine modification in cell.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:34562450, ECO:0000305|PubMed:33563959}. Mitochondrion {ECO:0000305|PubMed:33563959}. Note=Colocalizes with membranous compartments such as the endoplasmic reticulum and mitochondria. {ECO:0000269|PubMed:33563959}.
Interaction partners:
- Immunoglobulin superfamily member 6
- Probable methyltransferase-like protein 25
Sequence:
MRLLAGWLCLSLASVWLARRMWTLRSPLTRSLYVNMTSGPGGPAAAAGGRKENHQWYVCNREKLCESLQAVFVQSYLDQGTQIFLNNSIEKSGWLFIQLYHSFVSSVFSLFMSRTSINGLLGRGSMFVFSPDQFQRLLKINPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKKKYRVLGINEWQNTGFQYDVISCLNLLDRCDQPLTLLKDIRSVLEPTRGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWEEQVNSLPEVFRKAGFVIEAFTRLPYLCEGDMYNDYYVLDDAVFVLKPV
Protein: Glutaredoxin 4 (Grx4) (Monothiol glutaredoxin) (P0AC69)
Organism: Escherichia coli (strain K12)
Function: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15833738}.
Interaction partners:
- DNA-binding transcriptional regulator BolA
- Acid stress protein IbaG
- Glutaredoxin 3
- Fe/S biogenesis protein NfuA
- Glutaredoxin 1
- 4-hydroxybenzoate octaprenyltransferase
- Transcriptional regulator SlyA
- Iron-sulfur cluster insertion protein ErpA
- Iron-sulfur cluster assembly scaffold protein IscU
- Iron-sulfur cluster assembly protein SufB
Sequence:
MSTTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALAACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLIKETAAKYKSEEPDAE
Protein: Cytochrome P450 2B12 (EC 1.14.14.1) (CYPIIB12) (P33272)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. This isozyme seems responsible for metabolism of 2,2',4,4',5,5'-hexachlorobiphenyl.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 2U1
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 2E1
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Polyunsaturated fatty acid 5-lipoxygenase
- Arachidonate 12-lipoxygenase, 12R-type
- Cytochrome P450 7A1
- UDP-glucuronosyltransferase 1A1
Sequence:
MEFGVLLLLTLTVGFLLFLVSQSQPKTHGHLPPGPRPLPFLGNLLQMNRRGFLNSFMQLQEKYGDVFTVHLGPRPVVILCGTDTIREALVDQAEAFSGRGTVAVLHPVVQGYGVIFATGERWKTLRRFSLVTMKEFGMGKRSVDERIKEEAQCLVEELKKYKGAPLNPTFLFQSIAANTICSIVFGERFDYKDHQFLHLLDLVYKTSVLMGSLSSQVFELYSGFLKYFPGAHKQIFKNLQEMLNYIGHIVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFNHQNLVISVLSLFFAGTETTSTTLRCTFLIMLKYPHVAEKVQKEIDQVIGSHRLPTPDDRTKMPYTDAVIHEIQRFADLTPIGLPHRVTKDTVFRGYLLPKNTEVYPILSSALHDPRYFEQPDTFNPEHFLDANGALKKSEAFLPFSTGKRICLGEGIARNELFIFFTAILQNFTLASPVAPEDIDLTPINIGVGKIPSPYQINFLSR
Protein: No mechanoreceptor potential C isoform L (No mechanoreceptor potential C, isoform E) (E0A9E1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSQPRGGRGGGRGGGVGRKTPSSLTGPPDESATPSERATPASKADSDPKDDSSSNGDKKDMDLFPAPKPPSAGASIRDTANKVLGLAMKSEWTPIEAELKKLEKYVANVGEDGNHIPLAGVHDMNTGMTPLMYATKDNKTAIMDRMIELGADVGARNNDNYNVLHIAAMYSREDVVKLLLTKRGVDPFSTGGSRSQTAVHLVSSRQTGTATNILRALLAAAGKDIRLKADGRGKIPLLLAVESGNQSMCRELLAAQTAEQLKATTANGDTALHLAARRRDVDMVRILVDYGTNVDTQNGEGQTPLHIAAAEGDEALLKYFYGVRASASIADNQDRTPMHLAAENGHAHVIEILADKFKASIFERTKDGSTLMHIASLNGHAECATMLFKKGVYLHMPNKDGARSIHTAAAYGHTGIINTLLQKGEKVDVTTNDNYTALHIAVESAKPAVVETLLGFGADVHVRGGKLRETPLHIAARVKDGDRCALMLLKSGASPNLTTDDCLTPVHVAARHGNLATLMQLLEDEGDPLYKSNTGETPLHMACRACHPDIVRHLIETVKEKHGPDKATTYINSVNEDGATALHYTCQITKEEVKIPESDKQIVRMLLENGADVTLQTKTALETAFHYCAVAGNNDVLMEMISHMNPTDIQKAMNRQSSVGWTPLLIACHRGHMELVNNLLANHARVDVFDTEGRSALHLAAERGYLHVCDALLTNKAFINSKSRVGRTALHLAAMNGFTHLVKFLIKDHNAVIDILTLRKQTPLHLAAASGQMEVCQLLLELGANIDATDDLGQKPIHVAAQNNYSEVAKLFLQQHPSLVNATSKDGNTCAHIAAMQGSVKVIEELMKFDRSGVISARNKLTDATPLQLAAEGGHADVVKALVRAGASCTEENKAGFTAVHLAAQNGHGQVLDVLKSTNSLRINSKKLGLTPLHVAAYYGQADTVRELLTSVPATVKSETPTGQSLFGDLGTESGMTPLHLAAFSGNENVVRLLLNSAGVQVDAATIENGYNPLHLACFGGHMSVVGLLLSRSAELLQSQDRNGRTGLHIAAMHGHIQMVEILLGQGAEINATDRNGWTPLHCAAKAGHLEVVKLLCEAGASPKSETNYGCAAIWFAASEGHNEVLRYLMNKEHDTYGLMEDKRFVYNLMVVSKNHNNKPIQEFVLVSPAPVDTAAKLSNIYIVLSTKEKERAKDLVAAGKQCEAMATELLALAAGSDSAGKILQATDKRNVEFLDVLIENEQKEVIAHTVVQRYLQELWHGSLTWASWKILLLLVAFIVCPPVWIGFTFPMGHKFNKVPIIKFMSYLTSHIYLMIHLSIVGITPIYPVLRLSLVPYWYEVGLLIWLSGLLLFELTNPSDKSGLGSIKVLVLLLGMAGVGVHVSAFLFVSKEYWPTLVYCRNQCFALAFLLACVQILDFLSFHHLFGPWAIIIGDLLKDLARFLAVLAIFVFGFSMHIVALNQSFANFSPEDLRSFEKKNRNRGYFSDVRMHPINSFELLFFAVFGQTTTEQTQVDKIKNVATPTQPYWVEYLFKIVFGIYMLVSVVVLINLLIAMMSDTYQRIQAQSDIEWKFGLSKLIRNMHRTTTAPSPLNLVTTWFMWIVEKVKARMKKKKRPSLVQMMGIRQASPRTKAGAKWLSKIKKDSVALSQVHLSPLGSQASFSQANQNRIENVADWEAIAKKYRALVGDEEGGSLKDSDAESGSQEGSGGQQPPAQVGRRAIKATLADTTK
Protein: Big bang, isoform C (Big bang, isoform K) (PDZ domain-containing protein BBG-LP12) (Q9VUE8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Caspase-8
Sequence:
MASTPKANGTTAKTATINDDYITVVEVDDPTSNPKDRLKKLVKRQSSVAEDSSFITVLTINEMELLQQRKKEEDVGSGSSPTMEEQIENVTVFRLPGERLGFGLKFQGGTRSTELVQKLYIQSCAADSPASKVSTSWGNLREGDEIVSIDGRDVRELTRIDCVRGLKDNVAIKLVVRNGHGQKPPSEEDPQQQEHLSITLNAQPPPPPPVPPRKLVRRQNSKENQAQLLIEKPLTPPPDAEYYLNLLTESIKAGSESDDTASTISTVIDKFSVGSNYSSDSSLNGHELAKVLQPFTLLEQEFLPLEQPLGHPKLLIPGNNYENVEFKTEKVNVYENVELRSPETTPTPKPRVQLATVEPKKRSIIPMPRKIPTPTKLPIEVTPPRVPILEEPKTPTNNKVDSPKTPTNELKESPISATKIPKAKFSRAKTEGEIKLHLPAPKQQSPQSKSRIPIVSTPTAQKTVPKPVSPTMNGTPLSSNIPRLLQKQKSETDLKLNLYRSKSKESSPRPPLQRANSAEAPERTFIPVLLNGNSKSSNSLESVSSIGSSSSGNSVRSPKGPKPKPPERVQSLQKTQIPKLQALPTTPPQQIPKLSMQTFKQSPPTPRSTPVGTPSPTSNREIRFKIQTYESKTQDEDKLPSLFDLVHSQENDKDKDRDSDSLKTHNSITALLAAAAAEAADLSRESPPPLVVGKCMKIVDDTNTTTCYTSSSSGEEDEDDLDASNREYICEDGEKLGPPELINGPGPSEAYFNMFWHSNMLPTIGEVEEEFSSLEPQSLTNGNLVKSEESKKLPKMEVNAGGLAQLTDDKIADHDASATRADTRDEVTTNQTQEISSSSSSSVKSQKTTTTTRVTTTKTSSSSSSSSCSSTVIPDVAFKLQPYEERDDILSEPITTIHEERRVLSEQKTLSESRTRDALTGEEQLVTSANSKSSSARFKKISSNDNLLDLGDEQDMQEQPLTATITQESSLRERLECPQDNQSIDRGTLTLSERGKQLSEKEGLTTYTECETSEKESYLEGQQVLNGKGGFVSQDENSDQPTYEREVSETLTIVNDGEKQVTKKLEQNKEIAGKKGAKLLKKTDEERRLEQEAQKLIESYQKVKKEAEKLYKLELADDDQGFDLSAFEQAEEEDKPEVSEEIKEVKDSQPVKVDIQIEEEVKTPNQVIGEVKVEDVNKEIKETVQVSQQEIKKEVKVSHQETKETFKSEEKDESNELKIVKEEVKVTHQDLREQIQEIEAVKVVHKEVKVIKESAKVTTTTSHKQATKEVIISKEDHKNDSALPAVSTTKVEIISPPLEDDLGYVLHKHIIFPQEKVKTAPTPLPKPKPKPPVPTNKPKMPVNLTKPKSAPPPVPSKRSELSGSGGKPTPTQRRGSLETAQPPKPLERIIVGVEQRDEPEKPQPIINLASVDLPNVAPNSKQATVETTPVVEMPPDELQFESHQLPDDGEKEKDLHQESNDLLSGSSSSSVTTPITTPILVSATSSMDSVQSVIEVVNGMPIISNQQTDDDDIDEVAAYDDGMHLEAEGTKDVRPVQEVTTLTLDREHESDLGTLSNHHSNISSISGINASSNIPAATLISSSIKKTSTEAATTKPAAPQIPGKMELLSSNTGTTTTTTTATHHLHQATTTKQLLVQDYLSYASPPTYSRLPPDGHEFPPNFSEPLIMHSHPLKVTTELSYEIQKGGKDESSAPPLPKTGPPATVPRKVYRQDLVINVEPAPSLTRDYQRSLSGGTPRKPSDWRKDEKSEKSVRDKIAMFSSNNELDAIPPAPATAPISSSFTRKPLNRSSENLLDSCSSSSAPSLKTRAMSVENLNDVQRQYQLAKQLPQLHVADSMYSLNTATPTPSYASLPRRSHGGSYSSGVERRISFSGEGGDAANRKAAITNILEQRRRSLSKLRGLVIPERPQLLEPILDLPEIKSQVKAASGEDSTDSGLGESHRSTVNRNCQLGAGGAANNYRSILNTNQRRPLEQQLSQPPAKPPRTSLTPLQPRSMMIPPPPPPLDQESDTDSVFSHTARVATPPEKFALTRTLSSETNTSIASSNTSTLTSGSSAGSQASCSSLGSTPAVDLTRRVLKSQVINGEAVALSSRKSILASAKCRSAKSRGQEEDNDSTDGEACSLANRRMKPISSYKLQQQQIQLGKQLVVDKLINVAAYVELTSDTDDSSRRSDTPAKISAMFIDEERKASFKGDPNQQAKVKVEQVKPMVLPMLLPSAKREPLKQQTTAELREKFERSAAAQAQTQNHSPVIHKVTQKPHHERFSSLDSLASSSSGVSSTTQNVSTTQETATEFGSFSSLGSNQSLITAQDVQQIVEEADPPLKTPEAFIIVLQRENPESSIGITLAGGSDYEAKEITIHKILSNTPAAKDGRLKKGDRILAVNGMSMRGLTHRESISVLKTPRPEVVLVVTRSESLVVKALTKKRSSLGSLSSLNEKPTELDYERKRNYHKASRSLDLDLDLVSNEAGESPVATTPSTGSVSPPQPASLHDEDAEATIAGIRARRQLSRGDAAKLSTSELLERAAEARNAIAAEIRAQAEDAAASGGGARCVEIVKDSCGLGFSIEGGFDSPLGNRPLIVKKVFMGGAAQKTNQVRNGDEILSINGASTSRMTRVDAWNYMKQLPLGPVKICFA
Protein: Metallophosphoesterase domain-containing protein 1 (EC 3.1.-.-) (Adult brain protein 239) (239AB) (O15442)
Organism: Homo sapiens (Human)
Function: May have metallophosphoesterase activity (in vitro).
Interaction partners:
- Uridine-cytidine kinase 1
- Uracil phosphoribosyltransferase homolog
Sequence:
MWRSRWDASVLKAEALALLPCGLGMAFSQSHVMAARRHQHSRLIIEVDEYSSNPTQAFTFYNINQGRFQPPHVQMVDPVPHDAPKPPGYTRFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDQEFMADLIKQDFYYFPSVSKLKPENYENVQSLLTNCIYLQDSEVTVRGFRIYGSPWQPWFYGWGFNLPRGQALLEKWNLIPEGVDILITHGPPLGFLDWVPKKMQRVGCVELLNTVQRRVQPRLHVFGHIHEGYGVMADGTTTYVNASVCTVNYQPVNPPIVIDLPTPRNS
Protein: E3 ubiquitin-protein ligase makorin-1 (EC 2.3.2.27) (RING finger protein 61) (RING-type E3 ubiquitin transferase makorin-1) (Q9UHC7)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II-dependent transcription.
Interaction partners:
- Telomerase reverse transcriptase
- Polyadenylate-binding protein 1
- Polyadenylate-binding protein 4
Sequence:
MAEAATPGTTATTSGAGAAAATAAAASPTPIPTVTAPSLGAGGGGGGSDGSGGGWTKQVTCRYFMHGVCKEGDNCRYSHDLSDSPYSVVCKYFQRGYCIYGDRCRYEHSKPLKQEEATATELTTKSSLAASSSLSSIVGPLVEMNTGEAESRNSNFATVGAGSEDWVNAIEFVPGQPYCGRTAPSCTEAPLQGSVTKEESEKEQTAVETKKQLCPYAAVGECRYGENCVYLHGDSCDMCGLQVLHPMDAAQRSQHIKSCIEAHEKDMELSFAVQRSKDMVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEEKEEKQKLILKYKEAMSNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYRAQRRNHFWELIEERENSNPFDNDEEEVVTFELGEMLLMLLAAGGDDELTDSEDEWDLFHDELEDFYDLDL
Protein: Glyoxylate/succinic semialdehyde reductase 1 (AtGLYR1) (AtGR1) (SSA reductase 1) (EC 1.1.1.79) (EC 1.1.1.n11) (Gamma-hydroxybutyrate dehydrogenase) (AtGHBDH) (Q9LSV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the NADPH-dependent reduction of glyoxylate to glycolate as well as succinic semialdehyde (SSA) to gamma-hydroxybutyrate in vitro. May function in redox homeostasis and play a role in oxidative stress tolerance by detoxifying glyoxylate and SSA generated in glycolate metabolism and GABA metabolism, respectively.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18495639, ECO:0000269|PubMed:22309191}. Note=According to PubMed:22309191, GLYR1 does not localize in the peroxisome as initially described in PubMed:18495639.
Interaction partners:
- Gamma-aminobutyrate transaminase POP2, mitochondrial
- Succinate-semialdehyde dehydrogenase, mitochondrial
- Glyoxylate/hydroxypyruvate reductase HPR3
- Glyoxylate/hydroxypyruvate reductase A HPR2
- Isocitrate lyase
- Glycolate oxidase 3
- Peroxisomal
- Malate synthase
- Glycolate oxidase 2
- Phosphoglycolate phosphatase 1A, chloroplastic
Sequence:
MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSVVFDKGGVLEQICEGKGYIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYLGQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDMRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVKFSRE
Protein: Endothelial cell-specific molecule 1 (ESM-1) (Q9NQ30)
Organism: Homo sapiens (Human)
Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions.
Subcellular location: Secreted.
Interaction partners:
- Integrin alpha-L
- Integrin beta-2
Sequence:
MKSVLLLTTLLVPAHLVAAWSNNYAVDCPQHCDSSECKSSPRCKRTVLDDCGCCRVCAAGRGETCYRTVSGMDGMKCGPGLRCQPSNGEDPFGEEFGICKDCPYGTFGMDCRETCNCQSGICDRGTGKCLKFPFFQYSVTKSSNRFVSLTEHDMASGDGNIVREEVVKENAAGSPVMRKWLNPR
Protein: Small t antigen (O56327)
Organism: Simian virus 40 (SV40)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEVFASSLNPGVDAIYCKQWPECAKKMSTNCICLLCLLRMKHENRKLYRKDPLVWVDCYCFDCFRMWFGLDLCEGTLLLWCDIIGQTTYRDLKL
Protein: Dystroglycan 1 (Q91XP6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
DQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Protein: Facilitator of iron transport 2 (Q08906)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the uptake of non-siderophore and siderophore sources of iron. Has a role in the retention of iron in the cell wall and periplasmic space.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10383953}. Membrane {ECO:0000269|PubMed:10383953}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10383953}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Facilitator of iron transport 3
- Siderophore iron transporter ARN2
- mRNA decay factor CTH2
- Siderophore iron transporter ARN1
- Siderophore iron transporter 1
- Ferric reductase transmembrane component 5
- Siderophore iron transporter ENB1
- Iron transport multicopper oxidase FET3
- Facilitator of iron transport 1
- Ferric reductase transmembrane component 3
Sequence:
MKFSTIFGATTVMTAVSAAAVSSVMTTKTITATNGNNVYTKVVTDTADPIISYSTTRTVVVSNSDATYTKVVTEGPDTTSEKSTTKTLTLTNGSGSSTNLYTKTVTQAVESSTSSSSSSSSSSSSASSSGAAPAAFQGASVGALALGLISYLL
Protein: Tara 1B isoform (Q9NHC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCTEVNSAMGLQATAATKRKHELTFDSKDANTTYTGNCAPPPVKANKWAISNNNYLESLEEQQQQQQSPSEPAVESNNNHIVLEASMDALKPTEPSISNGHEVTTAVAAMKSQAEVPLPPTASAAIPEDSIARLEVVTSAVPCEPWTSNGPTTPSAVAGPAASAEPVDCISKLQAVAVPSDPWGSIATRSTLATTLLSADELDDDDDDFEDDYEEEESIIPTYCPMRYHPFVPHPHPHSHQLPSHPHQQQPQQLSQQQPHPQQQQLAQQQQQHPQQQRSYAPGYGSRQPNYYSEPFPQQNCSRTGGPQHMTQSPPTPQQARGFAPPQWATAGSSPANPSSGAQQFYEPTNGGAYAPPAAPQQTIRCAENGKSYLDLGCSSGASGNAGGSPISPPPSSAPVVPFAGLPLHGLPLKRCCDGRPGGWCSTNRSCYKDTRLKIRNLSMFKLSRFRQVSEQSLYRSVLICNTLKRIDREIEAEAKELHQAAQQHHQQAAAAAAAAAAAAAQAAQYHPAYQQQQQQQQSPPAPLHPHTQQQMDYAPVLNCARLANMDHYQQLSFQPQHQQQQQPSQPHSYHERLDSQPAYRGAAAGAGSFATQPSNCDTSAGASSSNTSGNSNNSSATAASSNSSLHPYDHYPFRESQSGRATPFPACPTTTAAAAAASAAAAASSGGAATTLSSNISSSPASSSTSSNTTSSTVISSSSGNTVSSNGTTPVAPTASSSNCDTSDSGYADDDSTRSINWSSVLSLSSQSALDPLNNNDLFSILPSAATPTAVPVSVPASSSSSSSGSTLAFSGSFTTVQASGGSSSSCGSSSTTATFTTLSTISSATHSLTSSYVSSISSNVSAGANTWEYGFLDMEFGLGSEFTELVPSCKLSSEDLFKSGLGGQVVTASRLHDNELEHPAHIMVGS
Protein: Hydroxylamine reductase (EC 1.7.99.1) (Hybrid-cluster protein) (HCP) (Prismane protein) (P75825)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}.
Interaction partners:
- NADH oxidoreductase HCR
- Cytochrome c-552
- Nitrite reductase large subunit
- Nitrite reductase small subunit
- Anaerobic nitric oxide reductase flavorubredoxin
- NADP-specific glutamate dehydrogenase
- Glutamine synthetase
- Flavohemoprotein
- Iron-sulfur cluster repair protein YtfE
- Putative electron transport protein YccM
Sequence:
MFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIAALQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFDSPRIVGYAREAIALREALKAQCLAVDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATAGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIIDPTVGAYDDRIWTRSIVGWPGVRHLDGDDFSAVITQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA
Protein: SSD domain-containing protein (Q5BBG1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- BHLH transcription factor
- BHLH transcription factor
- BHLH transcription factor
- Chromatin assembly factor 1 subunit A, putative
- INSIG domain protein
Sequence:
MRGLRFIPIVAALSFPAHSFAQGKTRIHENGRCAIRGHCGKQSFFGGELPCPDNDAAREPEAAVREKLVNLCGAKWQEGPVCCEEEQIDALSKNLKLAEGIISSCPACKDNFFNIFCTFTCSPDQSLFINVTKTEKGNSGKELVTELDNIWSEEYQSGFYDSCKNVKNGASGGKAIDFIGGGAKDYQQFLKFLGDKKFLGSPFQINYHTEPPEDSQGMQALPIHPKACNDADPAYRCSCVDCPDVCPELPAIKTEEHCHVGLLPCLSFSVILIYSVFLLGVAGFSSYFTYRERRYRKPERVRLLQDPNPSDDEDEGDIVHAGGHLEYPHGYYKLNSMLDTVFSRIGSVCARFPALTIISSVVAVVLLSLGWLRFAVETDPVRLWVSPTSAAAKEKAFFDENFGPFYRAEQAFLVNDDETGDGRVLDYDTLTWWFGVESRIRRVISLDRGLSLDDICYKPTGDACVIQSVTGYFGGSLSNLDPDTWQDRLTHCASSPGDASCLPDFSQPLRPEMILGGYEDSGNVLDAKALIVTWVVNNHAPGSEEEAEAIDWEDTFRGIFQVVQEEAKNRGLRVSFTTEASVEQELNKSSNTDAKIVVISYIIMFIYASLALGSVTMTWRSLINNPANALVQSKFTLGVVGIVIVLMSVSASVGLFSAAGVKVTLIIAEVIPFLVLAVGVDNIFLIVYEFERLNVSHPDEEIDERISRAIGRIGPSIFLSAITETVAFALGVFVGMPAVRNFAIYAAGAVFINAVLQITMFVSVLALNQKRVESLRADCIPCLTVRKAHSGMPEDLAFDDQDREGILQKFIRKVYAPLLLNRRVKVVVVITFLGILAAGLALTPEVAMGLDQRIALPSDSYLIDYFDDLSEYFNSGPPVYFVTRNVNITKREHQRQLCGRFTTCEEYSLPFVLEQESKRSNVSYIAGATASWIDDFFYWLNPQQDCCYEDGKLCFEGRTPGWNISLTGMPEGAEFIHYLEKWIKSPTDASCPLGGKAPYSNALVFDPKRITTNASHFRTSHTPLRTQDDFIKSYISARRIADGLSAEHGIDVFPYSKTYIFFDQYVSIVQVAGTLLGSAVAIIFAITSILLGSVATGAVVTATVIMIVIDIIGSMAISGVSLNAVSLVNLVICVGIGVEFCAHIARAFMFPSRSIMEIVPSKFRGKDARSWTALVNVGGSVFSGITVTKLLGVCVLAFTRSKIFEIYYFRVWLALIIFAATHALIFLPVALSYFGGDGYADPEASGGLEENLASRSYRSLLVDDDYDSDEY
Protein: Vomeronasal 2, receptor 120 (A0A3Q4EGU0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLIFVSVLLFLNFPVASCEPINPGCSLGMADAIFQDGDVLVDCHFVLLTVSIALQKIFHFLRFHLSFPMFIYRIHPNKYQYVIALNFAIEEINKNIHLLPNISLGYDMYSIVQYQATILEHSIRFLTGLKEAIPNYTCRKESKLIAVVTGTSWEFPSRISTILGLYKYPQLTFGPFDPMLSDHVKFPFIYQMAPEDTSLALGMVSLMVHFSWTWVGLIITENEKGIKFLSDLKREMKKNSVCAAFVQMLSLKYRYNWNDLLSTDPAIMGEMVKVFIVFADIDSTLVVIFKASGQVDPWRVWVTTSQWDIASSVRHFILDSFHGTLIFSQHHPEISAFKDFIQTVNPSKYPDDIFLSHIWKMYLNCPFSRVYCKTLKTCSSNGSLALLPWHRFDMDMSEESYHIYNAVYAVAHSLHEMLQEHADVQPVKSRKRLVFSPCRLHPFLKNIQFNNPSGDKVDLSHTGKLETKYDIFNFWNFPQGLGLKVKVGTFSSFLPRNKQFSLSDGMIEWGTKDKQTVFSV
Protein: Protein tamozhennic (Q9W1A4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has an essential role during oogenesis and embryogenesis, perhaps in modulating the levels of nuclear import of additional proteins. Modulates the nuclear import of dorsal (dl), Dif and male specific lethal 1 (msl-1). Negatively regulates nuclear import of dl and controls the accumulation of dl in the nucleus after immune challenge.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12653959}.
Interaction partners:
- Threonylcarbamoyladenosine tRNA methylthiotransferase
Sequence:
MSDFVPHDLIPDLWDEILRRHWMFLETEESIEKLEERKQLEGCLKEFLCVVQHDRKFFLPETGHVLRRSVLELPDFSAQNAIVAFETISQYANNLFTKPWRKEYRTLKTYSGCFQHDIQSRLLDAEQLFLAMGYRRAAEDTFVLEGPICPDQVTNVSRDAMAAYVECQIMKHIYAGVTAAGYVCTWKDILQFRERYVGGTSTTIKEMVRQLSEKRVRMEQPPMQENTYSNVVSAAPTACGMRSNNVAHHPSSSGTCALHPNGLNEAGKYLPPYPAPPPQQPHLPGPLMTHSRSLDHYQEPQAHLPHRHSFDQQLQQQCQLPHVYEAPYDCLDGLSMGSSASYAAVTGAYNAPGNRYPLPYNISSQLNAPYASPADFYGNGQHTNMYATLGKTGPAHSCDLHRRQPNTSAAAAAALAAMQHRQSTYPPDHHLIDFDERAHLTQHDFGTHDYDPQYAELRGQVQPSMRGNPVAMYATYGGYDLPTTLPQAPPPTGQDMYIYARPVPKSSRMRALAEAGGINSTDKHPRSAEKQSTMDNNRKMHKELKERNSRTAPAKRSGTERDIPTTISDLNSYDSASLDGFVALDSSSSPPLMPKVQEGVGSFESWNYVFKNLERSGYTKDLGDREDLLVQSLDLGSLSITNGGAAPPAEKRREATNPTNGEKARTLDKKSGTGRREAKVVQAPAPSPLPNSSSAGVKKVKSALKTAVVDNRGTGSRQRTGAVPKQPPNVSPQLIVTSPNEWSCSFCTFLNPDTKRICEMCCRSKDFNLEAASAASSSAAAAAASAASVSHASSTCV