wanglab/gogpt-training-data huggingface dataset:
Protein: Chromatin structure-remodeling complex protein RSC30 (Remodel the structure of chromatin complex subunit 30) (P38781)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall. Together with HTL1, LDB7, NPL6, RSC3 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC3
- Chromatin structure-remodeling complex subunit RSC7
- Chromatin structure-remodeling complex protein RSC58
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit RSC2
- Nuclear protein STH1/NPS1
- High temperature lethal protein 1
- Chromatin structure-remodeling complex subunit RSC9
- Chromatin structure-remodeling complex subunit RSC4
- Regulator of Ty1 transposition protein 102
Sequence:
MMDMQVRKVRKPPACTQCRKRKIGCDRAKPICGNCVKYNKPDCFYPDGPGKMVAVPSASGMSTHGNGQGSNHFSQGNGVNQKNVMIQTQYPIMQTSIEAFNFSFNPSVDTAMQWTKAASYQNNNTNNNTAPRQNSSTVSSNVHGNTIVRSDSPDVPSMDQIREYNTRLQLVNAQSFDYTDNPYSFNVGINQDSAVFDLMTSPFTQEEVLIKEIDFLKNKLLDLQSLQLKSLKEKSNLNADNTTANKINKTGENSKKGKVDGKRAGFDHQTSRTSQSSQKYFTALTITDVQSLVQVKPLKDTPNYLFTKNFIIFRDHYLFKFYNILHDICHINQFKVSPPNNKNHQQYMEVCKVNFPPKAIIIETLNSESLNNLNIEEFLPIFDKTLLLEFVHNSFPNGDTCPSFSTVDLPLSQLTKLGELTVLLLLLNDSMTLFNKQAINNHVSALMNNLRLIRSQITLINLEYYDQETIKFIAITKFYESLYMHDDHKSSLDEDLSCLLSFQIKDFKLFHFLKKMYYSRHSLLGQSSFMVPAAENLSPIPASIDTNDIPLIANDLKLLETQAKLINILQGVPFYLPVNLTKIESLLETLTMGVSNTVDLYFHDNEVRKEWKDTLNFINTIVYTNFFLFVQNESSLSMAVQHSSNNNKTSNSERCAKDLMKIISNMHIFYSITFNFIFPIKSIKSFSSGNNRFHSNGKEFLFANHFIEILQNFIAITFAIFQRCEVILYDEFYKNLSNEEINVQLLLIHDKILEILKKIEIIVSFLRDEMNSNGSFKSIKGFNKVLNLIKYMLRFSKKKQNFARNSDNNNVTDYSQSAKNKNVLLKFPVSELNRIYLKFKEISDFLMEREVVQRSIIIDKDLESDNLGITTANFNDFYDAFYN
Protein: Rhodopsin (Opsin-2) (P08100)
Organism: Homo sapiens (Human)
Function: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling.
Subcellular location: Membrane {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25664179, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}; Multi-pass membrane protein {ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25664179}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000269|PubMed:25664179}.
Interaction partners:
- S-arrestin
- Rhodopsin kinase GRK7
- Rhodopsin kinase GRK1
- Guanine nucleotide-binding protein G
- Arrestin-C
- Guanine nucleotide-binding protein G
- Recoverin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Beta-arrestin-1
Sequence:
MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA
Protein: Outer envelope pore protein 16-3, chloroplastic/mitochondrial (Chloroplastic outer envelope pore protein of 16 kDa 3) (AtOEP16-3) (OEP16-3) (Mitochondrial complex I subunit B14.7) (O48528)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Voltage-dependent high-conductance channel with a slight cation-selectivity; selective for amino acids but excludes triosephosphates or uncharged sugars. Non-essential amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB (By similarity).
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein At1g67785
- 2Fe-2S ferredoxin-like superfamily protein
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM9
- At4g16450
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM10
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- Gamma carbonic anhydrase-like 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
Sequence:
MDPAEMRYLEEEDGPLMKTIKGSITGFGAGTIYGTILATWKDVPRVERNVALPGLIRTLKMMGTHGLTFAAIGGVYIGVEQLVQNFRSKRDFYNGAIGGFVAGASVLGYRARSIPTAIAAGATLAVTSALIDSGGQTTRVDNGREYYPYTVEKRAEADS
Protein: Probable protein S-acyltransferase 14 (EC 2.3.1.225) (Probable palmitoyltransferase At3g60800) (Zinc finger DHHC domain-containing protein At3g60800) (Q8VYP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Palmitoyl acyltransferase.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Acyl-CoA-binding domain-containing protein 5
Sequence:
MHRSGTTMAWNVFKFCTALRGLGSIMILLVLGVVGVTYYAVVLTNYGPALSQGGLDSLAALTILILFHFLLAMLLWSYFSVVFTDPGVVPPNWRPSTDEERGESDPLNSLDFVGLQSDSSSSNPRVRFCRKCNQLKPSRCHHCSVCGRCVLKMDHHCVWVVNCVGALNYKYFLLFLFYTFLETTLVTLVLMPHFIAFFSDEEIPGTPGTLATTFLAFVLNLAFALSVMGFLIMHISLVAGNTTTIEAYEKKTTTKWRYDLGKKKNFEQVFGMDKRYWLIPGYTEEDLRRMPELQGLEYPSKPDFDSQ
Protein: Protein BEX4 (Brain-expressed X-linked protein 4) (Q9CWT2)
Organism: Mus musculus (Mouse)
Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NWD9}. Nucleus {ECO:0000250|UniProtKB:Q9NWD9}. Cytoplasm {ECO:0000269|PubMed:28295929}. Note=Also localizes to microtubules. {ECO:0000250|UniProtKB:Q9NWD9}.
Interaction partners:
Sequence:
MASKFKQVILDLTVEKDKKDKKGGKASKQSEEEPHHLEEVENKKPGGNVRRKVRRLVPNFLWAIPNRHVDRNEGGEDVGRFVVQGTEVKRKTTEQQVRPYRRFRTPEPDNHYDFCLIP
Protein: Transcription factor bHLH52 (Basic helix-loop-helix protein 52) (AtbHLH52) (bHLH 52) (Transcription factor EN 124) (bHLH transcription factor bHLH052) (Q9SA82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- BEL1-like homeodomain protein 4
- BEL1-like homeodomain protein 2
- Agamous-like MADS-box protein AGL12
Sequence:
MIIPETDSFFFQEQPQHQPLYPDEALSPSLFGFDHYDHFYESFLPSQEIFLPSPKTRVFNESQELDSFHTPKHQKLIDSSFHFNSHDPFSPSPESNYLLDSYITEASNISKFQAPDFSSTFKVGWTEQGDTKKRELSAQSIAARKRRRRITEKTQELGKLIPGSQKHNTAEMFNAAAKYVKFLQAQIEILQLKQTKMQTLDSSKVGREMQFLLGSQEIQEKLSTEEVCVVPREMVQVLKAEECILTNPKISRDINKLLSTNLMN
Protein: sn-1-specific diacylglycerol lipase ABHD11 (EC 3.1.1.116) (Alpha/beta hydrolase domain-containing protein 11) (Abhydrolase domain-containing protein 11) (Williams-Beuren syndrome chromosomal region 21 protein) (Q8NFV4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:32579589}. Mitochondrion matrix {ECO:0000269|PubMed:32792488}.
Interaction partners:
Sequence:
MLRWTRAWRLPREGLGPHGPSFARVPVAPSSSSGGRGGAEPRPLPLSYRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTGVSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVRQHLLTNLVEVDGRFVWRVNLDALTQHLDKILAFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFLV
Protein: ATP synthase subunit 9, mitochondrial (Lipid-binding protein) (P00842)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit alpha
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit gamma
- ATP synthase subunit d
- ATP synthase subunit 4
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit G
- Mitochondrial ATP synthase epsilon chain domain-containing protein
Sequence:
MASTRVLASRLASQMAASAKVARPAVRVAQVSKRTIQTGSPLQTLKRTQMTSIVNATTRQAFQKRAYSSEIAQAMVEVSKNLGMGSAAIGLTGAGIGIGLVFAALLNGVARNPALRGQLFSYAILGFAFVEAIGLFDLMVALMAKFT
Protein: Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain] (Q84V22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production.
Subcellular location: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion {ECO:0000269|PubMed:17449644}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion {ECO:0000269|PubMed:17449644}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 3
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Phosphatidylserine decarboxylase proenzyme 2
- Choline/ethanolaminephosphotransferase 1
- Choline/ethanolaminephosphotransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- Lysophospholipid acyltransferase 1
- Lysophospholipid acyltransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic/mitochondrial
- Phospholipase A
Sequence:
MKPRFPQNVYFLARYSYLRRFQHSQRRTFSSFLNNIRSNYSGARASPLGGSSGAGAGAGGGGTGDSKGNAFLVPGATMATILMLGALHARRLYEDKKIEEKREKGIELEFHPDIKASFLGVLPLRSISRAWGSFMSLEIPVWMRPYAYKAWARAFHSNLEEAALPLEEYTSLQDFFVRSLKEGCRPIDPDPCCLVSPVDGTVLRFGELKGNRGMIEQVKGHSYSVPALLGNNSLLPMEPEGKNESKEEAVGDKSDKSWLRVSLASPKLRENVSASPMKGLYYCVIYLKPGDYHRIHSPADWNATVRRHFAGRLFPVNERATRTIRNLYVENERVVLEGIWKEGFMALAAVGATNIGSIELFIEPELRTNKPKKKLFPTEPPEERVYDPEGLGLRLEKGKEVAVFNMGSTVVLIFQAPTANTPEGSSSSSDYRFCVKQGDRVRVGQALGRWKEE
Protein: U8-myrmicitoxin-Tb1a (U8-MYRTX-Tb1a) (A0A6M3Z9I6)
Organism: Tetramorium bicarinatum (Tramp ant)
Subcellular location: Secreted {ECO:0000269|PubMed:30149710}.
Interaction partners:
Sequence:
MKLSFLSLAFAVIFVMAIMYAPQVEAKASADADADADAAASADALAKASAGMLDRILGAVKGFMGS
Protein: Probable cytosolic iron-sulfur protein assembly protein CIAO1 homolog (Q581A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MIP18 family-like domain-containing protein
- MMS19 nucleotide excision repair protein
- MMS19 nucleotide excision repair protein
- MIP18 family-like domain-containing protein
- Iron-containing hydrogenase, putative
Sequence:
MLSSYFSWMEHVDARVLRAGGTSDNHMRPLYLPYEAPPLLRVEPVCTLRDHTDRIWCVAWCPTANVVASCSGDGTVRLWGYMLNVGREEIPNGRDQNGTWSCIYTLEGEHSRTVRHVSWSPSGTFIACASFDRTASVWRRVSDDPNCFEFELEAILDGHENEVKCAAWGTDNTLATCSRDRTVWVWDRVDVGEFECAGVLAGHAQDVKACAWLFPSGGVEKPLLFSCSYDNTVKVWTESHKRDDWYCHQTLTRHDGTVWSVAVQPIEQPIDSLQMEEEEREGTALEYSPVVCCSSDDKTVTFWSRDGDGNFRSVCTASGFAERTIYSVGWAPSGSDVSPAIVACGSGDNKVTLLGVYQSRGYEEVHVSVVAEVPSAHEADVNTVAFSRSTNELWGDNSRGGEGLLLASGGDDNIVRIWRVTAAL
Protein: Ice-binding protein (Antifreeze protein) (AFP) (LeIBP) (C7F6X3)
Organism: Leucosporidium sp. (strain AY30) (Arctic yeast)
Function: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point. The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM.
Subcellular location: Secreted {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635}.
Interaction partners:
Sequence:
MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL
Protein: L-lactate dehydrogenase (C6KT25)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Phosphoenolpyruvate carboxylase
- Citrate synthase
- Citrate synthase-like protein, putative
- Succinate--CoA ligase subunit beta, mitochondrial
- Isocitrate dehydrogenase
- Fumarate hydratase
- pyruvate kinase
- Pyruvate kinase
- Aspartate aminotransferase
- Succinyl-CoA ligase, putative
Sequence:
MTKIALIGSGQIGAIVGELCLLENLGDLILYDVVPGIPQGKALDLKHFSTILGVNRNILGTNQIEDIKDADIIVITAGVQRKEGMTREDLIGVNGKIMKSVAESVKLHCSKAFVICVSNPLDIMVNVFHKFSNLPHEKICGMAGILDTSRYCSLIADKLKVSAEDVNAVILGGHGDLMVPLQRYTSVNGVPLSEFVKKNMISQNEIQEIIQKTRNMGAEIIKLAKASAAFAPAAAITKMIKSYLYNENNLFTCAVYLNGHYNCSNLFVGSTAKINNKGAHPVEFPLTKEEQDLYTESIASVQSNTQKAFDLIK
Protein: Double-stranded RNA-binding protein 4 (dsRNA-binding protein 4) (AtDRB4) (Q8H1D4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the trans-acting small interfering RNAs (ta-siRNAs) biogenesis by binding and assisting DICER-LIKE 4 (DCL4). Required for DCL4 activity. Required for the 21 nucleotide ta-siRNAs production of the TAS3 transcript in leaves but not in flowers. Plays an important role in silencing RNA of both DNA and RNA viruses. Involved with argonaute 7 (AGO7) and RDR6 in turnip crinkle virus (TCV) silencing. May not be directly involved in viral siRNA production. May stabilize the 21 nucleotide viral siRNAs and deliver them to the RISC complex. Targeted by the viral silencing suppressor (VSR) transactivator/viroplasmin (TAV) protein of the cauliflower mosaic virus (CaMV) that inactivates DRB4 function in RNA silencing. Probably not involved in the guide strand selection from RNA duplexes. Involved in leaf morphology through its function in ta-siRNA-mediated silencing.
Subcellular location: Nucleus {ECO:0000269|PubMed:15821876}.
Interaction partners:
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 1
- RNA-dependent RNA polymerase 6
- Endoribonuclease Dicer homolog 3
- Protein DCL homolog, chloroplastic
- Endoribonuclease Dicer homolog 2
- Protein SUPPRESSOR OF GENE SILENCING 3
- Protein argonaute 7
- Protein argonaute 1
- Small RNA 2'-O-methyltransferase
Sequence:
MDHVYKGQLQAYALQHNLELPVYANEREGPPHAPRFRCNVTFCGQTFQSSEFFPTLKSAEHAAAKIAVASLTPQSPEGIDVAYKNLLQEIAQKESSLLPFYATATSGPSHAPTFTSTVEFAGKVFSGEEAKTKKLAEMSAAKVAFMSIKNGNSNQTGSPTLPSERQEDVNSNVKSSPQEIHSQPSSKVVMTPDTPSKGIKVNEDEFPDLHDAPASNAKEINVALNEPENPTNDGTLSALTTDGMKMNIASSSLPIPHNPTNVITLNAPAANGIKRNIAACSSWMPQNPTNDGSETSSCVVDESEKKKLIMGTGHLSIPTGQHVVCRPWNPEITLPQDAEMLFRDDKFIAYRLVKP
Protein: homocitrate synthase (EC 2.3.3.14) (Q6FNT3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Aconitate hydratase, mitochondrial
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Acetyl-CoA acetyltransferase
- 2-isopropylmalate synthase
- 2-isopropylmalate synthase
- Malate synthase
- Acetyl-CoA hydrolase
- Acetyltransferase component of pyruvate dehydrogenase complex
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MDQYQQVTESTPTVETSNPYGPNPADFLSNVKEFQLIDSTLREGEQFANAFFDTEKKIEIAKALDDFGVDYIELTSPVASEQSFRDCKAICNLGLKAKILTHIRCHMDDAKVAVETGVDGVDVVIGTSKFLRQYSHGKDMNYIAKSAIEVIEFVKSKGIEIRFSSEDSFRSDLVDLLNIYKTVDKIGVNRVGIADTVGCANPRQVYELVRTLKSVVSCDIECHFHNDTGCAIANAYTALEGGAKLIDVSVLGIGERNGITPLGGLMARMIVAAPEYVKSKYKLHKIRDIENLVAEAVEVNIPFNNPITGFCAFTHKAGIHAKAILANPSTYEILDPHDFGMKRYIHFANRLTGWNAIKSRVDQLNLNLTDDQVKEVTTKIKKLGDIRPLNIDDVDSIIKDFHADLATPMVRPTEDGADNEEPLQLDEPAKKKSKLSQ
Protein: Protein SanA (P0AFY2)
Organism: Escherichia coli (strain K12)
Function: Participates in the barrier function of the cell envelope.
Subcellular location: Cell inner membrane; Single-pass membrane protein.
Interaction partners:
- Uncharacterized protein YeiS
- Protein YdcF
Sequence:
MLKRVFLSLLVLIGLLLLTVLGLDRWMSWKTAPYIYDELQDLPYRQVGVVLGTAKYYRTGVINQYYRYRIQGAINAYNSGKVNYLLLSGDNALQSYNEPMTMRKDLIAAGVDPSDIVLDYAGFRTLDSIVRTRKVFDTNDFIIITQRFHCERALFIALHMGIQAQCYAVPSPKDMLSVRIREFAARFGALADLYIFKREPRFLGPLVPIPAMHQVPEDAQGYPAVTPEQLLELQKKQGK
Protein: Female sterile (2) ltoPP43, isoform C (M9PG97)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPAVVRIKRRIDEEPQTAFVLNGKRRRLHNDENALEDAGAVAGAVAGAVASDKDELTTVLKFAGTLEKQDDCATRKFAAARLNKAAARDLVQQQRSNDAAIASALRRDRQRQEAQENSREQRFRVVNCLRSTLENSAAEAECPESQSHESSSHITIVDIESQQQQHMGTASAAAEEQQQQEIAPSQDQQQPADSDVGYVYDLYVPENEMQAAYVDMMDDNYLRLYYPFNYYNNCYW
Protein: Small ribosomal subunit protein uS14m (37S ribosomal protein mrp2, mitochondrial) (O42859)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS15m
Sequence:
MRALGHLKHKAFRDLLCRRLFAEHEVERQSNLYIYRNPELPLRVRLEAKKRIEALPTNAHPTKIKNRCIETGRGRGVFRAFGLARFPFRLKALANKLPGVRKASW
Protein: Beta-galactosidase 6 (Lactase 6) (EC 3.2.1.23) (Q9FFN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Pectinesterase inhibitor 6
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Transcriptional corepressor LEUNIG_HOMOLOG
- Peroxidase 36
- Transmembrane E3 ubiquitin-protein ligase FLY1
- Cellulose synthase A catalytic subunit 5
- Subtilisin-like protease SBT1.7
- Probable galacturonosyltransferase-like 5
- Beta-D-xylosidase 1
- Xylan glycosyltransferase MUCI21
Sequence:
MEMGRLVFGLCLILIVGTFLEFSGGATAAKGVTYDGRSLIIDGQRKLLFSGSIHYPRSTPEMWPSLIKKTKEGGIDVIQTYVFWNLHEPKLGQYDFSGRNDLVKFIKEIRSQGLYVCLRIGPFIEAEWNYGGLPFWLRDVPGMVYRTDNEPFKFHMQKFTAKIVDLMKSEGLYASQGGPIILSQIENEYANVEGAFHEKGASYIKWAGQMAVGLKTGVPWIMCKSPDAPDPVINTCNGMKCGETFPGPNSPNKPKMWTEDWTSFFQVYGKEPYIRSAEDIAFHAALFVAKNGSYINYYMYHGGTNFGRTSSSYFITGYYDQAPLDEYGLLRQPKYGHLKELHAAIKSSANPLLQGKQTILSLGPMQQAYVFEDANNGCVAFLVNNDAKASQIQFRNNAYSLSPKSIGILQNCKNLIYETAKVNVKMNTRVTTPVQVFNVPDNWNLFRETIPAFPGTSLKTNALLEHTNLTKDKTDYLWYTSSFKLDSPCTNPSIYTESSGHVVHVFVNNALAGSGHGSRDIRVVKLQAPVSLINGQNNISILSGMVGLPDSGAYMERRSYGLTKVQISCGGTKPIDLSRSQWGYSVGLLGEKVRLYQWKNLNRVKWSMNKAGLIKNRPLAWYKTTFDGPNGDGPVGLHMSSMGKGEIWVNGESIGRYWVSFLTPAGQPSQSIYHIPRAFLKPSGNLLVVFEEEGGDPLGISLNTISVVGSSQAQSQFS
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (S4VP54)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAPSPSGGGGSGGGGGTPGPIGPPASGHPAVSSMQGFQINFCEKAQSKRKALKLNFANPPVKSTARFTLNPNTTGVQNPHIERLRTHSIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERTVEVACYVCKILDQMPATPSSPMYVD
Protein: Major allergen Alt a 1 (allergen Alt a 1) (P79085)
Organism: Alternaria alternata (Alternaria rot fungus) (Torula alternata)
Function: May bind and inhibit the beta-glucanase activity of host plant thaumatin-like proteins.
Subcellular location: Spore wall {ECO:0000269|PubMed:22078468, ECO:0000269|PubMed:24642375}. Secreted {ECO:0000269|PubMed:22640235, ECO:0000269|PubMed:24642375, ECO:0000269|PubMed:8957113}.
Interaction partners:
Sequence:
MQFTTIASLFAAAGLAAAAPLESRQDTASCPVTTEGDYVWKISEFYGRKPEGTYYNSLGFNIKATNGGTLDFTCSAQADKLEDHKWYSCGENSFMDFSFDSDRSGLLLKQKVSDDITYVATATLPNYCRAGGNGPKDFVCQGVADAYITLVTLPKSS
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (P61851)
Organism: Drosophila melanogaster (Fruit fly)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm.
Interaction partners:
- Superoxide dismutase, mitochondrial
- TAR DNA-binding protein 43
- Huntingtin, isoform A
- superoxide dismutase
- TAR DNA-binding protein 43
- Superoxide dismutase
- Extracellular superoxide dismutase
- Regulatory protein zeste
- Copper transport protein ATOX1
- LD30122p
Sequence:
MVVKAVCVINGDAKGTVFFEQESSGTPVKVSGEVCGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVNITDSKITLFGADSIIGRTVVVHADADDLGQGGHELSKSTGNAGARIGCGVIGIAKV