wanglab/gogpt-training-data huggingface dataset:
Protein: MAP kinase-activating death domain protein (Rab3 guanyl-nucleotide exchange factor) (Q9VXY2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanyl-nucleotide exchange factor that regulates small GTPases (By similarity). Converts GDP-bound inactive form of Rab3 to the GTP-bound active forms (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}.
Interaction partners:
- Ras-related protein Rab-3
- Rab3 GTPase-activating protein non-catalytic subunit
- EG:80H7.4 protein
- Rabconnectin-3A
- LD21953p
Sequence:
MSDQQKASLCPRLVDYMAIVGAHTTPPMPKGLQGLKAPPVQVPDLLRRYPPSDHADFPLPLDMVYFCQPEGCTSVGPRRTGSAIRDMTSFVFALTDKDSGKTRYGICVNFYRPIERPSSAAGSAGAGNDRPGNGGPGGHGGGAGGGAGGGGRGGRRSSAFRRESWRKSMERSSDSAFSSDYRSNVAPSDSDRELTSRRDSDQQRLHSHHSHHQPHHPSASPAVPKLGLMAPSADSESGGSHSPSPRASRKRTKLRNQSLTSLCIISHHPFFTTFRECLFILKKLIDACNESSSPKRVGASQKINRDNVWTVLTGHVSDATPSIVLHDVREIETWILRLLSTPVPVPGSTRVEVEVLSPTVHEPLLFALPDHTRFSLVDFPLHLPLELLGVETCLKVWTLIMQENKVLFQSRDYNALSMSVMAFVTMLYPLEYMFPVIPLLPTCLSCAEQLLLAPTPFVIGVPASFLVYKKNFRLPDDIWVVDLDSTKLTPPTGGYEEIPPLPEPEGTILKNHLKQALTSMTATNTAVSSQQLLPSVRDSLQEPPLLGVSQVRLPLQTPPHSAQASQRNSMSAQGTISSRQPSPMNSPALNPFVYGTDVDSVDVATRVAMVRFFNAQNTLANFAEHTRTLRLYPRPVVAFQINSFLRSRPRASQFLNQFARTQAVEFLAEWSLTPTNVAFLRVQTGVMDPMQVGDKPKWFAHALTPIRFSVWDDGSSLNGALRSLKQLECQPTDESGSDSEGADSSSSSYSSLSDFVSEMASSDLSPSLHDVFGSYNRPHVVPQTLSSNLDPALVYHPPSKLQYPEGIADAVASKEEEDEERADSPVSSSSSRSDLSSPSFNRDSEFDFQPKGGQTLGSTTVGSGAAAPSFELATPLAMRLEATIKMASIEQESDTVSTATGKTIAAGSKLQRHPSDSESRPEKKIPPPLTPPVKQPGVSNILARTGSSGSSSSSPGRQSSQSSLFENFASHAKELVRETTRQSSQEGLLAHVDKFTLHAKKAAGEASKQALEVSKQAAGVSKNTLEDLTYVGKSTLGDLTKTAKEAATKKGIIKIEEHSAGGAGPPPKSPGSQLATHKQVQQSGGQGGGNNFFSAIGTDFNGLASSTSTMFSGMFGKKSQQKQVPVQQKQPNVSAGKAKSGINFDPFPGRKGLVERTPLIKHSGPRQTQEELTRQQNQERSHSNAENQTFLKDVTNQVLAGEGVGWLKLNRFKKLMEDESYRTLVLSKLNKTLDKKIAPDDHIDDVCVTKPVWKGMLKCIQAIAGGLDVTFANFGLGGMASVFQLMEVAHTHYWSKEINEGSDMSSSLLSSHAASPMGSRENLRSPSSPNGSHSALGSEWASPQESRKSSTQLAHGGPGGSHSGAPINRRLSSADSQDGQSTTEMFKDMLSQKRSALKNMLTSFDSDTTTSKDSKKSSGNLWSGKSTLSAGFRYTGGHLINTSSSPSPDSPRVYLFEGLLGKDRLNLWNQMQFWEDAFLDAVSQERDMIGMDQGPIEMMERYKSLSESERKRLEHDEDRLLSTMLYNLTAILVMLNVAKDEIRRKIRRLLGKSHIGLVYSQEVHNVVDQINNLNGNDIDLKPLGSRLLHRQSFTVHQGTDVNGPLRFMEVRDDGLVLRSVDGTIVERWWYERLVNMTYSPKTKLLCLWRRNGGQTQLHKYYTRKCKELYNCIKEAMERGGTPTNVPELGGEFPVQDMNTGEGGLLQVCLEGVGLLFSNSKFFVRLDHIRKCFTQKGGIFVLEEYNPKTRNLIQRKYQSSMSDQICYSVLCVFSYVAAGQDQKKNPVVITPQIQDIHAQQKQKHQQQQQHQQPQQQQQPHQTTTQQNQPTAVASAVPTTTAPAGQVNPNRMTAKSQAGSISIRHTVPMQKPTITMSTVQPQARMPAQVATASVPVTVPVPPTPAPPTSNPAKLPQLPPRVPSQPSTESLASISSPPPKLRTPMSAPPGPPPAIPPRTGAISRSGSVPAARSFVRQASANSTPPQYTPQPPPPFVIPKRHSGLARASTLSSSTSPSMSSSSASNHPGHSQSQQRASHGSVAAVLQSMPEAEPGYGSGSGSISGSSSGSGSASGSIASASPQAHRKH
Protein: Insulin-like growth factor-binding protein 5 (IBP-5) (IGF-binding protein 5) (IGFBP-5) (P24594)
Organism: Rattus norvegicus (Rat)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P24593}. Cytoplasm {ECO:0000250|UniProtKB:P24593}. Nucleus {ECO:0000250|UniProtKB:P24593}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein complex acid labile subunit
- Pappalysin-1
- Insulin-like growth factor-binding protein 3
- Pappalysin 2.
- Insulin-like growth factor-binding protein 6
- Platelet-derived growth factor subunit B
- Platelet-derived growth factor subunit A
- Insulin-like growth factor 1 receptor
Sequence:
MVISVVLLLLAACAVPAQGLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYGEQTKIERDSREHEEPTTSEMAEETYSPKVFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRVIPAPEMRQESDQGPCRRHMEASLQEFKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHAFDSSNVE
Protein: Cell division coordinator CpoB (P45955)
Organism: Escherichia coli (strain K12)
Function: Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_02066, ECO:0000269|PubMed:8763928}. Note=Targeting to the Sec-translocase for transport across the inner membrane is SecB-dependent (PubMed:16352602). Localizes to the septum concurrent with PBP1B-LpoB and Tol at the onset of constriction (PubMed:25951518). Localization is dependent on divisome assembly and requires ongoing septal peptidoglycan synthesis (PubMed:25951518). {ECO:0000269|PubMed:16352602, ECO:0000269|PubMed:25951518}.
Interaction partners:
- Peptidoglycan-associated lipoprotein
- Tol-Pal system protein TolB
- Tol-Pal system protein TolQ
- Penicillin-binding protein 1B
- Tol-Pal system protein TolR
- Acyl-CoA thioester hydrolase YbgC
- Tol-Pal system protein TolA
- Penicillin-binding protein activator LpoB
- Penicillin-binding protein 1A
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MSSNFRHQLLSLSLLVGIAAPWAAFAQAPISSVGSGSVEDRVTQLERISNAHSQLLTQLQQQLSDNQSDIDSLRGQIQENQYQLNQVVERQKQILLQIDSLSSGGAAAQSTSGDQSGAAASTTPTADAGTANAGAPVKSGNANTDYNAAIALVQDKSRQDDAMVAFQNFIKNYPDSTYLPNANYWLGQLNYNKGKKDDAAYYFASVVKNYPKSPKAADAMFKVGVIMQDKGDTAKAKAVYQQVISKYPGTDGAKQAQKRLNAM
Protein: 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) (P0A6L2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular location: Cytoplasm.
Interaction partners:
- 4-hydroxy-tetrahydrodipicolinate reductase
- Aspartate-semialdehyde dehydrogenase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Diaminopimelate decarboxylase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Diaminopimelate epimerase
- Outer membrane protein assembly factor BamC
- Lysine-sensitive aspartokinase 3
- Succinyl-diaminopimelate desuccinylase
Sequence:
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
Protein: Phospholipase (EC 3.1.4.4) (Q9BP34)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
Sequence:
MADAGTVGGALPPYALTNSDEEHGSGEEDASEENSNNEEGEGVFRDCTDEAVVEHNNRCLPEFQFSLVDSEYDETLAFPDSVTILSNVGDKPVLVERKETDDDEEEFDDEENNSVVLRHEIPFTSIYGPSVKFNSFQRKVFIPGREIHVRIVDTERSVTTHLLNPNLYTIELTHGPFKWTIKRRYKHFNSLHQQLSFFRTSLNIPFPSRSHKEKRTTLKATAREMADESTLKDLPSHTKVKQTSTPLRAEGRSSKIAGSNANNAMAMISPNHSSILAGLTPRRIQKKRKKKKKRKLPRFPNRPESLVTVENLSVRIKQLEDYLYNLLNISLYRSHHETLNFVEVSNVSFVPGMGIKGKEGVILKRTGSTRPGQAGCNFFGCFQKNCCVRCNYFCSDVVCGTWRNRWFFVKETCFGYIRPTDGSIRAVILFDQGFDVSTGIYQTGMRKGLQVLTNNRHIVLKCWTRRKCKEWMQYLKNTANSYARDFTLPNPHMSFAPMRANTHATWYVDGAQYMSAVADGLEAALEEIYIADWWLSPEIYMKRPALDGDYWRLDKILLRKAEQGVRVFVLLYKEVEMALGINSYYSKSTLAKHENIKVMRHPDHARGGILLWAHHEKIVVIDQTYAFMGGIDLCYGRWDDHHHRLTDLGSISTSSFSGSTRRTPSLYFTKDDTDSAFGSRKSSRNAHYDTSAKERPPSPPPDEPNTSIELKTLKPGDRLLIPSTLVSSPGETPAESGIALEGMKLNTPEMERKNVLDRLKNNAMKGARMGKDFMHRLTATETEEKSAEVYTIESEEATDHEVNLNMASGGQEVAITTSSTQILSEFCGQAKYWFGKDYSNFILKDWMNLNSPFVDIIDRTTTPRMPWHDVGLCVVGTSARDVARHFIQRWNAMKLEKLRDNTRFPYLMPKSYHQVRLNPNIQQNRQQRVTCQLLRSVSAWSCGFIEADLVEQSIHDAYIQTITKAQHYVYIENQFFITMQLGMGVPGAYNNVRNQIGETLFKRIVRAHKERKPFRVYVIMPLLPGFEGDVGGSTGIAVRAITHWNYASISRGRTSILTRLQEAGIANPENYISFHSLRNHSFLNNTPITELIYVHSKLLIADDRVVICGSANINDRSMIGKRDSEIAAILMDEEFEDGRMNGKKYPSGVFAGRLRKYLFKEHLGLLESEGSSRSDLDINDPVCEKFWHGTWRRISMQNTEIYDEVFKCIPTDFVKTFASLRKYQEEPPLAKTAPDLAANRANDIQGYLVDLPLEFLNKEVLTPPVTSKEGLIPTSVWT
Protein: Cement protein 20 (20 kDa cement protein) (Mrcp-20k) (Q9GRC4)
Organism: Megabalanus rosa (Acorn barnacle)
Function: Component of the insoluble proteinaceous cement which allows underwater adhesion to rocks and other surfaces. Shows specific adsorption on calcite substrates.
Subcellular location: Secreted {ECO:0000269|PubMed:11368778, ECO:0000269|PubMed:18021251}.
Interaction partners:
Sequence:
MKWFLFLLTTAVLAAVVSAHEEDGVCNSNAPCYHCDANGENCSCNCELFDCEAKKPDGSYAHPCRRCDANNICKCSCTAIPCNEDHPCHHCHEEDDGDTHCHCSCEHSHDHHDDDTHGECTKKAPCWRCEYNADLKHDVCGCECSKLPCNDEHPCYRKEGGVVSCDCKTITCNEDHPCYHSYEEDGVTKSDCDCEHSPGPSE
Protein: H/ACA ribonucleoprotein complex subunit CBF5 (EC 5.4.99.-) (Centromere-binding factor 5) (Centromere/microtubule-binding protein CBF5) (H/ACA snoRNP protein CBF5) (Small nucleolar RNP protein CBF5) (p64') (P33322)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. Chromosome, centromere {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:14562095}.
Interaction partners:
- Protein SHQ1
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit GAR1
- H/ACA ribonucleoprotein complex subunit NOP10
- Nucleolar protein 56
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit NHP2
- ATP-dependent RNA helicase HAS1
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- RNA cytidine acetyltransferase
Sequence:
MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQMSTVDLASCDHGVVASVKRCIMERDLYPRRWGLGPVAQKKKQMKADGKLDKYGRVNENTPEQWKKEYVPLDNAEQSTSSSQETKETEEEPKKAKEDSLIKEVETEKEEVKEDDSKKEKKEKKDKKEKKEKKEKKDKKEKKEKKEKKRKSEDGDSEEKKSKKSKK
Protein: Putative lipid scramblase CLPTM1 (Cleft lip and palate transmembrane protein 1) (O96005)
Organism: Homo sapiens (Human)
Function: Involved in GABAergic but not glutamatergic transmission. Binds and traps GABAA receptors in the endoplasmic reticulum (ER). Modulates postsynaptic GABAergic transmission, and therefore inhibitory neurotransmission, by reducing the plasma membrane expression of these receptors. Altered GABAergic signaling is one among many causes of cleft palate (By similarity). Might function as a lipid scramblase, translocating lipids in membranes from one leaflet to the other one (By similarity). Required for efficient glycosylphosphatidylinositol (GPI) inositol deacylation in the ER, which is a crucial step to switch GPI-anchored proteins (GPI-APs) from protein folding to transport states. May play a role in T-cell development (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAAQEADGARSAVVAAGGGSSGQVTSNGSIGRDPPAETQPQNPPAQPAPNAWQVIKGVLFRIFIIWAISSWFRRGPAPQDQAGPGGAPRVASRNLFPKDTLMNLHVYISEHEHFTDFNATSALFWEQHDLVYGDWTSGENSDGCYEHFAELDIPQSVQQNGSIYIHVYFTKSGFHPDPRQKALYRRLATVHMSRMINKYKRRRFQKTKNLLTGETEADPEMIKRAEDYGPVEVISHWHPNITINIVDDHTPWVKGSVPPPLDQYVKFDAVSGDYYPIIYFNDYWNLQKDYYPINESLASLPLRVSFCPLSLWRWQLYAAQSTKSPWNFLGDELYEQSDEEQDSVKVALLETNPYLLALTIIVSIVHSVFEFLAFKNDIQFWNSRQSLEGLSVRSVFFGVFQSFVVLLYILDNETNFVVQVSVFIGVLIDLWKITKVMDVRLDREHRVAGIFPRLSFKDKSTYIESSTKVYDDMAFRYLSWILFPLLGCYAVYSLLYLEHKGWYSWVLSMLYGFLLTFGFITMTPQLFINYKLKSVAHLPWRMLTYKALNTFIDDLFAFVIKMPVMYRIGCLRDDVVFFIYLYQRWIYRVDPTRVNEFGMSGEDPTAAAPVAEVPTAAGALTPTPAPTTTTATREEASTSLPTKPTQGASSASEPQEAPPKPAEDKKKD
Protein: Cytochrome c oxidase assembly protein cox18, mitochondrial (Sp3) (cox18sp+) (O94587)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome c oxidase. Plays a central role in the translocation and export of the C-terminal part of the cox2 protein into the mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Uncharacterized protein C13G7.11
- Tryptophan synthase
Sequence:
MLQTLIGVHSYMPWCYEIPAMAIFLRSTITLPIAIASLKTARRFVQVQPLIKEAKKRCRTNTDFRTVRKKLYKRFNCHPLMIYALPITQLPLFAFASYQLRQAVDVCPESMSTEGMLWFTDLTLPDPHGVLPAVLAVTYLTNMSILKRPSDSRLLKIFNTAGIMSAFFVSFMAFKTSTALSLYWTTSAIYSLVQNVALRKLL
Protein: Calmodulin-2 (P0DP24)
Organism: Homo sapiens (Human)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.
Interaction partners:
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Putative Rho GTPase-activating protein C1565.02c (Q9P3B1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Actin cytoskeleton-regulatory complex protein sla1
- Cell division control protein 42 homolog
Sequence:
MEHDLERLCFIGGYDNDNDKVIVVVTKNLELFKKYDDINLIKEAYNHVHKLIQKDERYTAVFFAHDSTVFSYLGLSLKAYYGMDYYLHKNVKAVYVIHTDWMSKVAIRTLLSIASPKFTRKFRYLNSISDLNKYIPLSHLKLPPIVYEFDRNVEPAIFPSNPSATSNFIFPVQQWTRPPDALVEGMQVVSKSLQTEGLFRKSCSRKHLDIVIELYDNGCMVDLEAFGPIAACSLIKHLFRSLPSPLFSAEFLNGLTDHMDSGIDYAVSLQKLIDASMDKNSQKLARLIFSLLYQITQHEQENMMNAQNLALCIGPSFSKADNIAELMSMKDKEYNPYCYFLEYAILHWNTLFANEENWDSYIPQDPTLLLPKTP
Protein: Zn(II)2Cys6 transcription factor (Eurofung) (C8V8Z3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pentafunctional AROM polypeptide
- Catabolic 3-dehydroquinase
- Quinate dehydrogenase
- Uncharacterized protein
- Pentafunctional AROM polypeptide, putative
Sequence:
MSRPTVSIDRLTPRRVTAEPRESMNCKSCRKRKIKCNRLRPSCEACKVFQCPCIYDAVPKKRGPKTDVLEALLKRVDGLEKRLQDDGTHPLSPASPVKPDLPLPSSTSISHPASHSHAAHSHPPPHPQSHPAAFPLAPPAAYAHGHPHGHSQGHGHPPPGRVPDAMLDAYFARLHGKPFFILDETSTRQKHSSGQLPAPLSMAVYALTLRYTTVNPPPGSLEYARQARRMIDIDQPSIENLQTLLLLCQTFYAYGCGKKAYMTLGNAVSMVLALDLYREPPASHPSLSPERETRRRLFWSVYVLDRFLTCGSKRPCLIADHSILVRLPASHPSGQDPGDIFNPVGPNIPYSSDRRKTASSGAGSGACSSLLVDISRILGVTHRYLAAGGVKGDSHFPWHALSNLSKIRQELDLWAAGTHDLFASIEALFGHPESTLLLLSKLIYHLVHCLLYRPFLPIDLAELRGTGQHQSWQIEATTLCFSHANAIAELVELARHAPRIEWPDLVAYCLTVAGTVHIHGVHYNGRREGEVFASSPDFLNREMSQLDWLGGFWSGVRHHRDLLRTLEVCHAELVRSLAARPVRFAPVFHLEDFLDRYPGLSLGGGPGVDGSHVRLVDEDQIDLDPQLLYASTSVPTAGPTPILPSQPNGIHHTHARHLSTSSASASHSLSFTSSTWPEIPTDPELLNQSPASGSVGPNASTFFSPTLGSTTHYSHLTSHSQPQTYLQSQIQYATFPFESTPVPVPVPVESPSATSQSQPSSATAGPGSSGNGNGNEEKDPFLSLLEQIAENEHNPGGPSELDFFLEGLETDAGAGANAGTGAAAATRSSSSSLLSAVLKESRSLPRQIDTDPTTPTPDLPSPAQKRLLQFVRDVQRHLSQEYKVGYDGLRAAMNTDGGLFGDKLGTGYNARASGYCEQRDMGPLIDIDVDTRRNITGTGTTNSEVEDIFTPEVNSSLATAAASGSGSTRQRRRSSVSGAQKHLYNLLSFVSFLTKESLLLRPGAGERVAVEMIVETLEHPDPGNALKGHELWFGRAHHSVFGLGSGVVSSSGWRANETTVTAISLWLIIMGEELYARAQASVQTAKSNAKSASLIDLDDGPGSENGEGGEETWPQLSEIVIREWETWTTRLQFLSLRQDLEIQAREQAAEAAAVMRRVYY
Protein: Magnetosome protein MamL (Q6NE58)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Involved in magnetite crystal maturation, but not in magnetosome vesicle tubulation or formation. One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis.
Subcellular location: Magnetosome membrane {ECO:0000305|PubMed:27286560}; Single-pass membrane protein {ECO:0000255}. Note=Tagged protein forms chains, aligned patches but also unaligned patches in the cell; the chains and aligned patches are in the correct position to be magnetosomes. {ECO:0000269|PubMed:27286560}.
Interaction partners:
- Magnetosome protein MamM
- Probable membrane transporter protein MamO
- Magnetosome protein MamN
- Actin-like protein MamK
- Multi-heme protein MamP
- Magnetosome protein MamQ
- Magnetosome protein MamI
- Magnetosome formation protease MamE
- Magnetosome protein MamB
- Magnetosome protein MamR
Sequence:
MVRVIGSLVFGGLILLLASSNAHMVETRFGPLIMLAPHFVVLGITFFLGFAIGIVLVFANVMKRRKHKLPGKNIVIKR
Protein: Long neurotoxin MS4 (P86098)
Organism: Micrurus surinamensis (Surinam coral snake)
Function: Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Weak inhibitor of the endogenous nicotinic acetylcholine receptors (nAChR) in the human rhabdomyosarcoma TE 671 cell line with an IC(50) of 690 mM. This neurotoxin is lethal to zebrafish by injection at the back of the dorsolateral region, but is not toxic to mice by intraperitoneal injection.
Subcellular location: Secreted {ECO:0000269|PubMed:18384102}.
Interaction partners:
Sequence:
LTCKTCPFNTCANSETCPAGKNICYQKKWEEHRGERIERRCVANCPKLGSNDKSLLCCRRDDCN
Protein: EZH inhibitory protein (Q86X51)
Organism: Homo sapiens (Human)
Function: Inhibits PRC2/EED-EZH1 and PRC2/EED-EZH2 complex function by inhibiting EZH1/EZH2 methyltransferase activity, thereby causing down-regulation of histone H3 trimethylation on 'Lys-27' (H3K27me3). Probably inhibits methyltransferase activity by limiting the stimulatory effect of cofactors such as AEBP2 and JARID2. Inhibits H3K27me3 deposition during spermatogenesis and oogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:29909548, ECO:0000269|PubMed:30923826, ECO:0000269|PubMed:31086175}. Cytoplasm {ECO:0000269|PubMed:30923826}.
Interaction partners:
- Histone-lysine N-methyltransferase EZH2
- MBT domain-containing protein 1
- Polycomb protein SUZ12
Sequence:
MATQSDMEKEQKHQQDEGQGGLNNETALASGDACGTGNQDPAASVTTVSSQASPSGGAALSSSTAGSSAAAATSAAIFITDEASGLPIIAAVLTERHSDRQDCRSPHEVFGCVVPEGGSQAAVGPQKATGHADEHLAQTKSPGNSRRRKQPCRNQAAPAQKPPGRRLFPEPLPPSSPGFRPSSYPCSGASTSSQATQPGPALLSHASEARPATRSRITLVASALRRRASGPGPVIRGCTAQPGPAFPHRATHLDPARLSPESAPGPARRGRASVPGPARRGCDSAPGPARRGRDSAPVSAPRGRDSAPGSARRGRDSAPGPALRVRTARSDAGHRSTSTTPGTGLRSRSTQQRSALLSRRSLSGSADENPSCGTGSERLAFQSRSGSPDPEVPSRASPPVWHAVRMRASSPSPPGRFFLPIPQQWDESSSSSYASNSSSPSRSPGLSPSSPSPEFLGLRSISTPSPESLRYALMPEFYALSPVPPEEQAEIESTAHPATPPEP
Protein: Homeobox protein Dlx6a (Distal-less homeobox protein 6a) (DLX-6) (Q98877)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Endothelin-1 receptor
- Heart- and neural crest derivatives-expressed protein 2
- Endothelin 1.
- Endothelin receptor type Ab
Sequence:
MMTMTTMADGLEAQDSSKSAFMEFGQQSHSQQSSPSMAASHYPLHCLHSGSHHHHQHDSSPYSGSNSYNRSLPYSYVSHPHHSPYLPSYHSNASGTQTRLDATEQQKTTVIENGEIRFNGKGKKIRKPRTIYSSLQLQALNHRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLLKQGGNPHETDTLPGSIALSPRSPAIPPIWDVSASSKGVNMSANSYMPGYSHWYSSPHQDAMQR
Protein: Uncharacterized protein, isoform B (M9PF18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MNKKDVSPSGSTVPATSVRTGFLRRRNVVEAGSEPSTSQQAEIAIASGKVKKRGILLARKDVEIESGVEVLEDMIPSTAVHIDHSKDVANKRAEEVTDAGADADSRASLTLPVAPGFSTLASSYVEKESGVRDTRSRISFFSNLSMLSVSQWREKHQGATAFALPVLLSVLLILLMILPVPDFLRGVFATLLFFTVMDCCGGHLRALLEDFMLTTHPERVAFAIPNYKFMPICEIPAVEEHKTIKTYAGWMNEINSYDPNTFSFSLTRAVYVRLDGSILKMSGTNARIPKRRMWNEPPIDRHKIPFTDHRSYDLRDCRIELLPLGLANKRFFNRKYPIQLIIKSNRDVPDEQSSVESQSEATVKTDAKEAKAASSSGTTPPGGEEEKLVDFAGTVMQADLQQLRNTVNPDKELNDITVPCGDEVRLLLFSRCDREKEDWYRRFTNASRGLVHEQDLQVPMARFVEDSDLQAAAARQALLLVTGMGKAGVKSEDEISAGKGNDETDQQTPDGQFETITEEDLLDTPKEESFDGMIMSANVARNSPDYVRFMAVYQACNQSTIPVTRSSVGTMRTTDRRPRKSRRAKRQEDELWKGIDQSLFLGPSGSIVWANVLLGRCLYSWLHDAMLHEKLKEVLQKKLNSIKLPSFMEEVIITNIYLGESPLLCHRVSQPMLDERGVWIDADVTYEGLAHITVTTKLNLLRIRSKTKSPMATDNVPTTSMLPEQSQDLRSLSEVNSENVIYDSDAESSGGSSTESESPPPGNAPENAAGTEFFQNSPGNARRIFKIVDRIAASNLFQYATELPYVQRAMENMNANITLRVDLKGLVARGTLNVPPPPSDRVWVSFRGPPRLWISTKPQVGDKSVDWSIVTNVIESKLCEAVNKFLVYPNMVDFSIPFLSNPNFDEDQGNAAN
Protein: Iron-sulfur clusters transporter ABCB7, mitochondrial (ATP-binding cassette sub-family B member 7, mitochondrial) (ATP-binding cassette transporter 7) (ABC transporter 7 protein) (Q61102)
Organism: Mus musculus (Mouse)
Function: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis. Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis. In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1 (By similarity). May also play a role in hematopoiesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}.
Interaction partners:
- Ferrochelatase, mitochondrial
- Mitoferrin-1
- Glutaredoxin-related protein 5, mitochondrial
- Cysteine desulfurase
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Transmembrane protein 14C
- Iron-sulfur cluster assembly enzyme ISCU
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- LYR motif-containing protein 4
Sequence:
MALLAIHSWRWAAAAVAFEKHKHSAVLTRALVSMCGSGPRWSSSQRGASGSARLSQTTESLRNTTQQRWGKDNSRQLLDATKALQTWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPEDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMMLVSSVLYYKCGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQNAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKVMAPPLQITPQTATVAFDNVHFEYIEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNLQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKNPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSNRVQNQDSLGWDAKKESLSKEEERKKLQEEIVNSVKGCGNCSC