wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-sugar pyrophosphorylase (AtUSP) (EC 2.7.7.64) (Q9C5I1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the synthesis of the intine, the pectocellulosic inner wall of developing pollen. May function as the terminal enzyme of the myo-inositol oxidation (MIO) pathway. May also play a role in the salvage pathway for synthesis of nucleotide sugars. Can use a wide range of substrates including glucose-1-phosphate, galactose-1-phosphate, xylose-1-phosphate, arabinose-1-phosphate and glucuronate-1-phosphate.
Interaction partners:
- Probable glucuronokinase 2
- Glucuronokinase 1
- Probable phosphoglucomutase, cytoplasmic 1
- UDP-arabinose 4-epimerase 1
- Probable phosphoglucomutase, cytoplasmic 2
- Phosphoglucomutase, chloroplastic
- Putative UDP-glucose 6-dehydrogenase
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
- UTP--glucose-1-phosphate uridylyltransferase 1
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1
Sequence:
MASTVDSNFFSSVPALHSNLGLLSPDQIELAKILLENGQSHLFQQWPELGVDDKEKLAFFDQIARLNSSYPGGLAAYIKTAKELLADSKVGKNPYDGFSPSVPSGENLTFGTDNFIEMEKRGVVEARNAAFVLVAGGLGERLGYNGIKVALPRETTTGTCFLQHYIESILALQEASNKIDSDGSERDIPFIIMTSDDTHSRTLDLLELNSYFGMKPTQVHLLKQEKVACLDDNDARLALDPHNKYSIQTKPHGHGDVHSLLYSSGLLHKWLEAGLKWVLFFQDTNGLLFNAIPASLGVSATKQYHVNSLAVPRKAKEAIGGISKLTHVDGRSMVINVEYNQLDPLLRASGFPDGDVNCETGFSPFPGNINQLILELGPYKDELQKTGGAIKEFVNPKYKDSTKTAFKSSTRLECMMQDYPKTLPPTARVGFTVMDIWLAYAPVKNNPEDAAKVPKGNPYHSATSGEMAIYRANSLILQKAGVKVEEPVKQVLNGQEVEVWSRITWKPKWGMIFSDIKKKVSGNCEVSQRSTMAIKGRNVFIKDLSLDGALIVDSIDDAEVKLGGLIKNNGWTMESVDYKDTSVPEEIRIRGFRFNKVEQLEKKLTQPGKFSVED
Protein: Protein SCD5 (Protein FTB1) (P34758)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates both fluid phase and receptor-mediated endocytosis. Involved in vesicular transport at a late stage of the secretory pathway. Regulates actin cytoskeleton organization.
Subcellular location: Membrane {ECO:0000269|PubMed:8688556}; Peripheral membrane protein {ECO:0000269|PubMed:8688556}.
Interaction partners:
- Actin-regulating kinase PRK1
- Actin cytoskeleton-regulatory complex protein PAN1
- Serine/threonine-protein phosphatase PP1-2
- Actin cytoskeleton-regulatory complex protein SLA1
- Actin-regulating kinase 1
- Clathrin light chain
- Clathrin coat assembly protein AP180A
- Epsin-1
- Actin-binding protein
- GLC7-interacting protein 1
Sequence:
MSFDWLNVPGLDLSSGDQAEKRPSNGLGPPSVSFDFGINTAAPHDSSFWDQGSRSHSDTTLSYRNNHSNTAADNATNVSSPQKDNPPNGEVRTLSGGDVYAESPEDMQVPLSLSQNQLTHEEIRTYLRWYHYICLRTHGKLVRLNDVFRFLTNFNLSQKVKDRIVEIFRSCKNALNIGQFFAVLRLVSRAIIYGILPLRRMILEKAPVPKPRPILSSENHEEVYEEVEDDDSSAKTGDQKVDFDSFASLLLTGKTTRKRVRRRIKNLNFKSKKVRFSEHITFQDPPNLNQESSNNSEARKQDPDAEDEDQDSNNDSPLDFTLPMDQLLKRLYKRRKNSGLVSSLPSEQQETEEEKKVLEDMKDSLSHFKQIQTVDSASLPISSVFLQNGNTLPTSNVNNTTVPQQLPLEPLKPTATGSANHLVREEYNQGLHPSNGAIQTGLQPLKPTATGSANYLMRSHMEQPQSIKPSSTPETVTNSGGLQPLKPTATGSANYLMKQHISPSVNNPVSSMFQAQFTNQSSSPQSTGPAFLNSPNITLPQSNQQQPYQEVNPTQAKIEPSNISPQHTYSNNVRINNGNIVSMPKVEITGAFPPQNTLPQHQQSHLLSPQNTIPQHQRSQLISPQNTFTQNQPILSPQHTYSNNQATMISPQNTYTNNQQQPQHLPPPPPPRAQQQQQGAIVPPQHMYSNVQKQNNLVPTQPSYTNSPSIQSPNFLSPQNAANSYFQSLLSSSPSPNPTPSNASTVNGNNASNGISSFQNTSAAMNNTQSHQTYIQQQQQQQTQQRIYGGQLSQMQQHPGQLHLNNSDIHSQPNKPNYGMLGQQVHQQQQQQQQQFPFTADVNRSNSSDILGNLQSLQQQVDALQIQYNRRP
Protein: Styrene monooxygenase StyA (EC 1.14.14.11) (Styrene monooxygenase large component) (O06834)
Organism: Pseudomonas fluorescens
Function: Styrene monooxygenase which catalyzes the first step in the aerobic styrene degradation pathway by enantioselective epoxidation of the vinyl side chain. In a two-component system, StyB reductase utilizes NADH to reduce FAD, which is then transferred to the oxygenase; the electron transfer is proposed to occur via a diffusing flavin.
Interaction partners:
Sequence:
MKKRIGIVGAGTAGLHLGLFLRQHDVDVTVYTDRKPDEYSGLRLLNTVAHHAVTVQREVALDVNEWPSEEFGYFGHYYYVGGSQPMRFYGDLKAPSRAVDYRLYQPMLMRALEARGGKSCYDDVSTEDLEGLSEQYDLLVVCTGKNALGKVFEKQSENSPFEKPQRALCVGLFKGIKEAPIRAVTMSFSPGHGELIEIPTLSFNGMSTALVLENHIGSDLEVLAHTKYDDDPRAFLDLMLEKLRKHHPSVAERIDPAEFDLANSSLDILQGGVVPAFRDGHATLSNGKTIIGLGDVQATVDPVLGQGANMASHAAWILGEEILAHSVYDLRFSEHLERRRQDRVLCATRWTNFILSALSALPPEFLAFLQILSQSREMADEFTDNFNYPERQWDRFSSPERIGQWCNQYAPTIAA
Protein: Vacuolar membrane protein pep3 (Vacuolar protein sorting-associated protein 18) (O74925)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vacuolar biogenesis.
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Probable vacuolar protein sorting-associated protein 16 homolog
- E3 ubiquitin-protein ligase pep5
- Vacuolar protein sorting-associated protein 8
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 33
- Vacuolar morphogenesis protein 6
- Vacuolar protein sorting-associated protein 3
- Vesicle transport v-SNARE protein vti1
- Ypt/Rab-type GTPase ypt7
- Pep5-like zinc finger protein C16A10.03c
Sequence:
MSLAEDWIDPNSSEDSDIQEDAELEYTADNPEKEQRGVFSLEKVQLQFPVSIRCLAVENNILVMALTSDKLMIVDLERPEDIIDIELPKKVLALGLTYKIFLDPSGHYIFVTTTAGDNCLFTPSHQGRVLTKLKGHTVEAVQWNLNGGNILELLIASKSGVLLELVLTLDSANLKRIEKSINTLYSFPFMESPMGILKNIQDDSMTIVTNKRILRFEPKTSRGKDQLYFSPAFQGSMKEILSFSEEETAQCFSYSPFPKNLAEPYTLALKTSKRIIYLDIMNPVNPDIQDYEFNESPKLSVPTVEMNMILTSFHLAFLDLDTLYIVNRVNGKESYQQRVNLSPHEEILGLCCDHEKNTYWLYTTDSLHELVVNNETREASLVFLEKGDFEKALECANTAKVRNTVLVGYAEFLMEHEEYERAATLYAETLKSVEEVALKFIELNQKDVLRLYLWKKLRSYKSTMKIQKSLLVNWLLELMLAKLNSLDEKERLELFPENVMQQRQQVQREFSTLLNQYKDEINREAAYNLANNYGKEEQLLQIATVMKDQSYIMHYWVQRENYEKALETLNEGVSQETLIQHATALLTHRPNETVSIWERQTDLDVHALIPSLLSYNQRSHVPVEENAAIRYLRYVTGVLGCVDPSIHNTLFCIYACHSSSNESYLMNYIEQQGNHPLYDMDLGIRLCLQFNCRRSAVKILVLMKLYSQGVELALEADDCELAATIANIPEEDVVLKKTLWQTIAKYMFSKKSGIKETLRFLENSEVLQLPELIRLLPEDIKLDDLSDNVCDELDHCMKRIEQLDFEIGQASEVAHEIQTNAENMRNRYIVLEPNESCWHCNQPLFSEPFVLFPCQHAFHRSCMLEKTYKLASEKNILKECQLCGPSYAVRLINEPFSTDF
Protein: ATP synthase subunit delta, mitochondrial (F-ATPase delta subunit) (Q09544)
Organism: Caenorhabditis elegans
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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element (Probable).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit d
- F-ATPase gamma subunit
- ATP synthase c subunit
- ATP synthase subunit beta, mitochondrial
- ATP synthase F
- Oligomycin sensitivity conferral protein
- ATP synthase subunit alpha, mitochondrial
- ATP synthase F
- ATP synthase-coupling factor 6
- Putative ATP synthase subunit f
Sequence:
MLARTIQRFSVVAKRGYAAAAPAANANPEELRLTFASPDTAVFSNAVVKQVDVPTLAGMVGVLANHVPTIGVLKPGVVSVTTNEGTVQRLFVSSGTLSVNIDGSCQVLAEEVLKVEEIDESAARAELDAAQRASGEGSEVARAEAQIRAEVAEALIKAATNQQ
Protein: Plasma membrane sensor transducer (Eurofung) (Q5B1C0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Anaphase-promoting complex subunit 5
- Uncharacterized protein
Sequence:
MRSFTLSTVFATAALLASSSPAAAQEQTYIGCFSSSKPLEDQGSYTYQSNGYCMNLCYGKNKAVFGLYNANHCLCGDEIPAKSSKEDDDSCNKPCAAWPIVMCGGSDAYSVYLTGYKDNVPYYSDSSSSTTSSSNSSSTSTTSGDSTTTNANGAVVTTSSANGQQEMATSTASADNDSSKKDGPNTAAIAAGVVIGVVGLAALIGAGFFLWRFKKRHPADQRMREMSNVEQFGKPMSQDSMSDHRFDGDFMAHRRQSNGSIDDDRDFSRRVLQVTNPDRH
Protein: Adenylate kinase isoenzyme 6 homolog (AK6) (EC 2.7.4.3) (Dual activity adenylate kinase/ATPase) (AK/ATPase) (Q584W4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}.
Interaction partners:
- 40S ribosomal protein S14
- Adenosine kinase
- Adenosine kinase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Phosphodiesterase
- Pyruvate kinase
- DNA-dependent RNA polymerases, putative
Sequence:
MQQPKGINILITGTPGTGKTSLAELLVEELEGFSRIDVGKVVKENEFYTEYDKEFDTHVIDEDDEGRLLDFMEPIMVQGGNHVVDYHSSELFPKRWFHLVVVLRTSTEVLFERLMDRKYGELKRNENMEAEIHGICEEEARGAYDEDIIIVRDNNTLEEMAATVSLIQSRVGSIQAV
Protein: AT5g14910/F2G14_30 (Heavy metal transport/detoxification superfamily protein) (Q93VK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein bS1c
- Rhodanese-like domain-containing protein 4A, chloroplastic
- 5-oxoprolinase 1
- Proteasome assembly chaperone
- Ribosomal protein
- Kinetochore protein SPC25 homolog
Sequence:
MASIAASSTFHSFCRTKSPNLSSTHLLPLSKNLNFRTRAIGNSRNCSFAGFIKQNRLGLRKLSSIGEGGEGVAVAEEQPQETVSVPVSPSDMLTMFFQADGTLNEAAIPNVTRALQDIDGVSNLKVQVSEGVAVVELLKQTTVQATGVASNLVETIQGAGFKLQTLNLSFEDDDEVLV
Protein: Cytochrome c biogenesis protein family (F4K0A8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
MNLSVNRCITGGFVGGFSSCRLNHGKKRWVRAGKHCELERERSLVSDAVSLERLESKSIKLAMLASGLGVANLVTLSSAKAADLKMIVLDQATSIYILAEGSLGDSVGNFLYSANQQANEAVQDQLSALSVTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKSRGQVIGDTVAFALGLATTLALLGIVASFAGKAYGQIGQGLPVAASGLAIVMGLNLLEIIELQLPSFFNNFDPRAAAANFPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPVIGGSLLLTYTTGYVAPLIVAASFAGALQSLLSLRKVSAWINPISGALLLGGGLYTFLDRLFPAATMVM
Protein: Zinc finger protein 394 (Zinc finger protein with KRAB and SCAN domains 14) (Q53GI3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- SCAN domain-containing protein 1
- Zinc finger protein 397
- Zinc finger and SCAN domain-containing protein 20
Sequence:
MNSSLTAQRRGSDAELGPWVMAARSKDAAPSQRDGLLPVKVEEDSPGSWEPNYPAASPDPETSRLHFRQLRYQEVAGPEEALSRLRELCRRWLRPELLSKEQILELLVLEQFLTILPEELQAWVREHCPESGEEAVAVVRALQRALDGTSSQGMVTFEDTAVSLTWEEWERLDPARRDFCRESAQKDSGSTVPPSLESRVENKELIPMQQILEEAEPQGQLQEAFQGKRPLFSKCGSTHEDRVEKQSGDPLPLKLENSPEAEGLNSISDVNKNGSIEGEDSKNNELQNSARCSNLVLCQHIPKAERPTDSEEHGNKCKQSFHMVTWHVLKPHKSDSGDSFHHSSLFETQRQLHEERPYKCGNCGKSFKQRSDLFRHQRIHTGEKPYGCQECGKSFSQSAALTKHQRTHTGEKPYTCLKCGERFRQNSHLNRHQSTHSRDKHFKCEECGETCHISNLFRHQRLHKGERPYKCEECEKSFKQRSDLFKHHRIHTGEKPYGCSVCGKRFNQSATLIKHQRIHTGEKPYKCLECGERFRQSTHLIRHQRIHQNKVLSAGRGGSRL
Protein: Ataxin-3-like protein (EC 3.4.19.12) (Machado-Joseph disease protein 1-like) (Q9H3M9)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that cleaves both 'Lys-48'-linked and 'Lys-63'-linked poly-ubiquitin chains (in vitro).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Beclin-1
- Polyubiquitin-C
- UV excision repair protein RAD23 homolog B
- UV excision repair protein RAD23 homolog A
- Ataxin-2
- Transitional endoplasmic reticulum ATPase
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MDFIFHEKQEGFLCAQHCLNNLLQGEYFSPVELASIAHQLDEEERMRMAEGGVTSEEYLAFLQQPSENMDDTGFFSIQVISNALKFWGLEIIHFNNPEYQKLGIDPINERSFICNYKQHWFTIRKFGKHWFNLNSLLAGPELISDTCLANFLARLQQQAYSVFVVKGDLPDCEADQLLQIISVEEMDTPKLNGKKLVKQKEHRVYKTVLEKVSEESDESGTSDQDEEDFQRALELSRQETNREDEHLRSTIELSMQGSSGNTSQDLPKTSCVTPASEQPKKIKEDYFEKHQQEQKQQQQQSDLPGHSSYLHERPTTSSRAIESDLSDDISEGTVQAAVDTILEIMRKNLKIKGEK
Protein: Translation initiation factor eIF2 assembly protein (Cell division cycle protein 123) (Q05791)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates the cell cycle in a nutrient dependent manner. Accumulates in presence of nutrients and directs the destabilization of DMA1 and DMA2, whose accumulation results in a G1 block. Regulates also the abundance of GCD11 an essential component of the translational initiation factor 2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit gamma
- E3 ubiquitin-protein ligase DMA1
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 2 subunit alpha
- E3 ubiquitin-protein ligase DMA2
Sequence:
MSSQEYTTFIDIPVTRAQVEHCSYSFWSSLYPKYVPKSIVLKSLPKKFIQYLEQDGIKLPQEENSRSVYTEEIIRNEDNDYSDWEDDEDTATEFVQEVEPLIDFPELHQKLKDALNELGAVAPKLNWSAPRDATWILPNNTMKCNEVNELYLLLNASNYIMHDLQRAFKGCVDGDDIKGLKFDLVLRQWCDMNPALEFRVFVKNAHIVGATQRDLNYYDYLDELSDTFKDLIDEIVHDVVLPKFPDKSFVLDVYIPRPFNKIFIVDINPFARKTDSLLFSWNEIAAIAPPKNDVEDYELRLVTRHNTGRFASKEHSENHVPQDLVEASLNPEAIRELTQKWKELLSQQAKEESSDSENET
Protein: Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (mGPAT3) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) (Q8C0N2)
Organism: Mus musculus (Mouse)
Function: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Protects cells against lipotoxicity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17170135}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol kinase
- Glycerol kinase 2
- Glycerol-3-phosphate dehydrogenase 1-like protein
- glycerol kinase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Acylglycerol kinase, mitochondrial
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MEGADLAVKLLSTWLTLVGGLILLPSAFGLSLGISEIYMKILVKTLEWATLRIQKGAPKESALKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEELVSWNLLTRTNVNFQYISPRLTMVWVLGVLVRYCFLLPLRVTLAFIGISLLIIGTTLVGQLPDSSLKNWLSELVHLTCCRICVRSLSGTIHYHNKQYRPQKGGICVANHTSPIDVLILATDGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEIKDRHLVTKRLKEHIADKKKLPILIFPEGTCINNTSVMMFKKGSFEIGGTIYPVAIKYNPQFGDAFWNSSKYNLVSYLLRIMTSWAIVCDVWYMPPMTREEGEDAVQFANRVKSAIAVQGGLTELPWDGGLKRAKVKDTFKEEQQKNYSKMIVGNGSPNLARD
Protein: Archaic translocase of outer membrane 12 kDa subunit (Q57VZ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFMMLNGTADGESRWNKVWQFTKTYARHVGSVYLSFLTPAALVIAYNAAMVTQDTERFGLAWMHYAGVQDEEEREQKFPAYEPGSAPQRKRLAAAGTREYVSSTA
Protein: Cytoplasmic dynein 2 light intermediate chain 1 (Q7SXY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system, facilitating the assembly of these organelles.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8TCX1}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8K0T2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TCX1}. Note=Localizes to the apical cytoplasm. {ECO:0000250|UniProtKB:Q8K0T2}.
Interaction partners:
- Cytoplasmic dynein 2 intermediate chain 1 isoform X2
- WD repeat domain 34
- Tctex1 domain-containing 2.
- Dynein cytoplasmic 2 heavy chain 1.
- Dynein light chain roadblock-type 2.
- Dynein light chain roadblock
- Dynein light chain Tctex-type 1
- Dynein light chain
- WD repeat-containing protein 35
- WD repeat domain 19.
Sequence:
MPKVSSDTLWDIAAAEVRSRESRTDEEEAEEEDAHFPSQRTVFFMGSKAGGKTTILLRFLERDETAKPTLALEYTFGRRARGHNTPKDIAHLWELGGGISLSDLVQIPITADNVSFLSVVLVLDLSKPNALWETMESLLGSARNQVEKVCAALQKTGESRSGKQRVPRVLHKDYPDRELISPFPVPLLIVGSKFDIFQDFDSEKRKVICKTLRFLAHFYGASLIFTSSKSETTMSKSRSFINQLAFGTERPKSISTDPSKPLAIPAGSDSLSQIGPPVATEVDIGTLHAKNPFDLWKKVFEKVFPHESTRERKELKDPVKDPQFSEPLIDSIRAQKDQELDQYKREQAKSWKSLALDP
Protein: Synaptosomal-associated protein (H3BV99)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIK
Protein: Laminin subunit beta 1 (D3ZQN7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Laminin subunit gamma-1
- Laminin subunit gamma-2
- CD44 antigen
- Laminin subunit alpha-5
- Laminin subunit alpha-2
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Integrin subunit alpha 5
- Collagen type IV alpha 1 chain
- Integrin beta-1
- Integrin alpha-1
Sequence:
MGVLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTVQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPFGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVVVVERRYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPHSMEYEILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQAGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSVSAFCDAVTGQCHCFQGIYARQCDRCLPGFWGFPSCQPCQCNGHAEDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDGCASGYFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQFCQHGYYGDALRQDCRKCVCNYLGTVREHCNGSDCHCDKTTGQCSCLPNVIGQNCDRCAPHTWQLASGTGCEPCNCNAVHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIRDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLSDTASRSNSTAGELDALQAEAGSLDKTVNELAEQLEFIKNSDIQGALDSITKYFQISLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTHPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLNALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATREKVDRSNEDLRNLIKQIRDFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEADYIEKVVYSVKQSADEVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL
Protein: ATP synthase subunit epsilon, mitochondrial (ATPase subunit epsilon) (P21306)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit H
- ATP synthase subunit delta, mitochondrial
Sequence:
MSAWRKAGISYAAYLNVAAQAIRSSLKTELQTASVLNRSQTDAFYTQYKNGTAASEPTPITK
Protein: Monofunctional chorismate mutase (EC 5.4.99.5) (Q9HU05)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme together with cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment comprises a complete three-step chorismate to phenylalanine pathway and accounts for the so called hidden overflow pathway to phenylalanine in P.aeruginosa, in which two possible routes for it exists, namely either via phenylpyruvate or L-arogenate.
Subcellular location: Periplasm {ECO:0000269|PubMed:11532214}.
Interaction partners:
- Cyclohexadienyl dehydratase
- Chorismate synthase
- Bifunctional chorismate mutase/prephenate dehydratase
- Aromatic-amino-acid aminotransferase
- Aspartate aminotransferase
- Anthranilate synthase component 2
- Anthranilate synthase component 1, pyocyanine specific
- Anthranilate synthase component 1
- Anthranilate synthase component 2, pyocyanine specific
- Salicylate biosynthesis isochorismate synthase
Sequence:
MRPSFASWGLLALLLLQGPLLQAQPLSPALQQLLSLSSQRLQLADQVAQSKAQSGKAVQDSPREEQQLQMLAGQAGSHGVGAEQVRLLFAAQIEANKLVQYRLLSRPLPDAGQAVDLERIRSRLNQLNLELLRGYAPALAELRVDDCRPRLNQALQRQVRVDRLDELHAIALSRAAGDLCHWAEL
Protein: GM07741p (Q95S67)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNKGRVTVVLHWDQRQGGGSGGGGGGGAGGGVGSMCSGLGSSNGLLSSDKYSPSKKGLSAQSSLDNKSVSSQSSQPRYASPQITVISDDGPASIYHPGGVVLPPGVVIPGGSRRLSKQGSSFDSTVGVGVGAVHVHTPECAHHAHTPSRAGSPSTTECDFHCCALHEEGRKIAVHKSVATSPIQDGSSSPQPQSAPSVMDPMLGGSGGGGSGSMQRRSSGAKGHVRFLDIAPERDSSESETENTVMEDDKTTTEKFLLLIDQLSVDQKRHLSIKDIGIILERLNSKILDVERLDRESESDDCYNWTIKATIRGDALRELGVIYNGNYYAISEHPGYKEELEENGEEVEEEEEEDEEDRI
Protein: Protein ARABIDILLO 2 (Q9M224)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes lateral root initiation and development, independently of auxin (IAA) and abscisis acid (ABA).
Subcellular location: Nucleus {ECO:0000269|PubMed:16434475}.
Interaction partners:
- U-box domain-containing protein 27
- Armadillo repeat only 1
- U-box domain-containing protein 5
Sequence:
MSRRVRQRVEDNGKYKVDSPSYTVIGVEDLAPKVQQYVNWTSLPYDTVFHLFTRLNYRDRASLASTCRTWRSLGASSFLWSSLDLRAHKFDLSMAASLATRCVDLQKIRFRGVDSADAIIHLKARSLLEISGDYCRKITDATLSMIAARHEALESLQLGPDFCERITSDAIRVIAFCCPKLKKLRVSGMRDVSSEAIESLAKHCPQLSDLGFLDCLNINEEALGKVVSLRYLSVAGTSNIKWKVALENWEKLPKLIGLDVSRTTIDHIAVSRLLKSSQSLKVLCALNCPYLEEDKSYSSNRFKGKVLLAVFTDTFDELASIFADNSKKPKNIFSYWRDLIRKDKSIDEIMLWIEWIISHTLLRIAESSNSQGLNDFWLNQGATLLLSLMQSAQEDVQERAATGLATFIVVDDENASIDCGRAEAVMRDGGIRLLLELAKSWREGLQSEAAKAIANLSVNAKVAKAVAEEGGISVLADLAKSMNRLVAEEAAGGLWNLSVGEEHKNAIAQAGGVNALVDLIFRWPHGCDGVLERAAGALANLAADDKCSMEVARAGGVHALVMLARNCKYEGAQEQAARALANLAAHGDSNGNNAAVGQEAGALEALVQLTQSPHEGVKQEAAGALWNLAFDDKNRESIAAFGGVEALVALAKSSSNASTGLQERVAGALWGLSVSEANSIAIGHEGGIPPLIALVRSEAEDVHETAAGALWNLSFNPGNALRIVEEGGVVALVQLCSSSVSKMARFMAALALAYMFDGRMDEYAMIGTSLESTSKSVTLNGARTMALDQIKAFIKTFMEHQIFSTGALSSAPSMLAQVSERARIPEAGHLRCSGSEIGRFVTMLRNPCLVLRACAAFALLQFTIPESRHAMHHASLMQNAGEARGLRSAAAAASMPREAKIFMKIVLRNLEHQQAESPEGMKVSYNRI