wanglab/gogpt-training-data huggingface dataset:
Protein: Glial cell line-derived neurotrophic family receptor-like, isoform L (A0A0B4KH06)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MLKPFAVIIGIFYLGSTIKGVVAILNCILARQLCFEDPSCSAILEIIPRVCGPIPVSCSTVTVTKCQAALRTLQAFQFFRPTCLCKEPGMDPDCNHFRDFLFDHPCGFVLKKAEKDPYPIDALPTCNHALSVCQQERKCLKLFEDFKTHCKVRDNKCKMENRDACHDSWTNLRLSPMFGCICPNNHMKKRCDRIFNIVNHNPCVDRLIFFPNGLPKLKQPRPKAKPRPKPKPKSKPKPRQRHHGMNGTELMTNNIEYHDEPNGLSDPEDEANETVDEDPGGHGDEDEDEEDDDYDDRIRAEIYSNYPHYLHPPSWGINNPLVLASHSPHTLDDDDDVVVEVVANKKPPPVTLHHHNDELDHDVVVVVDAGPHSHSHPHSHTFYSHGDQSSTTGSGLPGPAPTIPSPPNTGTKMHKTAPLGDLVAGSDITHRTYTGPSMDERVRILGMDEKLHQRIFNDNLALIDTPLIAMGSGSGSGTVTTSVSGYGLGMGMGLSGSFNYLGSMHGVPSYPFNISGFHQRHMAAAAADNEPFDIIDTGLGYGGNGNAGVYYQSGQDVEVDLSTEIIKQHFQSTCHTALDTCREDPSCSSSLQPMLTHCELHRCNRNACMSSLQAFYKGPHEDLNLDIAFCLCKKTSSQQNGNGNRHDMCMIAQEKLHPVCAQRPPDNSNPASSNGIYYHPPPACHVVADSCKEDRECRLKLEYYEQACAVDSVTKKCAGRPSGCRTAMIGILGTMLRTTCACQGTDPQHLYQCVGWRRLLWMNPCVVEAQKDFHMKRLAELGFLTTTTTTTTTTTTTTTTTTTRAPPPPPPPTTTTTTTTSMQPRQTPRKPATHIFKDVITAKEKSEPTSVEHNYLDPPDSIPLPSVNVESGGNGGNDDYHNGNGNGHGNGNGNGRRKNGGKGRGGSVDFDDPVIFVDPRETTEFVGISITEPVTTTTTTMATTTTTQPPRNCVVQRPRQSDQLIREGSSKRIYSLDDVECSELCSCGESLILTCHALCVPFAPCRTALAFYSHASPAYQAFRGRCLCYSGRFICMKPPLGEYILPGGIFLLLGYSAADEALLRPHTNLGVQDAVRALQQYVTTYIDNQTQCTLTLFNMTEENIIIAARLPHDGKLKDIELLRKEKDECTAILKTISHQINSEHSELQSHRLLSIFKMSEVEVVWPESTSAAARSGHGPGQFAGCDRLLYAAMLALAYLSSWTTLRMSDVATXQPHS
Protein: HEPACAM family member 2 (Mitotic kinetics regulator) (A8MVW5)
Organism: Homo sapiens (Human)
Function: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-tubulin ring complex and promotes centrosome maturation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Midbody {ECO:0000269|PubMed:22864114}. Note=In interphase, localizes to the Golgi apparatus. Localizes to centrosomes and spindles during prophase, prometaphase, and metaphase of mitosis, and to midbodies at telophase. Translocation to mitotic centrosomes is the result of poly-ADP-ribosylation (PARsylation). {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}.
Interaction partners:
Sequence:
MGQDAFMEPFGDTLGVFQCKIYLLLFGACSGLKVTVPSHTVHGVRGQALYLPVHYGFHTPASDIQIIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFPDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIHPPSGAVEYVGNMTLTCHVEGGTRLAYQWLKNGRPVHTSSTYSFSPQNNTLHIAPVTKEDIGNYSCLVRNPVSEMESDIIMPIIYYGPYGLQVNSDKGLKVGEVFTVDLGEAILFDCSADSHPPNTYSWIRRTDNTTYIIKHGPRLEVASEKVAQKTMDYVCCAYNNITGRQDETHFTVIITSVGLEKLAQKGKSLSPLASITGISLFLIISMCLLFLWKKYQPYKVIKQKLEGRPETEYRKAQTFSGHEDALDDFGIYEFVAFPDVSGVSRIPSRSVPASDCVSGQDLHSTVYEVIQHIPAQQQDHPE
Protein: Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog) (Q12872)
Organism: Homo sapiens (Human)
Function: Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Splicing factor 3A subunit 3
- Splicing factor 3A subunit 2
Sequence:
MYGASGGRAKPERKSGAKEEAGPGGAGGGGSRVELLVFGYACKLFRDDERALAQEQGQHLIPWMGDHKILIDRYDGRGHLHDLSEYDAEYSTWNRDYQLSEEEARIEALCDEERYLALHTDLLEEEARQEEEYKRLSEALAEDGSYNAVGFTYGSDYYDPSEPTEEEEPSKQREKNEAENLEENEEPFVAPLGLSVPSDVELPPTAKMHAIIERTASFVCRQGAQFEIMLKAKQARNSQFDFLRFDHYLNPYYKFIQKAMKEGRYTVLAENKSDEKKKSGVSSDNEDDDDEEDGNYLHPSLFASKKCNRLEELMKPLKVVDPDHPLAALVRKAQADSSTPTPHNADGAPVQPSQVEYTADSTVAAMYYSYYMLPDGTYCLAPPPPGIDVTTYYSTLPAGVTVSNSPGVTTTAPPPPGTTPLPPPTTAETSSGATSTTTTTSALAPVAAIIPPPPDVQPVIDKLAEYVARNGLKFETSVRAKNDQRFEFLQPWHQYNAYYEFKKQFFLQKEGGDSMQAVSAPEEAPTDSAPEKPSDAGEDGAPEDAAEVGARAGSGGKKEASSSKTVPDGKLVKASFAPISFAIKAKENDLLPLEKNRVKLDDDSDDDEESKEGQESSSSAANTNPAVAPPCVVVEEKKPQLTQEELEAKQAKQKLEDRLAAAAREKLAQASKESKEKQLQAERKRKAALFLQTLKNPLPEAEAGKIEESPFSVEESSTTPCPLLTGGRPLPTLEVKPPDRPSSKSKDPPREEEKEKKKKKHKKRSRTRSRSPKYHSSSKSRSRSHSKAKHSLPSAYRTVRRSRSRSRSPRRRAHSPERRREERSVPTAYRVSRSPGASRKRTRSRSPHEKKKKRRSRSRTKSKARSQSVSPSKQAAPRPAAPAAHSAHSASVSPVESRGSSQERSRGVSQEKEAQISSAIVSSVQSKITQDLMAKVRAMLAASKNLQTSAS
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q54G37)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- WD repeat-containing protein 48 homolog
- Anaphase-promoting complex subunit 4-like WD40 domain-containing protein
- 26S proteasome regulatory subunit 8
- RuvB-like helicase
- HECT-type E3 ubiquitin transferase
Sequence:
MGNNQTKSDLEKLYEKYPDFPKNQKLFGLENFGNTCYCNSVLQVLYFCVPFRNKILQYYCELKGLPPVVINNSNENNNNNNNNNNNSNNDTNNINNDSMNSNNNNSDNNNNNQNSNDSNNSNSSSGSSGSSSTSYFKNMFNFFGISGSSVNNNNNTNNNNNNNNSYGQSSSFSSSYNNSRNQEKEGNLIINLGELFYTIHQNKETHGCLKPETFVERLKKENELFSSFMHQDAHEFLNFLLNSIAEFLQKQQKNKQPQQSSEKKECNKTLVHEIFEGTLTNETKCLTCESITNKDESFLDLSIDIEQNKSLTNCLSNFSSIEILSKNDKFFCDQCNSLQEAQKRMKIKKLPNTLIIHLKRFKYMENIQQYTKLNYRVVFPFEIIIQNTTSNIDEPDKKFNLFAVVIHVGSGPNHGHYYSLIKCHGVWFVFDDHHIDIREESDIYDCFGSSNEFNNDCSYLLFYQCEDSSSNNKQK
Protein: Putative colanic acid biosynthesis glycosyl transferase WcaI (P32057)
Organism: Escherichia coli (strain K12)
Interaction partners:
- GDP-mannose mannosyl hydrolase
- Putative colanic acid biosynthesis acetyltransferase WcaF
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- GDP-mannose 4,6-dehydratase
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- GDP-L-fucose synthase
- Putative colanic acid biosynthesis glycosyl transferase WcaE
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- Putative colanic acid biosynthesis acetyltransferase WcaB
- Putative polysaccharide export protein Wza
Sequence:
MKILVYGINYSPELTGIGKYTGEMVEWLAAQGHEVRVITAPPYYPQWQVGENYSAWRYKREEGAATVWRCPLYVPKQPSTLKRLLHLGSFAVSSFFPLMAQRRWKPDRIIGVVPTLFCAPGMRLLAKLSGARTVLHIQDYEVDAMLGLGLAGKGKGGKVAQLATAFERSGLHNVDNVSTISRSMMNKAIEKGVAAENVIFFPNWSEIARFQHVADADVDALRNQLDLPDNKKIILYSGNIGEKQGLENVIEAADRLRDEPLIFAIVGQGGGKARLEKMAQQRGLRNMQFFPLQSYDALPALLKMGDCHLVVQKRGAADAVLPSKLTNILAVGGNAVITAEAYTELGQLCETFPGIAVCVEPESVEALVAGIRQALLLPKHNTVAREYAERTLDKENVLRQFINDIRG
Protein: Putrescine export system permease protein SapB (P0AGH3)
Organism: Escherichia coli (strain K12)
Function: Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Probable ABC transporter periplasmic-binding protein SapA
- Putrescine export system ATP-binding protein SapD
- Putrescine export system permease protein SapC
- Putrescine export system ATP-binding protein SapF
- Probable D,D-dipeptide-binding periplasmic protein DdpA
- Dipeptide transport system permease protein DppC
- Probable D,D-dipeptide transport system permease protein DdpC
- Glutathione transport system permease protein GsiD
- Nickel transport system permease protein NikC
- Dipeptide transport ATP-binding protein DppD
Sequence:
MIIFTLRRILLLIVTLFLLTFVGFSLSYFTPHAPLQGASLWNAWVFWFNGLIHWDFGVSSINGQPIAEQLKEVFPATMELCILAFGFALIVGIPVGMIAGITRHKWQDNLINAIALLGFSIPVFWLALLLTLFCSLTLGWLPVSGRFDLLYEVKPITGFALIDAWLSDSPWRDEMIMSAIRHMILPVITLSVAPTTEVIRLMRISTIEVYDQNYVKAAATRGLSRFTILRRHVLHNALPPVIPRLGLQFSTMLTLAMITEMVFSWPGLGRWLINAIRQQDYAAISAGVMVCGSLVIIVNVISDILGAMANPLKHKEWYALR
Protein: Barrier-to-autointegration factor A (Q6NTS2)
Organism: Xenopus laevis (African clawed frog)
Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy.
Subcellular location: Nucleus {ECO:0000269|PubMed:19167377}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. {ECO:0000250|UniProtKB:O75531}.
Interaction partners:
Sequence:
MSSTSQKHRDFVAEPMGEKSVQCLAGIGEALGHRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDICSANAKQSRDCYGCLKEWCDAFL
Protein: A kinase anchor protein 10 isoform 3 (A0A0S2Z4Y8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
Protein: Ribokinase (RK) (EC 2.7.1.15) (P0A9J6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305}.
Interaction partners:
- D-ribose pyranase
- Ribose operon repressor
- Ribose import permease protein RbsC
- Ribose import binding protein RbsB
- Ribose-phosphate pyrophosphokinase
- Ribose import ATP-binding protein RbsA
- Ribose-5-phosphate isomerase A
- Ribose-5-phosphate isomerase B
- Transketolase 1
- Transketolase 2
Sequence:
MQNAGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDAFLDRQR
Protein: Inactive serine/threonine-protein kinase TEX14 (Testis-expressed sequence 14) (Testis-expressed sequence 14 protein) (Q7M6U3)
Organism: Mus musculus (Mouse)
Function: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro.
Subcellular location: Cytoplasm. Midbody. Chromosome, centromere, kinetochore. Note=Detected in the intercellular bridges that connect male germ cell daughter cells after cell division.
Interaction partners:
Sequence:
MSRGAPFPVPCPVLLGTFTDDSLEAQLHEYAKQGNCVKLKKILKKGVCVDAVNTQGQSALFVAALLGHVKLVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKLLTAGGDLRLHDEKGRNPQAWALTAGKDRSTQMVEFMQRCTSHMKAIIQGFSYDLLKKIDSPQRLIGSPPWFGSLIQGSPNSSPNRQLKPGIISAQNIYSFGFGKFYLTSGMQLTYPGSLPVIGEKEVVQADDEPTFSFFSGPYMVMTNLVWNRSRVTVKELNLPTRPHCSRLRLADLLIAEQEHSSNLRHPNLLQLMAVCLSRDLEKIRLVYERITVGTLFSVLHERRSQFPVLHMEVIVHLLLQVADALIYLHSRGFIHRSLSSYAVHIVSAGEARLTNLEYLTESQDSGAHRNVTRMPLPTQLYNWAAPEVVLQKAATVKSDIYSFSVIIQEILTDSIPWNGLDGSLVKETIALGNYLEADVRLPEPYYDIVKSGIHAKQKNRTMNLQDIRYILKNDLKEFIGAQKTQPTESPRGQSYEPHPDVNICLGLTSEYQKDPPDLDIKELKEMGSQPHSPTDHSFLTVKPTLAPQTLDSSLSAQKPDNANVPSPPAACLAEEVRSPTASQDSLCSFEINEIYSGCLTLGTDKEEECLGTAASPEGDRPNQGDELPSLEEELDKMERELHCFCEEDKSISEVDTDLLFEDDDWQSDSLGSLNLPEPTREAKGKTSSWSKTDEYVSKCVLNLKISQVMMQQSAEWLRKLEQEVEELEWAQKELDSQCSSLRDASLKFANAKFQPAVGPPSLAYLPPVMQLPGLKQPENGGTWLTLARSPGNEREFQEGHFSKKPEKLSACGWKPFTQVSEESRGDCSELNNQLPTLRGPGKQSTGEQLPSTQEARESLEKNTNQNSRSMASVSSEIYATKSRNNEDNGEAHLKWRLAVKEMAEKAVSGQLLLPPWNPQSSAPFESKVENESTPLPRPPIRGPESTEWQHILEYQRENDEPKGNTKFGKMDNSDCDKNKHSRWTGLQRFTGIRYPFFRNHEQPEQNEASQASCDTSVGTEKFYSTSSPIGDDFERFQDSFAQRQGYVEENFQIREIFEKNAEILTKPQFQAIQCAEDKQDETLGETPKELKEKNTSLTDIQDLSSITYDQDGYFKETSYKTPKLKHAPTSASTPLSPESISSAASHYEDCLENTTFHVKRGSTFCWNGQEAMRTLSAKFTTVRERAKSLESLLASSKSLPAKLTDSKRLCMLSETGSSNVSAAFVTSTHATKRKSLPRELAEATSQQHLDELPPPAQELLDEIEQLKQQQVSSLASHENTARDLSVTNKDKKHLEEQETNSSKDSSFLSSREIQDLEDTERAHSSLDEDLERFLQSPEENTALLDPTKGSTREKKNKDQDVVEQKRKKKESIKPERRESDSSLGTLEEDELKPCFWKRLGWSEPSRIIVLDQSDLSD
Protein: Eukaryotic aspartyl protease family protein (Q9M356)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alcohol dehydrogenase-like protein
- Alcohol dehydrogenase-like protein
- AIG2-like protein D
- TORTIFOLIA1-like protein 3
Sequence:
MERKVLNTLAFSVFAVLFFTSSASSQYQTLVVNTLPSSATLSWPESESLTDESLSESTTSLSVHLSHVDALSSFSDASPADLFNLRLQRDSLRVKSITSLAAVSTGRNATKRTPRTAGGFSGAVISGLSQGSGEYFMRLGVGTPATNVYMVLDTGSDVVWLQCSPCKACYNQTDAIFDPKKSKTFATVPCGSRLCRRLDDSSECVTRRSKTCLYQVSYGDGSFTEGDFSTETLTFHGARVDHVPLGCGHDNEGLFVGAAGLLGLGRGGLSFPSQTKNRYNGKFSYCLVDRTSSGSSSKPPSTIVFGNAAVPKTSVFTPLLTNPKLDTFYYLQLLGISVGGSRVPGVSESQFKLDATGNGGVIIDSGTSVTRLTQPAYVALRDAFRLGATKLKRAPSYSLFDTCFDLSGMTTVKVPTVVFHFGGGEVSLPASNYLIPVNTEGRFCFAFAGTMGSLSIIGNIQQQGFRVAYDLVGSRVGFLSRAC
Protein: Photoreceptor-specific nuclear receptor (Nuclear receptor subfamily 2 group E member 3) (Retina-specific nuclear receptor) (Q9Y5X4)
Organism: Homo sapiens (Human)
Function: Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:15689355}.
Interaction partners:
- Cone-rod homeobox protein
- Neural retina-specific leucine zipper protein
- Rhodopsin
- Peripherin-2
- Retinoid isomerohydrolase
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Tubby-related protein 1
- Ceramide kinase-like protein
- U4/U6 small nuclear ribonucleoprotein Prp31
- Protein eyes shut homolog
Sequence:
METRPTALMSSTVAAAAPAAGAASRKESPGRWGLGEDPTGVSPSLQCRVCGDSSSGKHYGIYACNGCSGFFKRSVRRRLIYRCQVGAGMCPVDKAHRNQCQACRLKKCLQAGMNQDAVQNERQPRSTAQVHLDSMESNTESRPESLVAPPAPAGRSPRGPTPMSAARALGHHFMASLITAETCAKLEPEDADENIDVTSNDPEFPSSPYSSSSPCGLDSIHETSARLLFMAVKWAKNLPVFSSLPFRDQVILLEEAWSELFLLGAIQWSLPLDSCPLLAPPEASAAGGAQGRLTLASMETRVLQETISRFRALAVDPTEFACMKALVLFKPETRGLKDPEHVEALQDQSQVMLSQHSKAHHPSQPVRFGKLLLLLPSLRFITAERIELLFFRKTIGNTPMEKLLCDMFKN
Protein: Flagellar P-ring protein (Basal body P-ring protein) (P0A6S3)
Organism: Escherichia coli (strain K12)
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular location: Periplasm. Bacterial flagellum basal body.
Interaction partners:
- Basal-body rod modification protein FlgD
- Peptidoglycan hydrolase FlgJ
- Flagellar basal body rod protein FlgB
- Flagellar L-ring protein
- Flagellar basal-body rod protein FlgC
- Flagellar M-ring protein
- Flagellar hook protein FlgE
- Flagellar basal-body rod protein FlgF
- Flagellar basal-body rod protein FlgG
- Flagellar motor switch protein FliM
Sequence:
MIKFLSALILLLVTTAAQAERIRDLTSVQGVRQNSLIGYGLVVGLDGTGDQTTQTPFTTQTLNNMLSQLGITVPTGTNMQLKNVAAVMVTASLPPFGRQGQTIDVVVSSMGNAKSLRGGTLLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAVIERELPSQFGVGNTLNLQLNDEDFSMAQQIADTINRVRGYGSATALDARTIQVRVPSGNSSQVRFLADIQNMQVNVTPQDAKVVINSRTGSVVMNREVTLDSCAVAQGNLSVTVNRQANVSQPDTPFGGGQTVVTPQTQIDLRQSGGSLQSVRSSASLNNVVRALNALGATPMDLMSILQSMQSAGCLRAKLEII
Protein: NADH-ubiquinone oxidoreductase chain 2 (EC 7.1.1.2) (NADH dehydrogenase subunit 2) (P03893)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Cytochrome b
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Cytochrome c oxidase subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MNPITLAIIYFTIFLGPVITMSSTNLMLMWVGLEFSLLAIIPMLINKKNPRSTEAATKYFVTQATASMIILLAIVLNYKQLGTWMFQQQTNGLILNMTLMALSMKLGLAPFHFWLPEVTQGIPLHMGLILLTWQKIAPLSILIQIYPLLNSTIILMLAITSIFMGAWGGLNQTQMRKIMAYSSIAHMGWMLAILPYNPSLTLLNLMIYIILTAPMFMALMLNNSMTINSISLLWNKTPAMLTMISLMLLSLGGLPPLTGFLPKWIIITELMKNNCLIMATLMAMMALLNLFFYTRLIYSTSLTMFPTNNNSKMMTHQTKTKPNLMFSTLAIMSTMTLPLAPQLIT
Protein: Phospholipid-transporting ATPase 3 (AtALA3) (EC 7.6.2.1) (Aminophospholipid ATPase 3) (Aminophospholipid flippase 3) (Protein ABERRANT LOCALIZATION OF PEN3 3) (Protein IRREGULAR TRICHOME BRANCH 2) (Q9XIE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Required for secretory processes during plant development. Requires an interaction with an ALIS protein for activity. Has activity with phosphatidylserine, phosphatidylcholine and phosphatidylethanolamine, but not with lysolipid. Modifies endomembranes in multiple cell types, enabling structural changes, or signaling functions that are critical for normal development and adaptation to varied growth environments. Required for the trafficking and endocytic recycling of ABCG36/PEN3 between the trans-Golgi network and the plasma membrane; thus promoting ABCG36/PEN3 recruitment to the host-pathogen interface upon infection by powdery mildews (e.g. Blumeria graminis) and bacteria (e.g. Pseudomonas syringae), or upon the detection of pathogen-associated molecular patterns (PAMPs) (e.g. flg22 and chitin).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000255}. Note=Requires the presence of an ALIS protein to exit the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:20053675}.
Interaction partners:
- ALA-interacting subunit 1
- ALA-interacting subunit 5
- ALA-interacting subunit 3
- Brefeldin A-inhibited guanine nucleotide-exchange protein 3
- RING/U-box superfamily protein
Sequence:
MVRSGSFSVDSSATHQRTPSRTVTLGHIQPQAPTYRTVYCNDRESNQPVRFKGNSISTTKYNVFTFLPKGLFEQFRRIANIYFLGISCLSMTPISPVSPITNVAPLSMVLLVSLIKEAFEDWKRFQNDMSINNSTVEILQDQQWVSIPWRKLQVGDIVKIKKDGFFPADILFMSSTNSDGICYVETANLDGETNLKIRKALERTWDYLVPEKAYEFKGEIQCEQPNNSLYTFTGNLVVQKQTLPLSPDQLLLRGCSLRNTEYIVGAVVFTGHETKVMMNAMNAPSKRSTLEKKLDKLIITIFCVLVTMCLIGAIGCSIVTDREDKYLGLHNSDWEYRNGLMIGFFTFFTLVTLFSSIIPISLYVSIEMIKFIQSTQFINRDLNMYHAETNTPASARTSNLNEELGQVEYIFSDKTGTLTRNLMEFFKCSIGGVSYGCGVTEIEKGIAQRHGLKVQEEQRSTGAIREKGFNFDDPRLMRGAWRNEPNPDLCKELFRCLAICHTVLPEGDESPEKIVYQAASPDEAALVTAAKNFGFFFYRRTPTMVYVRESHVEKMGKIQDVAYEILNVLEFNSTRKRQSVVCRFPDGRLVLYCKGADNVIFERLANGMDDVRKVTREHLEHFGSSGLRTLCLAYKDLNPETYDSWNEKFIQAKSALRDREKKLDEVAELIEKDLILIGSTAIEDKLQEGVPTCIETLSRAGIKIWVLTGDKMETAINIAYACNLINNEMKQFVISSETDAIREAEERGDQVEIARVIKEEVKRELKKSLEEAQHSLHTVAGPKLSLVIDGKCLMYALDPSLRVMLLSLSLNCTSVVCCRVSPLQKAQVTSLVRKGAQKITLSIGDGANDVSMIQAAHVGIGISGMEGMQAVMASDFAIAQFRFLTDLLLVHGRWSYLRICKVVMYFFYKNLTFTLTQFWFTFRTGFSGQRFYDDWFQSLFNVVFTALPVIVLGLFEKDVSASLSKRYPELYREGIRNSFFKWRVVAVWATSAVYQSLVCYLFVTTSSFGAVNSSGKVFGLWDVSTMVFTCLVIAVNVRILLMSNSITRWHYITVGGSILAWLVFAFVYCGIMTPHDRNENVYFVIYVLMSTFYFYFTLLLVPIVSLLGDFIFQGVERWFFPYDYQIVQEIHRHESDASKADQLEVENELTPQEARSYAISQLPRELSKHTGFAFDSPGYESFFASQLGIYAPQKAWDVARRASMRSRPKVPKK
Protein: Sterile alpha motif domain containing 9 (C9JKF1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKQLNLPENTDDWTKEDVNQWLESHKIDQKHREILTEQDVNGAVLKWLKKEHLVDMGITHGPAIQIEELFKELRKTAIEDSIQTSKMGKPSKNAPKDQTVSQKERRETSKQKQKGKENPDMANPSAMSTTAKGSKSLKVELIEDKIDYTKERQPSIDLTCVSYPFDEFSNPYRYKLDFSLQPETGPGNLIDPIHEFKAFTNTATATEEDVKMKFSNEVFRFASACMNSRTNGTIHFGVKDKPHGKIVGIKVTNDTKEALINHFNLMINKYFEDHQVQQAKKCIREPRFVEVLLPNSTLSDRFVIEVDIIPQFSECQYDYFQIKMQNYNNKIWEQSKKFSLFVRDGTSSKDITKNKVDFRAFKADFKTLAESRKAAEEKFRAKTNKKEREGPKLVKLLTGNQDLLDNSYYEQYILVTNKCHPDQTKHLDFLKEIKWFAVLEFDPESNINGVVKAYKESRVANLHFPSVYVEQKTTPNETISTLNLYHQPSWIFCNGRLDLDSEKYKPFDPSSWQRERASDVRKLISFLTHEDIMPRGKFLVVFLLLSSVDDPRDPLIETFCAFYQDLKGMENILCICVHPHIFQGWKDLLEARLIKHQDEISSQCISALSLEEINGTILKLKSVTQSSKRLLPSIGLSTVLLKKEEDIMTALEIICENECEGTLLEKDKNKFLEFKASKEEDFYRGGKVSWWNFYFSSESYSSPFVKRDKYERLEAMIQNCADSSKPTSTKIIHLYHHPGCGGTTLAMHILWELRKKFRCAVLKNKTVDFSEIGEQVTSLITYGAMNRQEYVPVLLLVDDFEEQDNVYLLQYSIQTAIAKKYIRYEKPLVIILNCMRSQNPEKSARIPDSIAVIQQLSPKEQRAFELKLKEIKEQHKNFEDFYSFMIMKTNFNKEYIENVVRNILKGQNIFTKEAKLFSFLALLNSYVPDTTISLSQCEKFLGIGNKKAFWGTEKFEDKMGTYSTILIKTEVIECGNYCGVRIIHSLIAEFSLEELKKSYHLNKSQIMLDMLTENLFFDTGMGKSKFLQDMHTLLLTRHRDEHEGETGNWFSPFIEALHKDEGNEAVEAVLLESIHRFNPNAFICQALARHFYIKKKDFGNALNWAKQAKIIEPDNSYISDTLGQVYKSKIRWWIEENGGNGNISVDDLIALLDLAEHASSAFKESQQQSEDREYEVKERLYPKSKRRYDTYNIAGYQGEIEVGLYTIQILQLIPFFDNKNELSKRYMVNFVSGSSDIPGDPNNEYKLALKNYIPYLTKLKFSLKKSFDFFDEYFVLLKPRNN