wanglab/gogpt-training-data huggingface dataset:
Protein: Multiple epidermal growth factor-like domains protein 11 (Multiple EGF-like domains protein 11) (A6BM72)
Organism: Homo sapiens (Human)
Function: May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Basolateral cell membrane {ECO:0000269|PubMed:17498693}; Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}. Note=Forms an irregular, mosaic-like adhesion pattern in region of the cell that becomes firmely fixed to the substrate. Localized to protruding lamellipodia. Does not localize with MEGF10.
Interaction partners:
- Intraflagellar transport protein 122 homolog
Sequence:
MVLSLTGLIAFSFLQATLALNPEDPNVCSHWESYAVTVQESYAHPFDQIYYTRCTDILNWFKCTRHRISYKTAYRRGLRTMYRRRSQCCPGYYESGDFCIPLCTEECVHGRCVSPDTCHCEPGWGGPDCSSGCDSDHWGPHCSNRCQCQNGALCNPITGACVCAAGFRGWRCEELCAPGTHGKGCQLPCQCRHGASCDPRAGECLCAPGYTGVYCEELCPPGSHGAHCELRCPCQNGGTCHHITGECACPPGWTGAVCAQPCPPGTFGQNCSQDCPCHHGGQCDHVTGQCHCTAGYMGDRCQEECPFGSFGFQCSQHCDCHNGGQCSPTTGACECEPGYKGPRCQERLCPEGLHGPGCTLPCPCDADNTISCHPVTGACTCQPGWSGHHCNESCPVGYYGDGCQLPCTCQNGADCHSITGGCTCAPGFMGEVCAVSCAAGTYGPNCSSICSCNNGGTCSPVDGSCTCKEGWQGLDCTLPCPSGTWGLNCNESCTCANGAACSPIDGSCSCTPGWLGDTCELPCPDGTFGLNCSEHCDCSHADGCDPVTGHCCCLAGWTGIRCDSTCPPGRWGPNCSVSCSCENGGSCSPEDGSCECAPGFRGPLCQRICPPGFYGHGCAQPCPLCVHSSRPCHHISGICECLPGFSGALCNQVCAGGYFGQDCAQLCSCANNGTCSPIDGSCQCFPGWIGKDCSQACPPGFWGPACFHACSCHNGASCSAEDGACHCTPGWTGLFCTQRCPAAFFGKDCGRVCQCQNGASCDHISGKCTCRTGFTGQHCEQRCAPGTFGYGCQQLCECMNNSTCDHVTGTCYCSPGFKGIRCDQAALMMEELNPYTKISPALGAERHSVGAVTGIMLLLFLIVVLLGLFAWHRRRQKEKGRDLAPRVSYTPAMRMTSTDYSLSGACGMDRRQNTYIMDKGFKDYMKESVCSSSTCSLNSSENPYATIKDPPILTCKLPESSYVEMKSPVHMGSPYTDVPSLSTSNKNIYEVEPTVSVVQEGCGHNSSYIQNAYDLPRNSHIPGHYDLLPVRQSPANGPSQDKQS
Protein: Alpha-2-macroglobulin (Alpha-2-M) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5) (P01023)
Organism: Homo sapiens (Human)
Function: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
Subcellular location: Secreted {ECO:0000269|PubMed:6203908}.
Interaction partners:
- Apolipoprotein A-I
- Prolow-density lipoprotein receptor-related protein 1
- Haptoglobin
- Kallikrein-4
- Interleukin-1 beta
- Albumin
- Alpha-1-antitrypsin
- Apolipoprotein E
- Endoplasmic reticulum chaperone BiP
- Alpha-2-antiplasmin
Sequence:
MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFRQGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLTVRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHYILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARLLIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAVDQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDNEDCINRHNVYINGITYTPVSSTNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARLVHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVEKEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVIKPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQNTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKHYDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCFRSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDHGSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQAPSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHALSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEGCVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAIVDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVRDLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA
Protein: Colicin-N (P08083)
Organism: Escherichia coli
Function: This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGSNGADNAHNNAFGGGKNPGIGNTSGAGSNGSASSNRGNSNGWSWSNKPHKNDGFHSDGSYHITFHGDNNSKPKPGGNSGNRGNNGDGASAKVGEITITPDNSKPGRYISSNPEYSLLAKLIDAESIKGTEVYTFHTRKGQYVKVTVPDSNIDKMRVDYVNWKGPKYNNKLVKRFVSQFLLFRKEEKEKNEKEALLKASELVSGMGDKLGEYLGVKYKNVAKEVANDIKNFHGRNIRSYNEAMASLNKVLANPKMKVNKSDKDAIVNAWKQVNAKDMANKIGNLGKAFKVADLAIKVEKIREKSIEGYNTGNWGPLLLEVESWIIGGVVAGVAISLFGAVLSFLPISGLAVTALGVIGIMTISYLSSFIDANRVSNINNIISSVIR
Protein: Serine-repeat antigen protein 5 (EC 3.4.22.-) (111 kDa antigen) (Serine protease SERA5) (p126) [Cleaved into: p47 (SER36); p56; p50; p18; p25n; p25c] (Q9TY95)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Plays an essential role during the asexual blood stage development by controlling the kinetics of merozoite egress from host erythrocytes. Specifically, prevents premature rupture of the parasitophorous vacuole and host erythrocyte membranes.
Subcellular location: [Serine-repeat antigen protein 5]: Parasitophorous vacuole {ECO:0000269|PubMed:25599609, ECO:0000269|PubMed:28683142, ECO:0000269|PubMed:29716996, ECO:0000305|PubMed:18083098}. Note=Secreted in large amount into the parasitophorous vacuole. {ECO:0000305|PubMed:18083098}.; SUBCELLULAR LOCATION: [p18]: Secreted {ECO:0000250|UniProtKB:P69193}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000250|UniProtKB:P69193}.; SUBCELLULAR LOCATION: [p25n]: Secreted. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000250|UniProtKB:P69193}.; SUBCELLULAR LOCATION: [p25c]: Secreted {ECO:0000250|UniProtKB:P69193}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000250|UniProtKB:P69193}.; SUBCELLULAR LOCATION: [p47]: Secreted {ECO:0000250|UniProtKB:P69193}. Cell membrane {ECO:0000269|PubMed:29567995}; Peripheral membrane protein {ECO:0000269|PubMed:29567995}; Extracellular side {ECO:0000250|UniProtKB:P69193}. Note=Secreted during merozoite egress from erythrocytes (By similarity). Colocalizes at the merozoite surface with human VTN (PubMed:29567995). {ECO:0000250|UniProtKB:P69193, ECO:0000269|PubMed:29567995}.; SUBCELLULAR LOCATION: [p50]: Secreted {ECO:0000269|PubMed:18083098, ECO:0000269|PubMed:25599609}. Note=Secreted during egress from host erythrocytes. {ECO:0000269|PubMed:25599609}.; SUBCELLULAR LOCATION: [p56]: Secreted {ECO:0000269|PubMed:18083098}. Note=Secreted during egress from host erythrocytes. {ECO:0000269|PubMed:25599609}.
Interaction partners:
- Uncharacterized protein
- Merozoite surface protein 9
Sequence:
MKSYISLFFILCVIFNKNVIKCTGESQTGNTGGGQAGNTGGDQAGSTGGSPQGSTGASPQGSTGASPQGSTGASQPGSSEPSNPVSSGHSVSTVSVSQTSTSSEKQDTIQVKSALLKDYMGLKVTGPCNENFIMFLVPHIYIDVDTEDTNIELRTTLKKTNNAISFESNSGSLEKKKYVKLPSNGTTGEQGSSTGTVRGDTEPISDSSSSSSSSSSSSSSSSSSSSSSSSSSSESLPANGPDSPTVKPPRNLQNICETGKNFKLVVYIKENTLILKWKVYGETKDTTENNKVDVRKYLINEKETPFTNILIHAYKEHNGTNLIESKNYAIGSDIPEKCDTLASNCFLSGNFNIEKCFQCALLVEKENKNDVCYKYLSEDIVSKFKEIKAETEDDDEDDYTEYKLTESIDNILVKMFKTNENNDKSELIKLEEVDDSLKLELMNYCSLLKDVDTTGTLDNYGMGNEMDIFNNLKRLLIYHSEENINTLKNKFRNAAVCLKNVDDWIVNKRGLVLPELNYDLEYFNEHLYNDKNSPEDKDNKGKGVVHVDTTLEKEDTLSYDNSDNMFCNKEYCNRLKDENNCISNLQVEDQGNCDTSWIFASKYHLETIRCMKGYEPTKISALYVANCYKGEHKDRCDEGSSPMEFLQIIEDYGFLPAESNYPYNYVKVGEQCPKVEDHWMNLWDNGKILHNKNEPNSLDGKGYTAYESERFHDNMDAFVKIIKTEVMNKGSVIAYIKAENVMGYEFSGKKVQNLCGDDTADHAVNIVGYGNYVNSEGEKKSYWIVRNSWGPYWGDEGYFKVDMYGPTHCHFNFIHSVVIFNVDLPMNNKTTKKESKIYDYYLKASPEFYHNLYFKNFNVGKKNLFSEKEDNENNKKLGNNYIIFGQDTAGSGQSGKESNTALESAGTSNEVSERVHVYHILKHIKDGKIRMGMRKYIDTQDVNKKHSCTRSYAFNPENYEKCVNLCNVNWKTCEEKTSPGLCLSKLDTNNECYFCYV
Protein: SD10763p (Q95ST8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPVSGCLPTATHSLQDMSAAAAAIALDMKPKLEPHPLAAATAMPSQKIKKCAYTDLFPTFMQTYVHTYVYMYNFYAKCSRKSIRRTSSRIYFISSLPIQIVRFTLCAMYIHIRTYVCMYIWVNKVRLIEVLRCLYRAFLKYSTVETRGLILFAFIFVSQQWFGATPPTS
Protein: Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic (EC 1.2.1.12) (Glyceraldehyde-3-phosphate dehydrogenase of plastid 2) (NAD-dependent glyceraldehydephosphate dehydrogenase chloroplastic 2) (Q5E924)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plastidial glycolytic pathway and plays a specific role in glycolytic energy production in non-green plastids and chloroplasts. Essential for breakdown of starch to form sucrose for export to non-photosynthetic tissues, and to generate primary metabolites for anabolic pathways such as fatty acid and amino acid synthesis. Plays an important role in plant development by providing substrates for the phosphorylated pathway of serine biosynthesis in roots. Plays a crucial role in pollen development. Functionally redundant with GAPCP1.
Subcellular location: Plastid, chloroplast stroma {ECO:0000305|PubMed:19675149}.
Interaction partners:
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, chloroplastic
- Phosphoribulokinase, chloroplastic
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- transaldolase
Sequence:
MALSSLLRSAATSAAAPRVELYPSSSYNHSQVTSSLGFSHSLTSSRFSGAAVSTGKYNAKRVQPIKATATEAPPAVHRSRSSGKTKVGINGFGRIGRLVLRIATFRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNYKGTINVIDDSTLEINGKQVKVVSKRDPAEIPWADLGAEYVVESSGVFTTVGQASSHLKGGAKKVIISAPSADAPMFVVGVNEKTYLPNMDIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKDASYEDVKAAIKFASEGPLRGILGYTEEDVVSNDFLGDSRSSIFDANAGIGLSKSFMKLVSWYDNEWGYSNRVLDLIEHMALVAASR
Protein: Guanine nucleotide-binding protein subunit gamma 2 (Ggamma-subunit 2) (Heterotrimeric G protein gamma-subunit 2) (AtAGG2) (Q93V47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the abscisic acid (ABA) and ethylene signaling pathways. Regulates basipetal transport of auxin (IAA) in roots and hypocotyls, and thus modulates root architecture (e.g. lateral root formation). The heterotrimeric G-protein controls defense responses to necrotrophic and vascular fungi probably by modulating cell wall-related genes expression; involved in resistance to Plectosphaerella cucumerina.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:17220359, ECO:0000269|PubMed:22068106}. Note=Localized to the cell membrane when attached to beta subunit GB1.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein alpha-1 subunit
- Extra-large guanine nucleotide-binding protein 2
- Guanine nucleotide-binding protein subunit gamma 3
- Extra-large guanine nucleotide-binding protein 1
- Guanine nucleotide-binding protein subunit gamma 1
- Extra-large guanine nucleotide-binding protein 3
- Chitin elicitor receptor kinase 1
- Regulator of G-protein signaling 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
Sequence:
MEAGSSNSSGQLSGRVVDTRGKHRIQAELKRLEQEARFLEEELEQLEKMDNASASCKEFLDSVDSKPDPLLPETTGPVNATWDQWFEGPKEAKRCGCSIL
Protein: Down syndrome cell adhesion molecule 3, isoform D (LP21844p) (Q6IDE9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLLEPPCLVLEKALLLGALLLAVLATPLLATSGLRVPTFLLEPAPRLLFGNDTGAQVTCTAHGSPPPLVTWVLRDGSLATQVPGLRKISGNGTLHFPPFLAQYYRTDVHEATYRCRASNEAGTVLSRNVQVHAVVRRQFHVHVENTEVYLGNSALIKCAIPEYVRPYVRVASWHRGEEILLPDLSDVAGRYVVLAASGDLYVRSVRSEDGLMKFSCLVTNTLNGERQRSDAVMLQVKELSKNLAPRTTQKPVMEIHVERGNDVHLPCNIQGNPFPIFTWYRVSDSAALYPIPSSQRVILSRTLLLIKNADERDAGKWICQASNQFGEQRIEIRLSVNSYVSVHILPQVQIVNSGGTANFNCTTTGSAIDAIDWLHNGKPLQANNALTTGRDNIRFLSKSSLLVQNVGRRDRGVYQCLVENQRASAQAMAELKLGDTVPELIYTFIEQNVRPGPLISLKCSASGSPPPQFAWLLDSQPIMDVSLHHRFAIGQFVDMSGDVISHLNISHVRPDDGGLYKCVASNSMGSVQHSARLNVYGPPYVRAIGPIKAVAGEDIIVHCPFAGYPVEQIRWEKAHQELTTSNHYELASVADGGQLVIKNVEPGRDQGIYTCIVRSRAGEEARRDMQLNVNSPPVIEPFKFPKNLQEGGRAQITCAVSSGDMPIYFSWKKDDSSIPSSLQITEKKEEFYSLLVFKDISARHSGKYTCYASNAAAKVNYTAELQVRVAPRWRYEPMDTAIMLGNTISINCEAEGYPIPTITWFKGQGKGSKDFKPLSMRNHSLLLNLATDNDEGYYMCQATNEIGAGLKKTIRINVNEPARFEQSARNISSRRNDPVTLDCHAKGDEPITIGWTQNNGRIDLNNFRFSIAEMKTEKGVDSQLTIGHSDRHDSGVYRCIAENPYGRAEQIIFLAVQERPDTPSHLEIFEVGSRTVKLSWRRPFDGNSPVLSYLVQYQALKYLQSHGSLAAAGGDWNGHVINVSLPSTSISRRYVFMLEIFLASQSATL
Protein: Gamma-aminobutyric acid receptor subunit gamma-3 (GABA(A) receptor subunit gamma-3) (GABAAR subunit gamma-3) (P27681)
Organism: Mus musculus (Mouse)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99928}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q99928}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Huntingtin-associated protein 1
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Trafficking protein, kinesin binding 2
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Gamma-aminobutyric acid receptor subunit beta-2
Sequence:
MAAKLLLLLCLFSGLHARSRRVEEDENEDSPSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDAHACPLTFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTTLGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTIRKKKTSLLHPDSTRWIPDRISLQAPSNYSLLDMRPPPPVMITLNNSMYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRRGRIHIDVSELDSYSRVFFPTSFLLFNLVYWVGYLYL
Protein: Glutamate dehydrogenase 1, mitochondrial (EC 1.4.1.3) (Q70PJ6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
SVSFPIKRDNGEWEVIEGYRAQHSQHRTPCKGGIRYSTEVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINVKNYTDNELEKITRRFTIELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYANTMGHHDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEAAYMSQLGLSPGFTDKTFVIQGFGNVGMHSMRYLHRFGAKCVGVGEMDGNIWNPNGIDPKELEDYKLQHGTIVGFPNSTPYEGSILEADCDILIPAASEKQLTRNNAHKIKAKIIAEGANGPTTPDADKIFLERNIMVIPDMYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGAIPVVPTSEFQARIAGASEKDIVHSGLAYTMERSARQIMRTANKYNLGLDLRTATYVNAIEKVFKVYNEAGLTFT
Protein: Renin (EC 3.4.23.15) (Angiotensinogenase) (P08424)
Organism: Rattus norvegicus (Rat)
Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P00797}. Membrane {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
Interaction partners:
- Renin receptor
- Angiotensinogen
- Type-2 angiotensin II receptor
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme 2
- Type-1 angiotensin II receptor A
- Mineralocorticoid receptor
- Natriuretic peptides A
- Kininogen-1
Sequence:
MGGRRMPLWALLLLWTSCSFSLPTDTASFGRILLKKMPSVREILEERGVDMTRISAEWGEFIKKSSFTNVTSPVVLTNYLDTQYYGEIGIGTPSQTFKVIFDTGSANLWVPSTKCGPLYTACEIHNLYDSSESSSYMENGTEFTIHYGSGKVKGFLSQDVVTVGGIIVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVDGVIPVFDHILSQRVLKEEVFSVYYSRESHLLGGEVVLGGSDPQHYQGNFHYVSISKAGSWQITMKGVSVGPATLLCEEGCMAVVDTGTSYISGPTSSLQLIMQALGVKEKRANNYVVNCSQVPTLPDISFYLGGRTYTLSNMDYVQKNPFRNDDLCILALQGLDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR
Protein: Sirohydrochlorin cobaltochelatase (EC 4.99.1.3) (Anaerobic cobalt chelatase) (Q05592)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Interaction partners:
- Cobalt-precorrin-4 C
- Cobalt-precorrin-5A hydrolase
- Cobalt-precorrin-2 C
- Cobalt-precorrin-5B C
- Cobalt-precorrin-6A reductase
- Probable cobalt-factor III C
- Cobyrinate a,c-diamide synthase
- Cobalt-precorrin-8 methylmutase
- Cobalt-precorrin-7 C
- Siroheme synthase
Sequence:
MKKALLVVSFGTSYHDTCEKNIVACERDLAASCPDRDLFRAFTSGMIIRKLRQRDGIDIDTPLQALQKLAAQGYQDVAIQSLHIINGDEYEKIVREVQLLRPLFTRLTLGVPLLSSHNDYVQLMQALRQQMPSLRQTEKVVFMGHGASHHAFAAYACLDHMMTAQRFPARVGAVESYPEVDILIDSLRDEGVTGVHLMPLMLVAGDHAINDMASDDGDSWKMRFNAAGIPATPWLSGLGENPAIRAMFVAHLHQALNMAVEEAA
Protein: Chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CsGalNAcT-1) (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1) (Beta4GalNAcT-1) (Q8TDX6)
Organism: Homo sapiens (Human)
Function: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. Important role in chondroitin chain biosynthesis in cartilage formation and subsequent endochondral ossification. Moreover, is involved in the metabolism of aggrecan (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:11788602}; Single-pass type II membrane protein {ECO:0000305|PubMed:11788602}.
Interaction partners:
- Chondroitin sulfate synthase 2
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Chondroitin sulfate glucuronyltransferase
- Chondroitin sulfate synthase 1
- Chondroitin sulfate synthase 3
Sequence:
MMMVRRGLLAWISRVVVLLVLLCCAISVLYMLACTPKGDEEQLALPRANSPTGKEGYQAVLQEWEEQHRNYVSSLKRQIAQLKEELQERSEQLRNGQYQASDAAGLGLDRSPPEKTQADLLAFLHSQVDKAEVNAGVKLATEYAAVPFDSFTLQKVYQLETGLTRHPEEKPVRKDKRDELVEAIESALETLNSPAENSPNHRPYTASDFIEGIYRTERDKGTLYELTFKGDHKHEFKRLILFRPFGPIMKVKNEKLNMANTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRVHLTVVYFGKEEINEVKGILENTSKAANFRNFTFIQLNGEFSRGKGLDVGARFWKGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGIIYGHHDAVPPLEQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKMCMQSKAMNEASHGQLGMLVFRHEIEAHLRKQKQKTSSKKT
Protein: Contig An12c0290, genomic contig (A2R0G9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSGLNPGDSFPADVTFSYIPWSEEKGEITACGIPINYYASKEWADKKVILFALPGAFTPVCSARHVPEYLEKLPEIRAKGVDVVAVLAYNDAYVMSAWGKANQVTNDDILFLSDPEAKFSKSIGWADEEGRTGRYAIIIDHGKVTYAKREPAKNHLEFSSAETVLKHL
Protein: FAST kinase domain-containing protein 3, mitochondrial (Q14CZ7)
Organism: Homo sapiens (Human)
Function: Required for normal mitochondrial respiration. Increases steady-state levels and half-lives of a subset of mature mitochondrial mRNAs MT-ND2, MT-ND3, MT-CYTB, MT-CO2, and MT-ATP8/6. Promotes MT-CO1 mRNA translation and increases mitochondrial complex IV assembly and activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:27789713}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 1
- ATP-dependent RNA helicase DHX30
- Small ribosomal subunit protein mS31
- Isoleucine--tRNA ligase, mitochondrial
- Small ribosomal subunit protein mS22
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Leucine-rich PPR motif-containing protein, mitochondrial
- 5-taurinomethyluridine-[tRNA] synthase subunit MTO1, mitochondrial
- FAST kinase domain-containing protein 2
- Elongation factor G, mitochondrial
Sequence:
MALITLRKNLYRLSDFQMHRALAALKNKPLNHVHKVVKERLCPWLCSRQPEPFGVKFHHAHCKKFHSKNGNDLHPLGGPVFSQVSDCDRLEQNVKNEESQMFYRRLSNLTSSEEVLSFISTMETLPDTMAAGALQRICEVEKKDGDQGLPKEILENSIFQALCFQFEKEPSQLSNTSLVTALQALILLHVDPQSSLLLNLVAECQNRLRKGGMEVRNLCILGESLITLHSSGCVTLELIINQLQGEKLETFTPEDIVALYRILQACTEKVDEHQTFLNKINNFSLSIVSNLSPKLISQMLTALVVLDQSQAFPLIIKLGKYVVRHVPHFTNEELRRVLEAFIYFGHHDTFFTKALEHRVAAVCLTLDPEVVCRVMEYCSRELILSKPILNAVAETFVCQTEKFSPRQISALMEPFGKLNYLPPNASALFRKLENVLFTHFNYFPPKSLLKLLHSCSLNECHPVNFLAKIFKPLFLQRLQGKESHLDTLSRAQLTQLFLASVLECPFYKGPKLLPKYQVKSFLTPCCSLETPVDSQLYRYVKIGLTNLLGARLYFAPKVLTPYCYTIDVEIKLDEEGFVLPSTANEDIHKRIALCIDGPKRFCSNSKHLLGKEAIKQRHLQLLGYQVVQIPYHEIGMLKSRRELVEYLQRKLFSQNTVHWLQE
Protein: Thylakoid soluble phosphoprotein (Q9SD66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Wax ester synthase/diacylglycerol acyltransferase 4
- Aspartate carbamoyltransferase, chloroplastic
Sequence:
MVSSLLMSFAPATVRVYATSTKGGSGGPKEEKNPIDFVLGFMTKQDQFYETNPLLKKVDEKEGTTTGGRGTVRGGKNSAPTPVPKKSEGGFGGLGSLFKK
Protein: Ubiquitin-related modifier 1 (P40554)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Adenylyltransferase and sulfurtransferase UBA4
- Cytoplasmic tRNA 2-thiolation protein 1
- Peroxiredoxin AHP1
- Cytoplasmic tRNA 2-thiolation protein 2
- Thiosulfate sulfurtransferase TUM1
- Elongator complex protein 3
- Elongator complex protein 6
- Elongator complex protein 1
- Cysteine desulfurase, mitochondrial
- Elongator complex protein 4
Sequence:
MVNVKVEFLGGLDAIFGKQRVHKIKMDKEDPVTVGDLIDHIVSTMINNPNDVSIFIEDDSIRPGIITLINDTDWELEGEKDYILEDGDIISFTSTLHGG