wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear RNA export factor 2 (Q99MW6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MWSSPKENLQGRSSMFVQKNINSETYKQRYGLPYKRSERFYHSEYKMNYNHGFQGRKRGVNYIWSQFDRKNNHFDHYGAPYAMGMKRRRERCSYDDQYFLNVWDDSKTEEGETDLDAENETEEKWYKVTIPSGRKYEKTWLMRSIQNFCSEPFIPVDFHYDKTQARFFVQNAKTASALKDVSYRICDETSRKIAIFVSPSVVPYSVQNKFTSEQMEYIRESMMNRYDASQKALDLEKFRFDQDLMDKDIDMMLNRRSCMVATLQIIQSDIPELLSLNLTNNKLYQLDGLSDMTEKAPHVKILNLSRNKLKSFTELEKVKELKLEELWLEGNPFCNCFLDHFEYISTIHDLFPKLLRLDGEDIIVPKRNLQNGKGLIVPTRNLQNGKDLIVPTGNPQDGKDLIVPTGNPQDGKDLIVPTGNPQDGKDLIVPTKMDIEVPQPCKESCNTSEVIKNLVLQFLKEYYLFYDNGDRLRLLDAYHDQACFSLSVPFDVSDPNLNNLEEYFKYSRDLKRQQDSSMRMQLLKHTKHDIVNSLSLLPKTQHDLCSFLVDLFLHTEMMLCFSVNGLFMEVEGKCRGCIRAFTRIFIAIPCSDSRICIMNDELIVRNASPKEIQKAFTSLPAPDTSFKPLLSEEQQEMVKSFSVQSGMKLDWSQKCLQDNEWDYTKAGEAFTALQNEGKIPKEFFK
Protein: Protein MEH1 (EGO complex subunit 1) (GSE complex subunit 2) (Q02205)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Component of the EGO complex, a complex involved in the regulation of microautophagy.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15989961}.
Interaction partners:
- GTP-binding protein GTR1
- Protein EGO2
- Protein SLM4
- GTP-binding protein GTR2
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Cystine transporter
- Protein LTV1
- Protein ERD1
- Glutamine sensor PIB2
- Translation initiation factor eIF2B subunit beta
Sequence:
MGAVLSCCRNHSGEENEALLREQQAGYGSQGNANDEYDAEQMRLKEHEHEQKLLAREQELRDIVANTNDKLIDISMINNSGIVIQGTDLQEALDKRQQEEGGDSREDERSAGDDNLSGHSVPSSGSAQATTHQTAPRTNTFTLLTSPDSAKISKEQLKKLHSNILNEIFSQSQVNKPGPLTVPF
Protein: Neurofibromin 1, isoform C (Q8IMS2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTQKPGEWASALLARFEDQLPNRIGAYGTQARMSQDQLVACLIHISRYRFSLVISGLTKMLQRVNEAALQNRHEPERCYFESLVIILTTLERCLTNQTKDTARFEEAMNVKLLLREISQFVDVQSDSNPNAAQLKALASKVLFALSQNHFSAVFNRISARIQELTSCSEENPDYNDIELIQHIDMDMIKLTKLLQETITKFRSKRAPPLILLYSLEKAIWNWIEYHPQEFQDLQRGTNRDISTCWEPLMDFVEYFKTENKKSKTLVWPLQMLLLILNPSCLEAVVNELQQSEKEKEKDKEKVASKSAQSTSRDKDFSAKQFIESIKRGLGQHSPSKQVTESAAIACVKLCKASTYINNTDSNNVVFKLVQFFINDLKALLFNPAKPFSRGQGYNFADIELMIDCWVSCFRINPHNIEALKVCLNLSSPQAYHFVIVCSLLRLAHIYVDFRLQNKNPFRIVNQPRLSWWPQTDVVHYRSAELRALFTDTLNKATQGYIAHTPLRYITSLTLKSKDTQKGLTRAEEGPAHKMLLLLLVRLIHADPTLLLNTQGKVAHEVQSSTLELINGLVSLVHQTTMPDVAQEAMEALLALHAPEKIEVWNPEAPINTFWDVSSQVLFSISQKLIQHQIANYTDVLKWLREILICRNTFLQRHKDYAHVGSQIAICKQAHIKMEVVFFMYLWSVDLDAVLTSLSCFGLLCEEAEICCSSDELTVGFIMPNYHIYQELAQLSTSATDSRICFFDNTHGNVLSRLTLQKRIMTLLRKIEHCVHGVQPAWEETFRNWEVSSKVLQTYPKCKGEDGQAEVFHRGMGKRRASHQSSEHDLEEQINEWANMTWFLLALGGVCLHKRSSSRQMLLQQSQNNASLGSLAQNSLYSSSTSSGHGSLHPSTVSLSTLPPAPPQDVSYCPVTQFVGQLLRLLVCSNEKIGLNIQKNVKELVGEEMSTQLYPILFDQVRAIVEKFFDQQGQVNVNVTDINTQFIEHTIYIMKSILDPKANKDPNNDQPSPSEHLGVTSIEGMMLGIVRYVRHLDMTVYAIRIKTKLCQLVEVMMKRRDDLAFRQEMKFRNKLVEYLTDWVMGTSHQIAPPSSADAAILTNTSLIFRDLDQACMEAVAALLRGLPLQPEESDRGDLMDAKSALFLKYFTLFMNLLNDCIDSSEAEKEMNNTPLLPPRPRMAAGKLTALRNATILAMSNLLGANIDSGLMHSIDLGYNPDLQTRAAFMEVLTQILQQGTEFDTLAETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSKEQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHSMSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPFDKMATLLAYLGPPEHKPVDSHMMFSSYARWSSIDMSSTNFEEIMVKHQMHEKEEFKTLKSMNIFYQAGTSKSGYPVFYYIARRYKIGETNGDLLIYHVILTLKPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAVYIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQQKLPGATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNESGQLSFIHNDCDNIVQAIIHIRNRWELSQPDSVTVHQKIRPKDVPGTLLNMALLNLGSCDPNLRTAAYNLLCALTATFDLKIEGQLLETQGLCIPSNNTIFIKSVSEKLATNEPHLTLEFLEESIQGFQRSTIELKHLCLEYMTPWLKNLVKFCKSNDDSKKLKVSQILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALASANVQLVSKKVITRICRVMDKSCTNPTQYLEQHMMWDDIAILGRYLLMLSFNNCLDVATSVPYLFHTITFLVCSGSLSMRASTHGLVINIIHSLCTCTNPSFSEEAQRVLRLSLDEFSLPKFYLLFGISKVKSAAVTAFRSSCRHPTDKWLGNERVTQPLPADRERLSLPSLEVITDALLEIMEACMRDVPDCEWLNTWTSLARSFAFCYNPALQPRALIVYGCISKSVTDHEVKQLLRILVKALESFNDLILIEALVMCLTRIQPLLRPESPIHRALFWVAISVLQLDEITLYGAGLALLEQNLHTLKSQGCFDKKETIAEVMMKTREKLEWHFKQLDHAVGLSFRSNFHFALVGHLIKGFRHPTPTTVSRTSRVLTMLLGIIAKPLHRDKFEVTPDSVAYLTALVAVSEEVRSRCHVKHALPRWPADLSSSVENGEASGGVQAIGLPLSRRQKSWDILDQSALQFARQHKVPTLQERGSRSSVSNESNVLLDPEVLPDLSIQALVLTVLATLVKYSSDEGETRVLYQYLAEGSVVFPKVFPVIHSLLDQKINNILSVSHDQVVLNSVQNIIQNMLASEDPSQQQLHFLQSCGFGGLWRFAGPFTKYNMMGESSELFVNCLEAMVETCLPGDESAPVPPSPRPYNLSSSLSSLTLGSPTDKECPEAMTTECERRK
Protein: UPF0297 protein SP_0192 (Q97SX1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MGFTEETVRFKLDDSNKKEISETLTDVYASLNDKGYNPINQIVGYVLSGDPAYVPRYNNARNQIRKYERDEIVEELVRYYLKGQGVDL
Protein: Heme oxygenase (EC 1.14.14.18) (Q96DI8)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00037869}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037869}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037869}.
Interaction partners:
Sequence:
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQHYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Protein: Protein Vpr (R ORF protein) (Viral protein R) (P12520)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Function: During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. {ECO:0000255|HAMAP-Rule:MF_04080}.
Interaction partners:
Sequence:
MEQAPEDQGPQREPYNEWTLELLEELKSEAVRHFPRIWLHNLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTRQRRARNGASRS
Protein: Serine/threonine-protein kinase ppk6 (EC 2.7.11.1) (Q9UTH3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSQDVFKHLTSKQVQRTRARSFGASFERPLASFLPKKENKNLLSNAARVKLLTFSSSSPYSFSYSPVLSRDANDGYIPLDTSSRANLWESVTDYDLQHANEPLVGNYYISTEALGDGLNRSPFTINPEKRRSLSDISYVPIPHKEHSNWPVHCSSQAIVTTSNTTFSIWSANDYFCLLFGYAGSQLNRHSVFDIFPKSFSSHLSNLIVSFPIDNEHERILFCGDVFPVITVDGVRLMDFWVKEKQGKLIWILEFVEESYIDIKLQDGVAVDERTEQPLTSDLLPSRLPKTWDQRLYLTTKTTEGYYCPSMIYPLSKSSFQYIIFHYAAGLLFINSDFKIISLNEALFESMLGYSDLLTKDISLIFPDFKLVLQQLADSHALDPGRVVSEIHVRHAYRTCTADKMKKADYPYLIHSDGNIIQIDCQIISVSPHSVKSNEPAFGVWLIFDSVDNRASDFVRSMRSSVILEEVVISDESEEEEDLSADEDYVDSEWEVVPHNIASYTTIKELGIGAYGQVKLATYKSNKVHEVILKSISKSRILLDSWMRDKDLGTVPMEISILHFLKAHSHPNIVKMITFFEDNENYYLLTEPQKPGIDLFDYIELKPSISEKESKAIFFQIALAVAHLHSFDIIHRDIKDENVILEGNGCARLIDFGSSSLTKNGPFDTFRGTVGFAAPELLRGEKYLGKEQDIWALGILLYTIVYRENPYYNIEEILDAKLRIPFELSKDNVDLICRMLDRNVHDRITIEETLQHHWFDDIRYLDTSHIRIPLSS
Protein: PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) (Q9NRD5)
Organism: Homo sapiens (Human)
Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.
Subcellular location: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
Interaction partners:
- Glutamate receptor 2
- Protein kinase C alpha type
- Glutamate receptor 3
- Glutamate receptor-interacting protein 1
- Tetraspanin-7
- Disks large homolog 4
- Islet cell autoantigen 1
- Glutamate receptor 1
- Glutamate receptor-interacting protein 2
- Metabotropic glutamate receptor 7
Sequence:
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPSRDTRGAAGPLDKGGSWCDS
Protein: Phenylalanine ammonia-lyase (EC 4.3.1.24) (F4JW69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU003955}.
Interaction partners:
Sequence:
MEFRQPNATALSDPLNWNVAAEALKGSHLEEVKKMVKDYRKGTVQLGGETLTIGQVAAVASGGPTVELSEEARGGVKASSDWVMESMNRDTDTYGITTGFGSSSRRRTDQGAALQKELIRYLNAGIFATGNEDDDRSNTLPRPATRAAMLIRVNTLLQGYSGIRFEILEAITTLLNCKITPLLPLRGTITASGDLVPLSYIAGFLIGRPNSRSVGPSGEILTALEAFKLAGVSSFFELRPKEGLALVNGTAVGSALASTVLYDANILVVFSEVASAMFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYVKEALHLHKIDPLQKPKQDRYVLGYALRTSPQWLGPQIEVIRAATKMIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVAMDNTRLALASIGKLMFAQFTELVNDFYNNGLPSNLSGGRNPSLDYGLKGAEVAMASYCSELQFLANPVTNHVESASQHNQDVNSLGLISSRTTAEAVVILKLMSTTYLVALCQAFDLRHLEEILKKAVNEVVSHTAKSVLAIEPFRKHDDILGVVNREYVFSYVDDPSSLTNPLMQKLRHVLFDKALAEPEGETDTVFRKIGAFEAELKFLLPKEVERVRTEYENGTFNVANRIKKCRSYPLYRFVRNELETRLLTGEDVRSPGEDFDKVFRAISQGKLIDPLFECLKEWNGAPISIC
Protein: Histone acetyltransferase KAT6B (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4) (MYST-4) (Protein querkopf) (Q8BRB7)
Organism: Mus musculus (Mouse)
Function: Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (By similarity). Involved in cerebral cortex development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Peregrin
- Histone acetyltransferase KAT6A
- Inhibitor of growth protein 5
- Chromatin modification-related protein MEAF6
- Bromodomain-containing 1.
- Bromodomain and PHD finger-containing protein 3
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Histone acetyltransferase KAT7
Sequence:
MVKLANPLYTEWILEAVQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKPTKGSKGPPCNDLRNVDWNKLLKRAIEGLEEPNGSSLKNIEKYLRSQSDLTGTTNHPAFQQRLRLGAKRAVNNGRLLKEGPQYRVNSGSSDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTANVKALRWQCIECKTCSACRVQGKNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMSAFTGRGSPGRGQKTKVSTTPSSGHAASGKHSSSRLAVTDPTRPGATTKTTTSSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATDTDIKISIKQESADVSLVGNKELVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYRHHERHISIKAISRATGMCPHDIATTLQHLHMIDRRDGRFVIIRREKLILGHMEKLKNCSRPNELDPESLRWTPMLISNAVVSEEEREAEKEAERLMEQASCWEKEEQEILSSRVSSRQSSAKVQSKNKYLHSPERRPVAGERGQLLELSKESSEEEEEEEEEDDEEEEEEEEEESIQTSPPRLTKPQSVSIKRKRPFVVKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIPVEEGGRKPVLRKAFPHQPGKKRQTEEEEGEDNHFFKTAALCRKDVDDDAEHLKEGSKDNPEPLKCRQVWPKGAKRGLSKWKQSKERKTGFKLNLYTPPETPMEPEDQVTIEEQKELSEDKGSPVGMEREVTETVDALLPQEGSRREETGIPVSPHKSPGGKVDEEDLIRGEEEGEEEGEEEGEREEQEEEEEVTTEKDLDGAKSKENPEPEISMEKEDPVHLGDHEEDEDEEEEPSHNEDHDADDEDDGHMEAANMERGDLPRETFKDALEGQEAFLDLSIQPSHSNPEVLMNCGVDLTMSCNSEPKELAGDTGTAPESDAEPPEEQTQKQDQKNSDGVDAELEEGGPAAVEIDSETAQAVQSLTQENREHDDTFPDCAETQEACRSLQNYTHTDQSPQIATTLDECQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQTAITVPPLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSSLTSSNLTQNSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLADIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHVSMRTKAASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGSQPYAQQPMQTPPHANMMYTAPGHHGYMNTGMSKQSLNGSYMRR
Protein: Elongation of very long chain fatty acids protein 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL2) (ELOVL fatty acid elongase 2) (ELOVL FA elongase 2) (Very long chain 3-ketoacyl-CoA synthase 2) (Very long chain 3-oxoacyl-CoA synthase 2) (B6V6V1)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03202}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Elongation of very long chain fatty acids protein 5
- Elongation of very long chain fatty acids protein 5
- Delta-5 fatty acyl desaturase isoform X1
- Delta-6 fatty acyl desaturase
- Estradiol 17-beta-dehydrogenase 12-B
- 3-ketoacyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase-like isoform X1
- Delta-6 fatty acyl desaturase
Sequence:
MNHLQSLDERLNKLFYFLFEDRDSRVRGWLLLDSYLPTLSLTILYLLSVYLGSKYMRNRPAYSLKGVLQVYNFSVTMLSLYMLVELVSATLSAGYRLQCQGLHEAGEADLRVAKVLWWYYFSKVIEFLDTIFFVLRKKNSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHVCMYSYYGLSTIPSMQKYLWWKRYLTQAQLIQFILTITHTLSAIVVPCGFPVGCLLFQFSYMATLVILFVNFYVQTYRKRRPEESIKSSRPNGHSVSTNGTSFKKRK
Protein: Uncharacterized protein (A0A178UN96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTNVRLPILVSSVLFLVFISSSLLFPTPSFAARVSHSLVQEEVKKVPEYTEPEEPEVPEEPELPSPEEPEIPEEPEIPEEPEVPGEPEVPEEPEEPEEPEGSTFEFPSWFPSFPIPGVNGGLPKTEKTKPTSTVEEVNVSNKKP
Protein: RNA-binding protein fusilli (Q9BJZ5)
Organism: Drosophila melanogaster (Fruit fly)
Function: mRNA splicing factor that regulates alternative splicing od specific genes. Has a maternal role in embryonic dorsal-ventral patterning; such role is probably indirect and due to its function as mRNA splicing factor regulator.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- TAR DNA-binding protein 43
Sequence:
MQVPEHVVSLYIATCGQNGSGLGSDEKEIILLVFVLLEVSTGQIVGTKQILVRPDGYFIKDRTISSSSDNSSVTNNTASSPPLAIGDANNGSGSTSGNGNSLENGSELILPIAEAQAAGKPLSEAIEEFDAYLRSLSLHDTEIKLVTDGQLPLRQCLHREASAKDVELPAYYNRFSDLRKEFLRYKSGDLARALVPVKDVKKMLQAPTLPMPQSIAEMLGELNISSVEDNDFYIRESRDMVTVIQTLLQAGHKFAANELVNLVLEPGICSIDDEVDGNCIVRARGLPWQSSDQDIAKFFRGLNVAKGGVALCLSPLGRRNGEALIRFVCQEHRDMALKRHKHHIGTRYIEVYRASGEDFLAIAGGASNEAQAFLSKGAQVIIRMRGLPYDATAKQVLDFFTTGDTPPCHVLDGNEGVLFVKKPDGRATGDAFVLFANETDAPKALGRHRESIGQRYIELFRSTTAEVQQVLNRSMDPKNYESGGGHSQPPLIAQLPTMQLPLLPQVGAHSLSHSLGASPANLCPPVPPPALPLPTQHLITSGTTKNCIRLRGLPYEAMVEHILHFLDDFAKHIIYQGVHMVINAQGQPSGEAFIQMDLEESARLCAQRRHNHYMMFGKKYRYIEVFQCSGDDMNMVLNGGLASPVAQPPPPHLGHAHKQQSLLAATTGMFSSAGQSPTTVAAGTAQSPLGGTHTHTHPHSHAHAHATGHAHAAAAAAHHGLSASSAMLPGLSAAASASGLASFMSAGQQSAAAAAHSAASLQNAAVALAPQGYALNPFSLPPPGSAAAAAASTPALLAQQQAQFIAQQSLLVRQQAAAAALAAEQQQQQQQQQQLYASAMLQQHPLYLQQQQQQQQLYASAMLQQGQPQFVLMQRPSAAYLPPFPLSYMSAAGAASGVGVAPGAAVAGAAAAASPSASNSSLSQSMKRSYENAFQQEAAGAAAAASAAKRALTRQPSSVYSYYNSGI
Protein: Large ribosomal subunit protein mL54 (39S ribosomal protein L54, mitochondrial) (L54mt) (MRP-L54) (Q6P161)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL10m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL41
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL34m
- Small ribosomal subunit protein mS25
Sequence:
MATKRLFGATRTWAGWGAWELLNPATSGRLLARDYAKKPVMKGAKSGKGAVTSEALKDPDVCTDPVQLTTYAMGVNIYKEGQDVPLKPDAEYPEWLFEMNLGPPKTLEELDPESREYWRRLRKQNIWRHNRLSKNKRL
Protein: Large ribosomal subunit protein bL28m (54S ribosomal protein L24, mitochondrial) (YmL14/YmL24) (P36525)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL15m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL32m
Sequence:
MQKIFRPFQLTRGFTSSVKNFRQWRLIETRKIAKQPNYQVGDAKPLHMPKERKKFPDYKYGESNIFKQSNKGLYGGSFVQFGNNISESKAKTRKKWLPNVVKKGLWSETLNRKISIKMTAKVLKTISKEGGIDNYLTKEKSARIKELGPTGWKLRYRVLKRKDEIENPPHKDAPIIEMAGGKKAKIYYDEIVNGSPRKISVGRRRLMSFLYPLEKLEYRSVGKDLNYKKFVELFADVPVKDILARLEDHKFDLSTITV
Protein: EH domain-containing protein 1a (EH-domain-containing 1a) (Zgc:77049) (Q6NY81)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Endosome membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125}.
Interaction partners:
- Rabenosyn, RAB effector.
- Rab11 family-interacting protein 2
- RAB11 family-interacting protein 1
- RAB11 family-interacting protein 1
- EH domain-containing protein 1b
- RAB11 family-interacting protein 5a
- Rab11 family-interacting protein 5-like
- Ras-related protein Rab-15
Sequence:
MFSWSNRDGKKDPELFQNVSDGLKRLYRTKLFPLEDTYHFHDFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRHLMEQDFPGMRIGPEPTTDSFIAVMHGEQEGVIPGNALVVDPKKPFRKLNAFGNAFLNRFMCAQLNNPVLESISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKMRVVLNKADQISTQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWAQPLLIAENRKLFEAEEQDLFQDIQSLPRNAALRKLNDLIKRARLAKVHAYIISALKKEMPSVFGKDSKKKELINNLGAIYEKIQKEHNISPGDFPNLKKMQELLSVQDFTKFPAMKPKLLESVEDMLGNDIAKLMALVRKEEATMPSQSVKGGAFEGISNGPFGHGYGEGAGEGIDELEWIVGRDKPSYDEIFYTLSPINGKISGATAKKEMTKSKLPNTVLGKIWTLADVDKDGYLDDEEFALANHLIKVKLEGFELPAKLPNHLVPPSKRQEHN
Protein: Protein SMAX1-LIKE 7 (AtSMXL7) (Protein D53-like 1) (AtD53-like 1) (Protein D53-like SMXL 7) (O80875)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of a transcriptional corepressor complex involved in branching control. Regulates cotyledon expansion and lateral root growth, but not germination or hypocotyl elongation. Promotes auxin transport and PIN1 accumulation in the stem and represses BRC1/TCP18 expression in axillary buds.
Subcellular location: Nucleus {ECO:0000269|PubMed:26546446}.
Interaction partners:
- Strigolactone esterase D14
- Probable esterase KAI2
- F-box protein MAX2
- Topless-related protein 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Carotenoid cleavage dioxygenase 8, chloroplastic
- Squamosa promoter-binding-like protein 15
- Cytochrome P450 711A1
- Carotenoid cleavage dioxygenase 7, chloroplastic
- ATP-dependent Clp protease adapter protein CLPS1
Sequence:
MPTPVTTARQCLTEETARALDDAVSVARRRSHAQTTSLHAVSGLLTMPSSILREVCISRAAHNTPYSSRLQFRALELCVGVSLDRLPSSKSTPTTTVEEDPPVSNSLMAAIKRSQATQRRHPETYHLHQIHGNNNTETTSVLKVELKYFILSILDDPIVSRVFGEAGFRSTDIKLDVLHPPVTSQFSSRFTSRSRIPPLFLCNLPESDSGRVRFGFPFGDLDENCRRIGEVLARKDKKNPLLVGVCGVEALKTFTDSINRGKFGFLPLEISGLSVVSIKISEVLVDGSRIDIKFDDLGRLKSGMVLNLGELKVLASDVFSVDVIEKFVLKLADLLKLHREKLWFIGSVSSNETYLKLIERFPTIDKDWNLHLLPITSSSQGLYPKSSLMGSFVPFGGFFSSTSDFRIPSSSSMNQTLPRCHLCNEKYEQEVTAFAKSGSMIDDQCSEKLPSWLRNVEHEHEKGNLGKVKDDPNVLASRIPALQKKWDDICQRIHQTPAFPKLSFQPVRPQFPLQLGSSSQTKMSLGSPTEKIVCTRTSESFQGMVALPQNPPHQPGLSVKISKPKHTEDLSSSTTNSPLSFVTTDLGLGTIYASKNQEPSTPVSVERRDFEVIKEKQLLSASRYCKDFKSLRELLSRKVGFQNEAVNAISEIVCGYRDESRRRNNHVATTSNVWLALLGPDKAGKKKVALALAEVFCGGQDNFICVDFKSQDSLDDRFRGKTVVDYIAGEVARRADSVVFIENVEKAEFPDQIRLSEAMRTGKLRDSHGREISMKNVIVVATISGSDKASDCHVLEEPVKYSEERVLNAKNWTLQIKLADTSNVNKNGPNKRRQEEAETEVTELRALKSQRSFLDLNLPVDEIEANEDEAYTMSENTEAWLEDFVEQVDGKVTFKLIDFDELAKNIKRNILSLFHLSFGPETHLEIENDVILKILAALRWSSDEEKTFDQWLQTVLAPSFAKARQKCVPAAPFSVKLVASRESPAEEETTGIQQFPARVEVI
Protein: Subtilisin-like protease SBT3 (EC 3.4.21.-) (LeSBT3) (SlSBT3) (Subtilase 3) (O82777)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Serine protease. Has preference for Gln in the P1 position and Lys in the P2 position of oligopeptide substrates. Active also with His in the P1 position. Involved in resistance against insects partly by regulating expression of systemic wound response genes and possibly by its post-ingestive activity in the insect gut. Apart from the role in defense, may be involved in regulation of pectin methylesterases (PMEs) activity and pectin methylesterification of the cell wall.
Subcellular location: Secreted {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}. Note=Autocatalytic cleavage is required for the secretion of the mature protein. {ECO:0000269|PubMed:19332543}.
Interaction partners:
- CTLH domain-containing protein
Sequence:
MELLHLLLFSWALSAHLFLALAQRSTYIVHLDKSLMPNVFTDHHHWHSSTIDSIKASVPSSVDRFHSAPKLVYSYDNVLHGFSAVLSKDELAALKKLPGFISAYKDRTVEPHTTHTSDFLKLNPSSGLWPASGLGQDVIVAVLDSGIWPESASFQDDGMPEIPKRWKGICKPGTQFNASMCNRKLIGANYFNKGILANDPTVNITMNSARDTDGHGTHCASITAGNFAKGVSHFGYAPGTARGVAPRARLAVYKFSFNEGTFTSDLIAAMDQAVADGVDMISISYGYRFIPLYEDAISIASFGAMMKGVLVSASAGNRGPGIGSLNNGSPWILCVASGHTDRTFAGTLTLGNGLKIRGWSLFPARAFVRDSPVIYNKTLSDCSSEELLSQVENPENTIVICDDNGDFSDQMRIITRARLKAAIFISEDPGVFRSATFPNPGVVVNKKEGKQVINYVKNSVTPTATITFQETYLDTKPAPVVAASSARGPSRSYLGISKPDILAPGVLILAAYPPNVFATSIGTNILLSTDYILESGTSMAAPHAAGIAAMLKAAHPEWSPSAIRSAMMTTADPLDNTRKPIKDSDNNKAATPLDMGAGHVDPNRALDPGLVYDATPQDYVNLLCSLNFTEEQFKTIARSSASHNCSNPSADLNYPSFIALYSIEGNFTLLEQKFKRTVTNVGKGAATYKAKLKAPKNSTISVSPQILVFKNKNEKQSYTLTIRYIGDEGQSRNVGSITWVEQNGNHSVRSPIVTSPIIEVW