wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase AIP2 (EC 2.3.2.27) (ABI3-interacting protein 2) (RING-type E3 ubiquitin transferase AIP2) (Q8RXD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of abscisic acid (ABA) signaling. Mediates ubiquitination and subsequent proteasomal degradation of the transcription factor ABI3.
Subcellular location: Nucleus {ECO:0000269|PubMed:15998807}. Cytoplasm {ECO:0000269|PubMed:15998807}.
Interaction partners:
- B3 domain-containing transcription factor ABI3
- E3 ubiquitin-protein ligase KEG
- Transducin/WD40 repeat-like superfamily protein
- Homeobox-leucine zipper protein ATHB-6
- WD repeat-containing protein DWA2
- THO complex subunit 6
- Protein ABSCISIC ACID-INSENSITIVE 5
- Cullin-4
- E3 ubiquitin-protein ligase RHA2B
- DET1- and DDB1-associated protein 1
Sequence:
MDASSSPSPSEESLKLELDDLQKQLNKKLRFEASVCSIHNLLRDHYSSSSPSLRKQFYIVVSRVATVLKTRYTATGFWVAGLSLFEEAERLVSDASEKKHLKSCVAQAKEQLSEVDNQPTESSQGYLFEGHLTVDREPPQPQWLVQQNLMSAFASIVGGESSNGPTENTIGETANLMQELINGLDMIIPDILDDGGPPRAPPASKEVVEKLPVIIFTEELLKKFGAEAECCICKENLVIGDKMQELPCKHTFHPPCLKPWLDEHNSCPICRHELPTDDQKYENWKEREKEAEEERKGAENAVRGGEYMYV
Protein: Smtnl protein (Q5BL23)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDAGPLASVAEGSPEGETVCAALARYETTLRDAVREIHVDVSAFKLGIERRLEEAIHVSGPLGRAVAQLQQENRQLRGQLEALTRQVEMLTGSVCDRSALLTGGSQSSNSTGHQSPPSAAPSVAALTGSASGSASSPTTTRFSSRATFSVTSKTNSIERDEPIEVDPAPISQGLENGHLSSTENSIVPLRRNSPPNGVLHENSAPVPMAMPHLPITATTKVADSTVMKSPESPSSPMQATPSAITDSLTNSPPVTSDNQPQLESPVHAVSSVKTWAPTPARTMGSPRLTEKASSAPAKSVTYSGLFPHNTDRNVDTPGDLSFGRGIERRRELVRSQTLPRNIGAQARRSIFERLDSENNSRPKPVDSKPKLKRSQSFGVSSASSIKQILLEWCRSKTIGYQNIDIQNFSSSWSDGMAFCALVHSFFPTEFDYNGLSPAERKHNFELAFSTAEKKAGCDRLIEVEDMMVMGRKPDPMCVFTYVQSLYNHLRKFE
Protein: ATP synthase subunit alpha (EC 7.1.2.2) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) (P9WPU7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
Interaction partners:
- ATP synthase subunit b-delta
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase epsilon chain
- ATP synthase subunit b
- ATP synthase subunit beta
- ATP synthase gamma chain
- Uncharacterized protein Rv1507c
- Multifunctional 2-oxoglutarate metabolism enzyme
- Inorganic pyrophosphatase
Sequence:
MAELTIPADDIQSAIEEYVSSFTADTSREEVGTVVDAGDGIAHVEGLPSVMTQELLEFPGGILGVALNLDEHSVGAVILGDFENIEEGQQVKRTGEVLSVPVGDGFLGRVVNPLGQPIDGRGDVDSDTRRALELQAPSVVHRQGVKEPLQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVCVDTILNQRQNWESGDPKKQVRCVYVAIGQKGTTIAAVRRTLEEGGAMDYTTIVAAAASESAGFKWLAPYTGSAIAQHWMYEGKHVLIIFDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDDLGGGSLTGLPIIETKANDISAYIPTNVISITDGQCFLETDLFNQGVRPAINVGVSVSRVGGAAQIKAMKEVAGSLRLDLSQYRELEAFAAFASDLDAASKAQLERGARLVELLKQPQSQPMPVEEQVVSIFLGTGGHLDSVPVEDVRRFETELLDHMRASEEEILTEIRDSQKLTEEAADKLTEVIKNFKKGFAATGGGSVVPDEHVEALDEDKLAKEAVKVKKPAPKKKK
Protein: Cys-Gly metallodipeptidase DUG1 (EC 3.4.13.-) (Deficient in utilization of glutathione protein 1) (GSH degradosomal complex subunit DUG1) (P43616)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17179087}. Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Probable glutamine amidotransferase DUG3
- Glutathione hydrolase proenzyme
- Glutathione synthetase GSH2
- Glutamate--cysteine ligase
- Glutathione-specific gamma-glutamylcyclotransferase
- Protein ARG5,6
- Serine hydroxymethyltransferase, cytosolic
- Homocysteine/cysteine synthase
- Serine hydroxymethyltransferase, mitochondrial
- Putative mitochondrial cysteine synthase
Sequence:
MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSESPEN
Protein: Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)] (P61810)
Organism: Rattus norvegicus (Rat)
Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution.
Subcellular location: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}.; SUBCELLULAR LOCATION: [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
Interaction partners:
- Cyclin-dependent kinase 5
- Microtubule-associated protein tau
- Calpain-1 catalytic subunit
- Calpain-2 catalytic subunit
- Cellular tumor antigen p53
Sequence:
MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
Protein: Protein inhibitor of activated STAT, 1 (G3V9T0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
- Signal transducer and activator of transcription 1
- Small ubiquitin-related modifier 1
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription 3
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 3
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 2
- Androgen receptor
Sequence:
LVDTQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRSLLQHKFSTTPTNIDRFPFLKLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQECFVSAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD
Protein: Uncharacterized protein (Q385J6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMNRNENSGCKALWSNTRLEWCYWCHLIRSSKCSFALFFAVLCVLAIIVGNTILLLGVNFWLDLMVKESTEGFTPIAVQVIVCLFLVLCFGVLIIVYIAVYGIKPLVRALCDTNRAGSPLYRMLLIFSSGATNGLSSALAIYAMTYTPEFMQAVLLSVIPFFAQIWTYALVREERDRCYSSMTLIGSLVLCIAGVLLASLSSFFTTDMSTKKAPWGWAFVYFLSCIVFGLWCVVQRLYFDAIMIKGTKPQEGEREPHQPLSHQHPEITNSGRYEGRGGQRLPAEAAAAGVDGVTQSNEVEEVASSENAENPMLNREWAKQDENDLAAKALVLFLGIIFQAMVSFAFVPIDAIPGFGNSKDMKESWKNFSATFDFVFASWFNLRFGLLHTLGFLMSFIGCAYLNERSPPLASVVLQLAGPITSLVLIIIPEWDVFGEHGILSHKASGVIFLIIAGWAYHVWEVAYPNAYKSATTTAAVMRGTGNV
Protein: Copper transport protein ATOX1 (Metal transport protein ATX1) (M9PD88)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- P-type Cu
- Superoxide dismutase
- NADH dehydrogenase 13 kDa B subunit
- Copper transport protein
- Copper transport protein
- Cytochrome c oxidase assembly protein COX11
- Superoxide dismutase
- AT19154p
- Mitochondrial ribosomal protein S11
- LD10456p
Sequence:
MTVHEFKVEMTCGGCASAVERVLGKLGDKVEKVNINLEDRTVSVTSNLSSDELMEQLRKTGKSTTYVGVKKXDEFLSKFQKYGRLKLEV
Protein: Transcriptional activator/repressor GIS1 (Q03833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor involved in the regulation of gene expression upon nutrient starvation. Recognizes and binds to the post-diauxic-shift element 5'-T[AT]AGGGAT-3' in the promoter region. Can act as a transcriptional activator (e.g. of stress genes like SSA3, HSP12 and HSP26) as well as a repressor (e.g. of pyrophosphate phosphatase DPP1). GIS1 also acts as a DNA damage-responsive transcriptional repressor of photolyase PHR1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein kinase SCH9
- Ras-like protein 2
- Zinc finger protein MSN2
- Serine/threonine-protein kinase RIM15
- Zinc finger protein MSN4
- JmjC domain-containing histone demethylation protein 1
- Protein ECM5
- Histone H3
- DNA damage-responsive transcriptional repressor RPH1
- Serine/threonine-protein kinase TOR1
Sequence:
MEIKPVEVIDGVPVFKPSMMEFANFQYFIDEITKFGIENGIVKVIPPKEWLELLEGSPPAESLKTIQLDSPIQQQAKRWDKHENGVFSIENEYDNKSYNLTQWKNLAESLDSRISQGDFNDKTLKENCRVDSQQDCYDLAQLQILESDFWKTIAFSKPFYAVDENSSIFPYDLTLWNLNNLPDSINSSNRRLLTGQSKCIFPWHLDEQNKCSINYLHFGAPKQWYSIPSANTDQFLKILSKEPSSNKENCPAFIRHQNIITSPDFLRKNNIKFNRVVQFQHEFIITFPYCMYSGFNYGYNFGESIEFILDQQAVVRKQPLKCGCGNKKEERKSGPFSNLSYDSNESEQRGSITDNDNDLFQKVRSFDELLNHSSQELQNLEDNKNPLFSNINMNRPQSSSLRSTTPNGVNQFLNMNQTTISRISSPLLSRMMDLSNIVEPTLDDPGSKFKRKVLTPQLPQMNIPSNSSNFGTPSLTNTNSLLSNITATSTNPSTTTNGSQNHNNVNANGINTSAAASINNNISSTNNSANNSSSNNNVSTVPSSMMHSSTLNGTSGLGGDNDDNMLALSLATLANSATASPRLTLPPLSSPMNPNGHTSYNGNMMNNNSGNGSNGSNSYSNGVTTAAATTTSAPHNLSIVSPNPTYSPNPLSLYLTNSKNPLNSGLAPLSPSTSNIPFLKRNNVVTLNISREASKSPISSFVNDYRSPLGVSNPLMYSSTINDYSNGTGIRQNSNNINPLDAGPSFSPLHKKPKILNGNDNSNLDSNNFDYSFTGNKQESNPSILNNNTNNNDNYRTSSMNNNGNNYQAHSSKFGENEVIMSDHGKIYICRECNRQFSSGHHLTRHKKSVHSGEKPHSCPRCGKRFKRRDHVLQHLNKKIPCTQEMENTKLAES
Protein: Serine/threonine-protein kinase hippo (EC 2.7.11.1) (Drosophila homolog of MST1 and MST2) (STE20-like kinase MST) (dMST) (Q8T0S6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Phosphorylates Sav, Wts and Th/DIAP1. Regulates the level of Th/DIAP1 apoptosis inhibitor.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:26954546}. Cytoplasm {ECO:0000269|PubMed:26954546}.
Interaction partners:
- Scaffold protein salvador
- Transcriptional coactivator yorkie
- MOB kinase activator-like 1
- LD40758p
- Serine/threonine-protein kinase Warts
- Protein expanded
- Death-associated inhibitor of apoptosis 1
- Protein kibra
- P53, isoform B
- MOB kinase activator-like 2
Sequence:
MSEPEVTSVVDMKSPNISSSCSFFKLKKLSEESLLQPPEKVFDIMYKLGEGSYGSVYKAVHKESSSIVAIKLVPVESDLHEIIKEISIMQQCDSPYVVRYYGSYFKQYDLWICMEYCGAGSVSDIMRLRKKTLTEDEIATILSDTLQGLVYLHLRRKIHRDIKAANILLNTEGYAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIEEIGYDCVADIWSLGITALEMAEGKPPYGEIHPMRAIFMIPQKPPPSFREPDRWSTEFIDFVSKCLVKEPDDRATATELLEHEFIRNAKHRSILKPMLEETCAIREQQRANRSFGGVLAASQAKSLATQENGMQQHITDNAFMEDPGTLVPEKFGEYQQSSASDATMIAHAEQGVDEGTLGPGGLRNLSKAAAPAAASSAASPLDMPAVDSGTMVELESNLGTMVINSDSDDSTTAKNNDDQKPRNRYRPQFLEHFDRKNAGDGRGDEKPIATEYSPAAAEQQQQQQQQQQQQQQDEQHLASGANDLNNWEHNMEMQFQQISAINQYGLQQHQQQQQVLMAYPLMNEQLIALNNQPNLLLSNAAPMGQQGIPAAAPAQPPPAYQNQHMHTQSHAYVEGEFEFLKFLTFDDLNQRLCNIDHEMELEIEQLNKKYNAKRQPIVDAMNAKRKRQQNINNNLIKI
Protein: Shewanella-like protein phosphatase 2 (EC 3.1.3.16) (Q8I5Y5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein phosphatase inhibitor 3
Sequence:
MNISYLRNFSCIYFLIIIWKFSYVYNESYSNIKWEHDLFSISDLHSDLDALKKTLLTENIIDEENNAIRENVFVIITGDVLDPAYDDIEILYFIQNYNIKAKPLNSKIQLILGNHEVQNICLDFIGNKKYGEEYKARNKLFKKGEVLYNYLLDLPFVIKVNDILFSHASILPYYAKRGIDYINDEGRSEIKNNCTLLKFKRKTGQRFCVCCYNGPTFNRYFSRAAEMPFRREVCKSLFKTLNKLSAKKLVNGHTIQRNRKVNEYCKGGLIMADTGISKWKYGVINYVQYFQDGSYKVNYINSDI
Protein: Phosphoenolpyruvate carboxylase (PEPC) (PEPCase) (EC 4.1.1.31) (Q97WG4)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Interaction partners:
- Malate dehydrogenase
- Phosphoenolpyruvate synthase
- Phosphoenolpyruvate carboxykinase
- Pyruvate kinase
- Enolase
- Citrate synthase
- Formate dehydrogenase Alpha subunit
- Cyclase family protein
- Formate dehydrogenase Alpha subunit
- ATPase
Sequence:
MRIIPRTMSTQHPDNAKVPEWAKSEVIEGEDEVKEAFLAYSMYGVHEVMWDAEGKDVDTHVVRKLLSNYPDYFREHILGKDLFLTYRLPNPKVEGADRKVFAETMESIPITYDLAEKFYGNGITIPVFEVILPMTTSSLEIISVARYYEKAVANEDELELYDGVKVKDLVGEIYPKVIEVIPLVEDRDSLQNINNIVEGYYKVIKPKYMRVFLARSDPAMNYGMITAVLSVKIALSELYKLSESLNFEIYPIIGVGSLPFRGHLSPENYEKVLEEYKGVYTYTIQSAFKYDYDYDKVKSAISSINNSRISPARILEKYEEDVLRKITILYTERYQPIIESLANAINDVSVLLPRRRARKLHIGLFGYSRSAGKVSLPRAISFVGSLYSIGIPPELIGISSLSNLDEKEWDIFKQNYVNFKHDLQTAARFLNWESFKLIKDIWKISEDTIAKIKEDIDYAESVIGIKLGGIDYDSRKHILMSSLFLLSFKEKILQESKKYLYEMALIRRSLG
Protein: 50S ribosomal protein L16, putative (Q57UM6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C2H2-type domain-containing protein
- Uncharacterized protein
- Ribosomal protein L11, putative
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- AB hydrolase-1 domain-containing protein
- Ribosomal protein L22p/L17e
Sequence:
MPSPFQQTLLARAYHYVHPKTGRPIRQFRRYGDPRYINNEAALIRGQWGLITADFGMVTQSQMENARLAILRRLPRGSFTLTMHTDYEEFPVVKKSPESRMGAGKANIHHFAFKFTTGVPLFEIMPISARRLNQAEAEGIFLAGRPFIPLQTVVVPQGRVDEYHVFK
Protein: Meiosis-specific protein ASY2 (Protein ASYNAPTIC 2) (F4JTJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal meiosis.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:F4HRV8}. Nucleus {ECO:0000250|UniProtKB:F4HRV8}.
Interaction partners:
- DNA mismatch repair protein MSH4
- RNA binding / RNA-directed DNA polymerase
- DNA polymerase zeta processivity subunit
- Meiosis-specific protein ASY3
- Crossover junction endonuclease MUS81
- Structural maintenance of chromosomes protein 4
- Meiotic recombination protein SPO11-2
- Meiotic recombination protein SPO11-1
- Putative recombination initiation defects 3
- Separase
Sequence:
MVVVSKNNEQQSLILTTELLRTAIFNISYIRGLFPVRYFKDMSVPALDLKMKKLMPMDAESRRLIGWMEKGVYDALHKKHLKKLIFYICETVDGPLIEEYIFSFSYSDSDSQDVRMNINITGINTYGGTLNSTADNSTADMTLNQMSSVDEDFGQNARRSNAFVTYQRFSVYISFHIANYRLCYFFASVQRTILMKLLYYEYVPPDYQPPFFRGCSEEEEAQYVWPKIPLRMEIGNVNSQHHVLTVKVKSVLDPYDPCEDENDNMQDDERSKGPDSLHDDQPCKVFTKPSKLILTENKDADHGEVNEEKLLLITPICEILQDVKQDQVEHQLAKVKDTKGRPASIVQNPILQSHEYDIRRLKARLQRLERHISVPDSPQEGIRKWFAAVSSQLFYKVMEACTRRKPILGDAILSSTVKVQNFNAKICSKLLKKPASIYRKKHFTLNSASLRISGLAGSIFAWAVGFCLFSAQIGHVFVQPKTRSSESKPKVTMEELEEKLTPPSSEPKSAPPSSEPKSAPPSSEPLEKLAVIRRILPEIFAQRCGQRNSSFEAFAQRRTTYDYYNIRLNPREIIFRRLQEESKVALALSSANYFVLSILYRFFRQWSEVSLVRRNSRLTGNPSNEAQSSRSNRIEIPTLLDEPDREGSGGHLAAPEDPVDFLAQFDPLIDLEDAYNTQPQYTEAEVNARLLHEDHVEFDLVPVVSWNTEITAKKTLSTTESVAEVFALCGSGDRPLTCMIPGENERPWNPPRGYVCMYEAYFRQCHLWFPIPSLIISFLNRRHMAFSQLTPAAICNFVAALTFGAEEGYLVNVRCFEEMTTLKAIRSPGYWVVNNRPKHNFLPGPKVSNFKNWEEYYFYVRVDLESYERPFSGRKRMWTEFPDRYRPSPDFPVEFEGVLEAIFRARRRTWKDVTRSRVNRIMGKVRKSFISFAAGLLNMPPPPAPIEEERQPLDGEAAASNPPVSAGPSGVDQVSHEMVNPESQDRMCLEGADVVPAQEIAECDRSQSVQVVEPEVQNITDDRSVVVYAAPPAGEEVNTGLTILDQDKDETVAEPGISRRSREEKGKGGANQSKKRSASEAGLDEAAAPKTFRLSRGETLNSDQFTFKYSGEKFLVRDQEAASHLWRNLMLPGTKDFPNPDDLVLKEGYQKFARSSLETAALANDLIATYDRKLKLKLADREAFDNLKKCADQAKAIYAKDMKEMASLRDAAEIHKAEMSSLNDEVKRLNSREADLQKEFSDLQVALVAVKEHGERECNRLRNDRAAKVARTTKKAQARLDRVKAYLKEQEDLVGPKVDAENQARGAEEIVGILMQRGAKIAASELSGLKELTKRATDEVNALNVIELGDDDLNMSPDQLGFSRQISQVAPVADQHGSNVDLLAEVIRRVSVEETNQTT
Protein: Indole glucosinolate O-methyltransferase 3 (EC 2.1.1.-) (Q9LPU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in indole glucosinolate biosynthesis. Catalyzes methoxylation reactions of the glucosinolate indole ring. Converts the hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate(1MO-I3M), respectively.
Interaction partners:
- Protein trichome birefringence-like 19
Sequence:
MGYLFEETLSSNPKTPIVVDDDNELGLMAVRLANAAAFPMVLKASLELGVFDTLYAEASRTDSFLSPSEIASKLPTTPRNPGAPVLLDRMLRLLASYSMVKCEKVSVGKEQRVYRAEPICRFFLKNNIQDIGSLASQVIVNFDSVFLNTWAQLKDVVLEGGDAFGRAHGGMKLFDYMGTDERFSKLFNQTGFTIAVVKKALEVYQGFKGVNVLVDVGGGVGNTLGVVTSKYPNIKGINFDLTCALAQAPTYPGVEHVAGDMFVDVPTGNAMILKRILHDWTDEDCVKILKNCWKSLPQNGKVVVIELVTPDEAENGDINANIAFDMDMLMFTQCSGGKERSRAEFEALAAASGFSHCQFVCQAYHCWIIEFCK
Protein: Vitellogenin (O93605)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MRAVVLALTLALVASQSVNFAPDFAASKTYVYKYEALLLGGLPEEGLARAGVKVISKVLISAVAENTYLLKLVNPEIFEYSGVWPKDPFVPAAKLTSALAAQFSIPIKFEYAKGVVGKVFAPTAVSETVLNVHRGILNILQLNIKKTQNVYELQEAGAQGVCKTHYVIREDAKAERIHLTKSKDLNNCQQRIMKDFGLAYTEKCVECRQRGEALMGAATYNYLMKPVDNGALILEATVTELHQFTPFNEMSGAAQMEAKQMLTFVEIKKDPIIVPDNNYVHRGSIRYEFATEILQMPIQLLKISNARAQ
Protein: IP20609p (Lectin-30A) (Lectin30A) (Q6GV06)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Accessory gland-specific peptide 26Aa
- ACP53C14B
- Serpin 28F
- ACP53C14A
- Sulfhydryl oxidase
- Accessory gland protein Acp53Ea
- GH11711p
- Accessory gland protein Acp76A
- Accessory gland-specific peptide 26Ab
- Serpin 38F, isoform A
Sequence:
MFKYCFICVILAWASRDVLANKTENPLLIDQVAINQQQWFTFIALKESEMQQKIVRIERSIEERLMAMQSKLAYALNELQTIMGNQSVETLEKLRISHRINPALFQRMGTRRFYIEKENKQNWFGASNTCRQLGGHIATIRDEQEFNEIFSRAPAGVFWIDMNAMFKNGLFASSLTGRSPPFFKWKKEERGNKFDCVNVYNKEMYNENCFNTHLFICQAEQWD
Protein: Oleate delta-12 desaturase (C8VTX5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Acyl-CoA desaturase
- Acyl-CoA desaturase
- Bifunctional oelate/linoleic acid delta desaturase
- Elongation of fatty acids protein
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase
- very-long-chain enoyl-CoA reductase
- Elongation of fatty acids protein
Sequence:
MSSTALPKRVALHRNPTTDSSVPSSVSVSPLDSPRQSPSSTSLSSMASDAGKGDLGKMLDTYGNEFKIPDYTIKDIRDAIPSHCYNRSAIRSLSYVFRDLAVLASVFYVFHKYVTPETVPSYPARVALWTLYTVVQGLFGTGIWVLAHECGHQAFSTSKVLNDTVGWILHSALLVPYFSWKISHGKHHKATGNLARDMVFVPKTREVYASRIKKTIYDLNEVMEETPLATATHSILQQLFGWPLYLLTNVTGHDNHERQPEGRGKGKRNGYFTGVNHFNPNSPLFEAKDAKLIILSDIGLAITASILYLIGSKFGWMNLLVWYGIPYLWVNHWLVAITYLQHTDPTLPHYQPESWTFARGAAATIDREFGFIGRHILHGIIETHVLHHYVSTIPFYHADEASEAIKKVMGSHYRSEAHTGPLGFLKALWTSARVCHWVEPTEGTKGENAGVLFFRNTNGIGVPPIKLTKPN
Protein: Plastidal glycolate/glycerate translocator 1, chloroplastic (Bacterial membrane protein LrgB-like protein) (AtLrgB) (Q9FVQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycolate/glycerate transporter required for photorespiration.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305|PubMed:12766230, ECO:0000305|PubMed:23382251}; Multi-pass membrane protein {ECO:0000305|PubMed:12766230, ECO:0000305|PubMed:23382251}.
Interaction partners:
- Probable sodium/metabolite cotransporter BASS6, chloroplastic
- Phosphoglycolate phosphatase 1A, chloroplastic
- Glycerate dehydrogenase HPR, peroxisomal
- Dicarboxylate transporter 1, chloroplastic
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Malate synthase
- Dicarboxylate transporter 2.1, chloroplastic
- Uncharacterized protein At5g13720)
- Mitochondrial carnitine/acylcarnitine carrier-like protein
- Protein CLT2, chloroplastic
Sequence:
MATLLATPIFSPLASSPARNRLSCSKIRFGSKNGKILNSDGAQKLNLSKFRKPDGQRFLQMGSSKEMNFERKLSVQAMDGAGTGNTSTISRNVIAISHLLVSLGIILAADYFLKQAFVAASIKFPSALFGMFCIFSVLMIFDSVVPAAANGLMNFFEPAFLFIQRWLPLFYVPSLVVLPLSVRDIPAASGVKICYIVAGGWLASLCVAGYTAIAVRKMVKTEMTEAEPMAKPSPFSTLELWSWSGIFVVSFVGALFYPNSLGTSARTSLPFLLSSTVLGYIVGSGLPSSIKKVFHPIICCALSAVLAALAFGYASGSGLDPVLGNYLTKVASDPGAGDILMGFLGSVILSFAFSMFKQRKLVKRHAAEIFTSVIVSTVFSLYSTALVGRLVGLEPSLTVSILPRCITVALALSIVSLFEGTNSSLTAAVVVVTGLIGANFVQVVLDKLRLRDPIARGIATASSAHGLGTAALSAKEPEALPFCAIAYALTGIFGSLLCSVPAVRQSLLAVVG
Protein: Threonylcarbamoyl-AMP synthase (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (Q8I610)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- riboflavin kinase
- N
- tRNA N6-adenosine threonylcarbamoyltransferase
- tRNA N6-adenosine threonylcarbamoyltransferase
Sequence:
MALIIKGNEIFENEDLRKKLKEHIEGDKLIGIPTETVYGLGGNSLSQRSLQNIFRMKNRPVSDPIISHVYNIYQAYDQLYHINIYEKYIIYILSKYFWPGPLSIIAKAKKEAPLILTAYTQFCAVRIPDNKITREIIKICNTPIAAPSANKFQHISPTNSLHVYDEFKNEDLLIFDDGQCDVGIESTVLKITKYRINHEDKNTDEVLKEKDVNVMKDIKKINNINVNNSEGNNPVEIVNDEEYECECNEELAFLRAATNSKESESNMEVYEKLKNMFDLIERMNSINNDDDNNNNDDNNNNDNNNNNNIIVDKILKYKSLYNYSIKIYRRGKYTKGDIENVLKKYDLLKDINVEMYEKIKFENLDIFKNEYPKSGIKDYRCDNINKEDDIYKTFNNEIEKNEVCPGLLLTHYSPFVSTYLLDIISCKTIEKENKGELLETNNNVCKKINLNKCVLLDIGSSLLKYDKNFLKYINICYDSLEVNERIKYITKQFFLFLRQAERLAIENKADNILISIVNIKSCDENYLSIFDRIYRAASGKMINLFIEHKDIIAYIK
Protein: Vacuolar amino acid transporter 3 (P36062)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11274162}; Multi-pass membrane protein {ECO:0000269|PubMed:11274162}.
Interaction partners:
- Autophagy-related protein 22
- Vacuolar amino acid transporter 4
- Vacuolar amino acid transporter 6
- Vacuolar amino acid transporter 7
Sequence:
MNGKEVSSGSGRTQSNNNKKNNNGGSTGISHASGSPLTDGNGGNSNGNSRSRSRSRKSSGTTGGLLKKPPLLVNNEAVHASVPDASHTSCNNGTLEVSINNPEPHVVDAVARHLIRNPSNSLQLQGGDITRDLYKWTNDHPSSPSQYQYPSQPALSTSIPSQAPSFSNRKRSMSFSAASIASSSHLNNNSEANGNPLAAIGLAPAPMTHEEIRAPGGFRRSFIIQKRRKHNVDAPIPNFFTRNFIEFLTLYGHFAGEDLSEEEEEEEETEEEPEEEALETESTQLVSREHGRHPHKSSTVKAVLLLLKSFVGTGVLFLPKAFHNGGWGFSALCLLSCALISYGCFVSLITTKDKVGVDGYGDMGRILYGPKMKFAILSSIALSQIGFSAAYTVFTATNLQVFSENFFHLKPGSISLATYIFAQVLIFVPLSLTRNIAKLSGTALIADLFILLGLVYVYVYSIYYIAVNGVASDTMLMFNKADWSLFIGTAIFTFEGIGLLIPIQESMKHPKHFRPSLSAVMCIVAVIFISCGLLCYAAFGSDVKTVVLLNFPQDTSYTLTVQLLYALAILLSTPLQLFPAIRILENWTFPSNASGKYNPKVKWLKNYFRCAIVVLTSILAWVGANDLDKFVSLVGSFACIPLIYIYPPLLHYKASILSGTSRARLLLDLIVIVFGVAVMAYTSWQTIKMWSQ