wanglab/gogpt-training-data huggingface dataset:
Protein: Limbic system-associated membrane protein (LSAMP) (IgLON family member 3) (Q13449)
Organism: Homo sapiens (Human)
Function: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hippocampal mossy fiber projection (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MVRRVQPDRKQLPLVLLRLLCLLPTGLPVRSVDFNRGTDNITVRQGDTAILRCVVEDKNSKVAWLNRSGIIFAGHDKWSLDPRVELEKRHSLEYSLRIQKVDVYDEGSYTCSVQTQHEPKTSQVYLIVQVPPKISNISSDVTVNEGSNVTLVCMANGRPEPVITWRHLTPTGREFEGEEEYLEILGITREQSGKYECKAANEVSSADVKQVKVTVNYPPTITESKSNEATTGRQASLKCEASAVPAPDFEWYRDDTRINSANGLEIKSTEGQSSLTVTNVTEEHYGNYTCVAANKLGVTNASLVLFRPGSVRGINGSISLAVPLWLLAASLLCLLSKC
Protein: Arginine kinase (EC 2.7.3.3) (Q38EU9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Arginase, putative
- Arginine kinase
- Arginine kinase
Sequence:
MATRDVAAELEKAFAKLQAAKDCHSLLKKYLTSDVFKKLKDKKTKLGATLLDVIQSGVQNLDSGVGLYAPDAEAYTVFADLFDPVIEDYHNGFKVTDKQPPKDFGDLNTLVDVDPEGKYVISTRVRCGRSLAGYPFNPCLTKEQYEEMESRVREQLSTMTDDLQGTYYPLSGMTKETQQQLIDDHFLFKEGDRFLQAARACEYWPTGRGIYHNNDKTFLVWVNEEDHLRIISMQKGGNLKEVFGRLVKAVNTIEKKVEFSRDDRLGFLTFCPSNLGTTIRASVHIKLPKLGADRAKLEEVAAKYNLQVRGTAGEHSDSPDGIYDISNKRRLGLSEYEAVKEMQDGILELIKLEKSK
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (P61107)
Organism: Rattus norvegicus (Rat)
Function: Regulates, together with its guanine nucleotide exchange factor, DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion (By similarity). Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes.
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:P61106}. Early endosome membrane {ECO:0000269|PubMed:15004230}; Lipid-anchor {ECO:0000305|PubMed:15004230}; Cytoplasmic side {ECO:0000305|PubMed:15004230}. Golgi apparatus membrane {ECO:0000269|PubMed:15004230}; Lipid-anchor {ECO:0000305|PubMed:15004230}; Cytoplasmic side {ECO:0000305|PubMed:15004230}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15004230}; Lipid-anchor {ECO:0000305|PubMed:15004230}; Cytoplasmic side {ECO:0000305|PubMed:15004230}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes by DENND6A. {ECO:0000250|UniProtKB:P61106}.
Interaction partners:
- TBC1 domain family member 1
- Solute carrier family 2, facilitated glucose transporter member 4
- Rab GDP dissociation inhibitor alpha
Sequence:
MATTPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSLDLNAAESGVQHKPSAPQGGRLTSEPQPQREGCGC
Protein: Inner kinetochore subunit IML3 (CENP-L homolog) (Constitutive centromere-associated network protein IML3) (Increased minichromosome loss protein 3) (Minichromosome maintenance protein 19) (P38265)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit NKP1
- Inner kinetochore subunit NKP2
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit CTF19
- Inner kinetochore subunit AME1
Sequence:
MPYTWKFLGISKQLSLENGIAKLNQLLNLEVDLDIQTIRVPSDPDGGTAADEYIRYEMRLDISNLDEGTYSKFIFLGNSKMEVPMFLCYCGTDNRNEVVLQWLKAEYGVIMWPIKFEQKTMIKLADASIVHVTKENIEQITWFSSKLYFEPETQDKNLRQFSIEIPRESCEGLALGYGNTMHPYNDAIVPYIYNETGMAVERLPLTSVILAGHTKIMRESIVTSTRSLRNRVLAVVLQSIQFTSE
Protein: Glutamine synthetase, type I (EC 6.3.1.2) (Q725N2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Carbamoyl phosphate synthase large chain
- Glutamine--fructose-6-phosphate aminotransferase
- glutamate synthase
- L-glutamate gamma-semialdehyde dehydrogenase
- Glutamate synthase, small subunit
- Carbamoyl phosphate synthase small chain
- Glutamine synthetase, type III
- Amidophosphoribosyltransferase
- Pyridine nucleotide-disulfide oxidoreductase
- Glutamyl-Q tRNA
Sequence:
MDIPVFNCKNGDDVIRAVKEYNVSFVQFWFVDILGNLKSFQVTPSELEAAFEEGMGFDGSSILGFTRIEESDMVAFPDATTFQICSWRPLERPVARMFCDIRTPDGTPYEGDPRYILRKLIDKAAQKGYTFYVGPELEFFFFSSPQCPTPIDAGGYFDAPPLDLGNDVRRDIIFALQRMGIPVEYSHHEVAPSQHEIDLRYNEAMKMADVVMTYKVVVKEMARKHGIYATFMPKPIFGENGSGMHVHQSLFRNGKNAFFDPNDQHNLSHECRSYIAGLLKHAREFCCVTNQWINSYKRLVPGYEAPVYIAWAQRNRSALIRVPMYKPGKEAATRIELRSPDPACNPYLAFAVMLGAGLEGIENNYELPKAVEANIFHMGEEDLGKHGIGSLPGSLYEAAMELRNSNLMKEILGEHTHANIVGNKLIEWDDYRTHISEFELKRYLPIL
Protein: DNA gyrase subunit A (EC 5.6.2.2) (P0AES4)
Organism: Escherichia coli (strain K12)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase IV (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than many other bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical. The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
Interaction partners:
- DNA topoisomerase 4 subunit B
- DNA gyrase subunit B
- DNA-directed RNA polymerase subunit beta
- DNA gyrase inhibitor YacG
- Small ribosomal subunit protein uS12
- Protein RecA
- Chaperone protein DnaK
- Ribosomal RNA small subunit methyltransferase G
- Beta-lactamase
- Multiple antibiotic resistance protein MarR
Sequence:
MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE
Protein: Serine/threonine-protein phosphatase 6 regulatory subunit 3 (SAPS domain family member 3) (Sporulation-induced transcript 4-associated protein SAPL) (Q5H9R7)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
- Serine/threonine-protein phosphatase 6 regulatory subunit 1
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B
- Splicing factor 3B subunit 1
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- NF-kappa-B inhibitor epsilon
Sequence:
MFWKFDLHSSSHIDTLLEREDVTLKELMDEEDVLQECKAQNRKLIEFLLKAECLEDLVSFIIEEPPQDMDEKIRYKYPNISCELLTSDVSQMNDRLGEDESLLMKLYSFLLNDSPLNPLLASFFSKVLSILISRKPEQIVDFLKKKHDFVDLIIKHIGTSAIMDLLLRLLTCIEPPQPRQDVLNWLNEEKIIQRLVEIVHPSQEEDRHSNASQSLCEIVRLSRDQMLQIQNSTEPDPLLATLEKQEIIEQLLSNIFHKEKNESAIVSAIQILLTLLETRRPTFEGHIEICPPGMSHSACSVNKSVLEAIRGRLGSFHELLLEPPKKSVMKTTWGVLDPPVGNTRLNVIRLISSLLQTNTSSINGDLMELNSIGVILNMFFKYTWNNFLHTQVEICIALILASPFENTENATITDQDSTGDNLLLKHLFQKCQLIERILEAWEMNEKKQAEGGRRHGYMGHLTRIANCIVHSTDKGPNSALVQQLIKDLPDEVRERWETFCTSSLGETNKRNTVDLVTTCHIHSSSDDEIDFKETGFSQDSSLQQAFSDYQMQQMTSNFIDQFGFNDEKFADQDDIGNVSFDRVSDINFTLNTNESGNIALFEACCKERIQQFDDGGSDEEDIWEEKHIAFTPESQRRSSSGSTDSEESTDSEEEDGAKQDLFEPSSANTEDKMEVDLSEPPNWSANFDVPMETTHGAPLDSVGSDVWSTEEPMPTKETGWASFSEFTSSLSTKDSLRSNSPVEMETSTEPMDPLTPSAAALAVQPEAAGSVAMEASSDGEEDAESTDKVTETVMNGGMKETLSLTVDAKTETAVFKSEEGKLSTSQDAACKDAEECPETAEAKCAAPRPPSSSPEQRTGQPSAPGDTSVNGPV
Protein: Non-structural protein 1 (NS1) (NS1A) (P03495)
Organism: Influenza A virus (strain A/Udorn/307/1972 H3N2)
Function: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Note=In uninfected, transfected cells, NS1 is localized in the nucleus. Only in virus infected cells, the nuclear export signal is unveiled, presumably by a viral protein, and a fraction of NS1 is exported in the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04066}.
Interaction partners:
Sequence:
MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD
Protein: Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP) (P24369)
Organism: Mus musculus (Mouse)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P23284}. Melanosome {ECO:0000250|UniProtKB:P23284}.
Interaction partners:
- Prolyl 3-hydroxylase 1
- Cartilage-associated protein
- Protein disulfide-isomerase A4
- Endoplasmin
- Protein disulfide-isomerase
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum chaperone BiP
- DnaJ homolog subfamily B member 11
- Stromal cell-derived factor 2-like protein 1
- Protein disulfide-isomerase A6
Sequence:
MLRLSERNMKVLFAAALIVGSVVFLLLPGPSVANDKKKGPKVTVKVYFDLQIGDESVGRVVFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTSWLDGKHVVFGKVLEGMDVVRKVESTKTDSRDKPLKDVIIVDSGKIEVEKPFAIAKE
Protein: WD repeat-containing protein 25 (Q64LD2)
Organism: Homo sapiens (Human)
Interaction partners:
- Crooked neck-like protein 1
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SYF1
- SNW domain-containing protein 1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-splicing factor SYF2
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing-splicing factor 8
- Splicing factor YJU2
Sequence:
MTARTLSLMASLVAYDDSDSEAETEHAGSFNATGQQKDTSGVARPPGQDFASGTLDVPKAGAQPTKHGSCEDPGGYRLPLAQLGRSDWGSCPSQRLQWPGKEPQVTFPIKEPSCSSLWTSHVPASHMPLAAARFKQVKLSRNFPKSSFHAQSESETVGKNGSSFQKKKCEDCVVPYTPRRLRQRQALSTETGKGKDVEPQGPPAGRAPAPLYVGPGVSEFIQPYLNSHYKETTVPRKVLFHLRGHRGPVNTIQWCPVLSKSHMLLSTSMDKTFKVWNAVDSGHCLQTYSLHTEAVRAARWAPCGRRILSGGFDFALHLTDLETGTQLFSGRSDFRITTLKFHPKDHNIFLCGGFSSEMKAWDIRTGKVMRSYKATIQQTLDILFLREGSEFLSSTDASTRDSADRTIIAWDFRTSAKISNQIFHERFTCPSLALHPREPVFLAQTNGNYLALFSTVWPYRMSRRRRYEGHKVEGYSVGCECSPGGDLLVTGSADGRVLMYSFRTASRACTLQGHTQACVGTTYHPVLPSVLATCSWGGDMKIWH
Protein: Ferredoxin-like protein FixX (P68646)
Organism: Escherichia coli (strain K12)
Function: Could be part of an electron transfer system required for anaerobic carnitine reduction. Could be a 3Fe-4S cluster-containing protein.
Interaction partners:
- Protein FixC
- Protein FixB
- Protein FixA
- Oxamate carbamoyltransferase subunit AllH
- Uncharacterized lipoprotein GfcD
- Probable electron transfer flavoprotein-quinone oxidoreductase YdiS
- Putative metabolite transport protein YaaU
- Probable electron transfer flavoprotein-quinone oxidoreductase YgcN
- Putative electron transfer flavoprotein subunit YdiQ
- Putative electron transfer flavoprotein subunit YdiR
Sequence:
MTSPVNVDVKLGVNKFNVDEEHPHIVVKADADKQALELLVKACPAGLYKKQDDGSVRFDYAGCLECGTCRILGLGSALEQWEYPRGTFGVEFRYG
Protein: Histone-lysine N-methyltransferase eggless (EC 2.1.1.355) (SETDB1 homolog) (Q32KD2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting Su(var)205/HP1 to methylated histones. Plays a central role during oogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17164421}. Chromosome {ECO:0000305|PubMed:17164421}.
Interaction partners:
- BcDNA.LD26050
- Uncharacterized protein, isoform C
- Histone H3
- Heterochromatin protein 1
- Histone H3.3A
- Protein panoramix
- Calmodulin-lysine N-methyltransferase
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase
- Protein piwi
- Suppressor of variegation 2-10, isoform I
Sequence:
MSGQPTAVDCLESSGSTVEDVQETPASREKSYGLPVRKGENSLESPAEQAAKDVEIEELTHSEAIAATGSTRKQCPYGGKAPDEPGKLADESEDRKGENTKAIASSPVLVAVDSDSSVELIESPVKFSSANESEKDPPKPDAVNEAAAKEAEEMTDSSISSPTSESFPEKDEKTNKENEQEPPGMEVDQDVEESISRPAEEYKIENTLKGHKRISLTEIEEHKIVDKKDDVLEVELEKGTAPKAAEDEKLNALLSDGDVFYDKECVNCNCTKLHKQYVLANMATLNFYQVLRKSSKQQFLCMGCHDTAMDLYEEYAGQLMAKQPLLLKDFHQDHADFVALDSSDEEEEEKQPEKSDFSKNKLQLIEDELDDAIKNVLNKVDFTAQLSWSKTILQAKADHLERQFALADVELEKVQTTADKMHCALYNSCPVAHKHLPTLDIEPSDYVHEVPPPGEIVRPPIQLGETYYAVKNKAIASWVSIKVIEFTESTAINGNTMKSYKIRYLNTPYQMIKTVTAKHIAYFEPPPVRLTIGTRVIAYFDGTTLSRGKDKGVVQSAFYPGIIAEPLKQANRYRYLIFYDDGYTQYVPHRDVRLVCQASEKVWEDVHAASRDFIQKYVEKYSVDRPMVQCTRGQSMTTESNGTWLYARVIDIDCSLVLMQFEGDKNHTEWIYRGSLRLGPVFRETQNNMNSSSAQQLRVPRRTEPFIRYTKEMESSSKVNQQMRAFARKSSASAQNNALAAASSAATPAGGRTNAGGVSTSNSASAVRHLNNSTIYVDDENRPKGHVVYFTAKRNLPPKMYKCHECSPNCLFKIVHRLDSYSPLAKPLLSGWERLVMRQKTKKSVVYKGPCGKSLRSLAEVHRYLRATENVLNVDNFDFTPDLKCLAEYSIDPSIVKDTDISKGQEKMAIPLVNYYDNTLPPPCTYAKQRIPTEGVHLNLDEEFLLCCDCEDDCSDKSKCACWQLTVAGVRYCNPKKPIEEIGYQYKRLHEHVPTGIYECNSRCKCKKNCLNRVVQFSLEMKLQVFKTSNRGWGLRCVNDIPKGAFICIYAGHLLTETMANEGGQDAGDEYFADLDYIEVAEQLKEGYESEVDHSDPDAEEDNGGPDAEDDDDFRPNYHYQRKIKRSSRSGSTQNSSTQSSELDSQERAVINFNPNADLDETVRENSVRRLFGKDEAPYIMDAKTTGNLGRYFNHSCSPNLFVQNVFVDTHDLRFPWVAFFSAAHIRSGTELTWNYNYEVGVVPGKVLYCQCGAPNCRLRLL
Protein: Immune system released activating agent (B2CXA1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAGETVLQGCPLCPDHAEGDRSPRIGGSQRQSPLLEVTHTQCCHLILSCLYVWCPVTQSLYGAPEQHSFLSPLVLLHASQRPGTHPLAISLLTLPSQLVPEYTEVTSLQVIRILVNPSESANCLG
Protein: Ent-copalyl diphosphate synthase, chloroplastic (AtCPS) (Ent-CDP synthase) (EC 5.5.1.13) (Ent-kaurene synthase A) (KSA) (Protein GA REQUIRING 1) (Q38802)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Ent-kaurene oxidase, chloroplastic
- Ent-kaur-16-ene synthase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- 
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
- Gibberellin 3-beta-dioxygenase 1
- Solanesyl diphosphate synthase 2, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- Geranylgeranyl pyrophosphate synthase 11, chloroplastic
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2
Sequence:
MSLQYHVLNSIPSTTFLSSTKTTISSSFLTISGSPLNVARDKSRSGSIHCSKLRTQEYINSQEVQHDLPLIHEWQQLQGEDAPQISVGSNSNAFKEAVKSVKTILRNLTDGEITISAYDTAWVALIDAGDKTPAFPSAVKWIAENQLSDGSWGDAYLFSYHDRLINTLACVVALRSWNLFPHQCNKGITFFRENIGKLEDENDEHMPIGFEVAFPSLLEIARGINIDVPYDSPVLKDIYAKKELKLTRIPKEIMHKIPTTLLHSLEGMRDLDWEKLLKLQSQDGSFLFSPSSTAFAFMQTRDSNCLEYLRNAVKRFNGGVPNVFPVDLFEHIWIVDRLQRLGISRYFEEEIKECLDYVHRYWTDNGICWARCSHVQDIDDTAMAFRLLRQHGYQVSADVFKNFEKEGEFFCFVGQSNQAVTGMFNLYRASQLAFPREEILKNAKEFSYNYLLEKREREELIDKWIIMKDLPGEIGFALEIPWYASLPRVETRFYIDQYGGENDVWIGKTLYRMPYVNNNGYLELAKQDYNNCQAQHQLEWDIFQKWYEENRLSEWGVRRSELLECYYLAAATIFESERSHERMVWAKSSVLVKAISSSFGESSDSRRSFSDQFHEYIANARRSDHHFNDRNMRLDRPGSVQASRLAGVLIGTLNQMSFDLFMSHGRDVNNLLYLSWGDWMEKWKLYGDEGEGELMVKMIILMKNNDLTNFFTHTHFVRLAEIINRICLPRQYLKARRNDEKEKTIKSMEKEMGKMVELALSESDTFRDVSITFLDVAKAFYYFALCGDHLQTHISKVLFQKV
Protein: E3 ubiquitin-protein ligase RHA1B (EC 2.3.2.27) (RING-H2 finger A1b) (RING-H2 zinc finger protein RHA1b) (RING-type E3 ubiquitin transferase RHA1B) (Q9SUS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro.
Interaction partners:
- E3 ubiquitin-protein ligase RMA2
Sequence:
MGLPTDFKELQIPGYVLKTLYVIGFFRDMVDALCPYIGLPSFLDHNETSRSDPTRLALSTSATLANELIPVVRFSDLLTDPEDCCTVCLSDFVSDDKIRQLPKCGHVFHHRCLDRWIVDCNKITCPICRNRFLPEEKSTPFDWGTSDWFRDEVESTN
Protein: Cilia- and flagella-associated protein 418 (Q3UJP5)
Organism: Mus musculus (Mouse)
Function: May be involved in photoreceptor outer segment disk morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22177090, ECO:0000269|PubMed:29440555}. Photoreceptor inner segment {ECO:0000269|PubMed:29440555}. Note=In the retina, located at the base of the primary cilium (PubMed:22177090). Expressed throughout photoreceptors cell body including the basal body, inner segment and synaptic terminus, but not in the outer segment (at the protein level). {ECO:0000269|PubMed:29440555}.
Interaction partners:
Sequence:
MAKDLDELLDEVETKFCRLDPLRLDLGERPKGDGGGGSHSGDRNGAQEKETLRSTETFKKEDDLDSLINEIFEEPDFDRKSFQKFKSKSSSNTCVRAPMQGVSKSCSPVYLSGSAIPCGIGTNTSQRACDRLRCVACDFRIVSYNDYMWDKSCDYLFFRNNMPEFHKLKTKLIEKKGARAYACQCSWRTVEELTDLQTDHQLRWVCGKH
Protein: Cell cycle transcriptional repressor whi5 (Meiotically up-regulated gene 54 protein) (Q9HGL9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cyclin-dependent kinase 1
- MBF complex negative regulatory component yox1
- Serine/threonine-protein kinase csk1
- Zinc finger protein sfp1
Sequence:
MAGGHKKNEATRQTDEVIQQKYDESLSKHKNRCELSLTFEYKLSNKLRARLKAAFFKVDHGWEDQTLDQVETLVRKENHVHRRSRSINDLDSSKLRRPHHPNSIMGSNTGKLRASSFTRLVSPREGFAQLPYKKPVSPYSSSSAVSSTSSSFDRTSPPWLNYVEPHTELPRLPFELSHASTASAKSPLFGMNYHISRPEETDESLRLGTANLSRIRKSTSLPFPTAYPLSADDCKAAEVMLTLVNSMPSKKP
Protein: Protein SIX6OS1 (Six6 opposite strand transcript 1) (Q8N1H7)
Organism: Homo sapiens (Human)
Function: Meiotic protein that localizes to the central element of the synaptonemal complex and is required for chromosome synapsis during meiotic recombination. Required for the appropriate processing of intermediate recombination nodules before crossover formation.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q9CTN5}. Note=Component of the central element of the synaptonemal complex. In spermatocytes, detected from zygonema to pachynema and localizes along synapsed lateral elements. Loading to the central element of the synaptonemal complex is dependent on the assembly of the tripartite synaptonemal complex structure that occurs upon synapsis between homologous chromosomes. {ECO:0000250|UniProtKB:Q9CTN5}.
Interaction partners:
- Synaptonemal complex central element protein 2
- Synaptonemal complex central element protein 1
- Testis-expressed protein 12
- Synaptonemal complex protein 1
- Synaptonemal complex central element protein 3
Sequence:
MNDSLFVSLDRLLLEFVFQYEQDISTKEEMIQRINKCCEDIKENKVTICRIHETINATDEEIDHYCKHSEEIKDNCRNWKPTCDVFRKHEDYMQDQFTVYQGTVEKDKEMYHDYICQYKEVLKQYQLKYSETPFSREYYEKKREHEEIQSRVLACTEQLKMNETIFMKFRVPAPFPSLTKWTLNIVNLRCETQDILKHASNLTKSSSELKKEVDEMEIEINYLNQQISRHNETKALSETLEEKNKNTENRKELKERIFGKDEHVLTLNKTQSSQLFLPYESQKLVRPIKMHSSEPRVADIKEESSAKQSKLANIDFRQKENDTQIFNDSAVDNHSKCSHITTITSSQKFMQVRLLTPQKQSNSNQWSEKGDKDAEYGDKGTVRQVRESKCTSQAIYTEHFGKSVENDSDEVEERAENFPRTSEIPIFLGTPKAVKAPESLEKIKFPKTPPFEINRNRNAVPEVQTEKESPGLSFLMSYTSRSPGLNLFDSSVFDTEISSDQFNEHYSARNLNPLSSEQEIGNLLEKPEGEDGFTFSFPSDTSTHTFGAGKDDFSFPFSFGQGQNSIPSSSLKGFSSSSQNTTQFTFF
Protein: NADH dehydrogenase (EC 1.6.99.3) (Q38A31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Acyl carrier protein
- Electron transfer protein, putative
- Uncharacterized protein
Sequence:
MICRTSFLRKPKVVVVGTGWAGCYFVRDTKPQLAELHVLSTRNHHVLTPLLPQTTTGTLEFRSICEPITRIQPALAHLPNRFSRCFVYDINFEQKRVDCISVDNTSVGPHALVNTFDVQYDKLVLAHGAQPNTFNVPGAVERACFLREVNEARTIRKRLVQNIMTANLPVTSVEEKKRLLHTVVVGGGPTGVEFSADLAEFLRDDVKNINPELVQFCKVTVLEAGEVFSTFDLRVREWGKRRLDALGVRIVKGNVVAVQEKEVITKSGEVFSTGLVVWSTGVGPSPLTKELKVDRTRQGRISVDEHLRVLRDGVPIPDVYAIGDCATNESNPLPTLAAVASRQGVYLAKKINAELAGKPFATPFKYESLGSMVSLGTSSAVVELNGPRKLDFVGLKALFFWRSAYLSIVGSWRNRLYVIVNWLGSAIFGRDLTLINDYNDERTWLSLASEGAAREKVSRMNKVKTDGDGSNGNETTARSKVDLPATKKQNE
Protein: Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier atg8) (Q86CR8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ubiquitin-like modifier involved in autophagosomes formation. Participates in membrane fusion events that take place in the secretory pathway (By similarity).
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- PB1 domain-containing protein
- ZZ-type zinc finger-containing protein
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme atg7
- Cysteine protease
- Cysteine protease atg4
- Ubiquitin-like protein atg12
- Serine/threonine-protein kinase atg1
- Autophagy protein 5
- Autophagy-related protein 18
Sequence:
MVHVSSFKNDHPLDKRREVAERIRSKYLDRIPVIVEKAPRSDAPDIDKKKYLVPADITVGKFVYEIRKHMTKVSAEKAIYLFVNNTIPPTAALISQIYERYKDEDGFLYITYSGENTFGSDL