wanglab/gogpt-training-data huggingface dataset:
Protein: EKC/KEOPS complex subunit gon7 (A6X972)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Gon7 likely plays a supporting role to the catalytic subunit pgp2 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}.
Interaction partners:
- EKC/KEOPS complex subunit SPAC4H3.13
- tRNA N6-adenosine threonylcarbamoyltransferase
- Signal peptidase complex subunit 1
- Threonylcarbamoyl-AMP synthase
- EKC/KEOPS complex subunit cgi121
- EKC/KEOPS complex subunit SPAP27G11.07c
Sequence:
MNNLELTYKCETDTTRPFLKSLPVGFEPVEVDDYYISLKEQVRAMQDHCNEEFTKKMQTEGKNDVPEEKPIIL
Protein: Glutamate receptor ionotropic, NMDA 3A (GluN3A) (N-methyl-D-aspartate receptor) (N-methyl-D-aspartate receptor subtype 3A) (NMDAR3A) (NR3A) (NMDAR-L) (A2AIR5)
Organism: Mus musculus (Mouse)
Function: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. During the development of neural circuits, plays a role in the synaptic refinement period, restricting spine maturation and growth (By similarity). By competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting signaling and limiting the maturation and growth of inactive synapses. May also play a role in PPP2CB-NMDAR mediated signaling mechanism (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9R1M7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13224}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic density {ECO:0000250|UniProtKB:Q9R1M7}. Note=Requires the presence of GRIN1 to be targeted at the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q9R1M7}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 2D
- Disks large homolog 4
- Glutamate receptor ionotropic, NMDA 3B
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Proenkephalin-B
Sequence:
MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTTAPRAASRAQDGGRAGAQRDEPESGTWRPPAPSQGARWLGSALHGRGPPGSRKLGEGAGTETLWPRDALLFAVENLNRVEGLLPYNLSLEVVMAIEAGLGDLPLMPFSSPSSPWSSDPFSFLQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSSVLHIPVLSIVRHEFPRESQNPLHLQLSLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTENNSKFHLESIINITANLSSTKDLLSFLQVQLENIRNSTPTMVMFGCDMGSIRQIFEMSTQFGLSPPDLHWVLGDSQNVEELRTEGLPLGLIAHGKTTQSVFEYYVQDAMELVARAVATATMIQPELALLPSTMNCMDVKTTNLTSGQYLSRFLANTTFRGLSGSIKVKGSTIVSSENNFFIWNLQYDPMGKPMWTRLGSWQGGRIVMDSGIWPEQAQRHKTHFHHPNKLHLRVVTLIEHPFVFTREVDDEGLCPAGQLCLDPMTNDSSILDSLFSSLHSSNDTVPIKFKKCCYGYCIDLLEQLAEDMNFDFDLYIVGDGKYGAWKNGHWTGLVGDLLSGTANMAVTSFSINTARSQVIDFTSPFFSTSLGILVRTRDTAAPIGAFMWPLHWTMWLGIFVALHITAIFLTLYEWKSPFGMTPKGRNRNKVFSFSSALNVCYALLFGRTAAIKPPKCWTGRFLMNLWAIFCMFCLSTYTANLAAVMVGEKIYEELSGIHDPKLHHPSQGFRFGTVRESSAEDYVRQSFPEMHEYMRRYNVPATPDGVQYLKNDPEKLDAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPPNSPLTSNISELISQYKSHGFMDVLHDKWYKVVPCGKRSFAVTETLQMGIKHFSGLFVLLCIGFGLSILTTIGEHIVYRLLLPRIKNKSKLQYWLHTSQRFHRALNTSFVEEKQPCSKTKRVEKSRWRRWTCKTEGDSELSLFPRSNMGPQQLMVWNTSNLSHDNQRKYIFNDEEGQNQLGTQTHQDIPLPPRRRELPASLTTNGKADSLNVARNSVMQELSELEKQIQVIRQELQLAVSRKTELEEYQRTNRTCES
Protein: Replication enhancer protein (REn) (Protein AC3) (Protein AL3) (P03563)
Organism: Tomato golden mosaic virus (strain Yellow vein) (TGMV)
Function: Increases viral DNA accumulation. Enhances infectivity and symptom expression (By similarity).
Interaction partners:
Sequence:
MDSRTGEPITVPQAENGVYIWEITNPLYFKIISVEDPLYTNTRIYHLQIRFNHNLRRALDLHKAFLNFQVWTTSTTASGRTYLNRFKYLVMLYLEQLGVICINNVIRAVRFATDRSYITHVLENHSIKYKFY
Protein: Replication in mitochondria 2, isoform C (M9ND06)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MAQNTADTLIHLIAGGSAGTVGAVVTCPLEVVKTRLQSSTAFMTPSRLAENAGGGPANGGQSELLRPEQRRKLSTTILRNRSQPQIMAISHCGISSTTPKSMSIVQCLRHIVQNEGPRALFKGLGPNLVGVAPSRAIYFCTYSQTKNTLNSLGFVERDSPLVHIMSAASAGFVSSTATNPIWFVKTRMQLDYNSKVQMTVRQCIERVYAQGGVAAFYKGITASYFGICETMVHFVIYEFIKSKLLEQRNQRHTDTKGSRDFLEFMMAGAVSKTIASCIAYPHEVARTRLREEGNKYNSFWQTLHTVWKEEGRAGLYRGLATQLVRQIPNTAIMMATYEAVVYVLTRRFNNKSNEFYDF
Protein: Radial spoke head protein 4 homolog A (Radial spoke head-like protein 3) (Q5TD94)
Organism: Homo sapiens (Human)
Function: Component of the axonemal radial spoke head which plays an important role in ciliary motility. Essential for triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile cilia (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:19200523}.
Interaction partners:
- Radial spoke head protein 9 homolog
- Radial spoke head 1 homolog
- Dynein axonemal intermediate chain 1
- Dynein axonemal heavy chain 5
- Dynein axonemal intermediate chain 2
- Dynein axonemal assembly factor 1
- Protein kintoun
- Dynein axonemal heavy chain 11
- Thioredoxin domain-containing protein 3
- Radial spoke head protein 3 homolog
Sequence:
MEDSTSPKQEKENQEELGETRRPWEGKTAASPQYSEPESSEPLEAKQGPETGRQSRSSRPWSPQSRAKTPLGGPAGPETSSPAPVSPREPSSSPSPLAPARQDLAAPPQSDRTTSVIPEAGTPYPDPLEQSSDKRESTPHHTSQSEGNTFQQSQQPKPHLCGRRDVSYNNAKQKELRFDVFQEEDSNSDYDLQQPAPGGSEVAPSMLEITIQNAKAYLLKTSSNSGFNLYDHLSNMLTKILNERPENAVDIFENISQDVKMAHFSKKFDALQNENELLPTYEIAEKQKALFLQGHLEGVDQELEDEIAENALPNVMESAFYFEQAGVGLGTDETYRIFLALKQLTDTHPIQRCRFWGKILGLEMNYIVAEVEFREGEDEEEVEEEDVAEERDNGESEAHEDEEDELPKSFYKAPQAIPKEESRTGANKYVYFVCNEPGRPWVKLPPVIPAQIVIARKIKKFFTGRLDAPIISYPPFPGNESNYLRAQIARISAGTHVSPLGFYQFGEEEGEEEEEAEGGRNSFEENPDFEGIQVIDLVESLSNWVHHVQHILSQGRCNWFNSIQKNEEEEEEEDEEKDDSDYIEQEVGLPLLTPISEDLEIQNIPPWTTRLSSNLIPQYAIAVLQSNLWPGAYAFSNGKKFENFYIGWGHKYSPDNYTPPVPPPVYQEYPSGPEITEMDDPSVEEEQAFRAAQEAVLLAAENEESEEDEDEEDDYD
Protein: Transcription factor TCP14 (AtTCP14) (Q93Z00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved the regulation of plant development. Together with TCP15, modulates plant stature by promoting cell division in young internodes. Represses cell proliferation in leaf and floral tissues. Together with TCP15, acts downstream of gibberellin (GA), and the stratification pathways that promote seed germination. Involved in the control of cell proliferation at the root apical meristem (RAM) by regulating the activity of CYCB1-1. Involved in the regulation of seed germination. May regulate the activation of embryonic growth potential during seed germination. Acts together with SPY to promote cytokinin responses that affect leaf shape and trichome development in flowers. Transcription factor involved in the regulation of endoreduplication. Represses endoreduplication by activating the gene expression of the key cell-cycle regulators RBR1 and CYCA2-3. Regulates the expression of the defense gene pathogenesis-related protein 2 (PR2) in antagonism to SRFR1, a negative regulator of effector-triggered immunity. Involved in positive regulation of plant defense. Represses jasmonate (JA) response to promote disease resistance. Regulates the plant immune system by transcriptionally repressing a subset of JA-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:28132837, ECO:0000269|PubMed:29250092}. Note=Localizes in sub-nuclear foci. {ECO:0000269|PubMed:28132837, ECO:0000269|PubMed:29250092}.
Interaction partners:
- Dof zinc finger protein DOF3.2
- Transcription factor TCP13
- Protein DA1-related 1
- Protein DA1-related 2
- DELLA protein GAI
- Transcription factor TCP5
- Transcription factor TCP17
- Suppressor of RPS4-RLD 1
- Transcription factor TCP2
- Transcription factor TCP3
Sequence:
MQKPTSSILNVIMDGGDSVGGGGGDDHHRHLHHHHRPTFPFQLLGKHDPDDNHQQQPSPSSSSSLFSLHQHQQLSQSQPQSQSQKSQPQTTQKELLQTQEESAVVAAKKPPLKRASTKDRHTKVDGRGRRIRMPALCAARVFQLTRELGHKSDGETIEWLLQQAEPSVIAATGTGTIPANFTSLNISLRSSGSSMSLPSHFRSAASTFSPNNIFSPAMLQQQQQQQRGGGVGFHHPHLQGRAPTSSLFPGIDNFTPTTSFLNFHNPTKQEGDQDSEELNSEKKRRIQTTSDLHQQQQQHQHDQIGGYTLQSSNSGSTATAAAAQQIPGNFWMVAAAAAAGGGGGNNNQTGGLMTASIGTGGGGGEPVWTFPSINTAAAALYRSGVSGVPSGAVSSGLHFMNFAAPMAFLTGQQQLATTSNHEINEDSNNNEGGRSDGGGDHHNTQRHHHHQQQHHHNILSGLNQYGRQVSGDSQASGSLGGGDEEDQQD
Protein: Putative cytochrome c biosynthesis ccmC-like mitochondrial protein (Q2F993)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion membrane {ECO:0000256|RuleBase:RU364092}.
Interaction partners:
Sequence:
MSVSLLQPYFFMSKTKSYAQILIGSRLFLTAMAIHLSLRVAPPDLQQGGNSRISYVHVPAARMSIVIYIATAINSSLFPLTKHPLFLRSSGTGTEIGAFSTLFTLVTGGFRGRPMWGTFRVWDARLTSVFILFLIYLGALRFQKLPVEPAPISIRAGPIDIPIIKSPVNWWNTSHQPGSISRSGTSIHVPMPIPILSNFANFPFSTRILFVLETRLPIPSFPESPLTEEIEAREGIPLKT
Protein: LRRGT00184 (Q6QI24)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAACPGTAVPVWLSEEDLSCIICQGLLDWPTTLPCGHSFCLQCLKDLWVSKRAGVDSCPWACPICRKGPSAKPVLHKNPLLQDLVDKYRQAALELEAGPEPAPVPRSLCTPTPPQVTVQKSTTQVVQELTELVGQLVDIVKSLQTQRPSLASGLDNALGILHMDSSSEEEYPLDSPKLVTFSASQKKIQEILRDLEKIQETLQGSVTGNEAPKKQVEEMASSVGLLPDQRYPVSRKASQFSLWAISPTFDLRSLSCNLEVSNNCRMVTVSRALQPYHWSSERFSISQVLCSQAFSSGQKYWEVDTRNCSHWAVGVASWGMKRDKMLGRTMDSWCIEWRGPSQFSAWAMMKKTDLSSGPPEVVGVWLDLELGKLAFYSVADQERPLYECEVSSSSPLHPAFWLYGLTPGNYLEILQIYKIVHEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEETVCLQGRCSIHESVDVPKALVPRRTPSSSPPPPASAEPEEAELACPGSEAERQRRSRCRRTMSVIFSSDQVNSRALPPHVADIIGKHSRVGKTSLIMSLVSEEFPEE
Protein: Ubiquitin-conjugating enzyme E2 5A (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 5A) (Ubiquitin carrier protein 5a) (OsUBC5a) (Ubiquitin-protein ligase 5A) (Q8S920)
Organism: Oryza sativa subsp. japonica (Rice)
Function: E2 conjugating enzyme that associates with the E3 ubiquitin-protein ligase EL5 to mediates ubiquitination of target proteins.
Interaction partners:
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- Os05g0392000 protein
- Os05g0392050 protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 11
- Os10g0491801 protein
- Ubiquitin-ribosomal protein eS31z fusion protein
Sequence:
MASKRIQKELKDLQKDPPTSCSAGPVGEDMFHWQATIMGPSDSPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRHKYENTARTWTQRYAM
Protein: Tetraspanin-17 (Q11098)
Organism: Caenorhabditis elegans
Function: Protects dopaminergic neurons against oxidative stress-induced neurodegeneration. May act partly via dopamine receptor dop-2 to negatively regulate dopamine reuptake transporter dat-1 activity. Also plays a role in modulating behaviors linked to dopamine signaling. Confers protection against oxidative stress in the whole body.
Subcellular location: Cell membrane {ECO:0000305|PubMed:25474638}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000305|PubMed:25474638}. Cell projection, axon {ECO:0000305|PubMed:25474638}. Note=May localize near the nucleus or ER. {ECO:0000305|PubMed:25474638}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 1
- Elongator complex protein 2
- Tetraspanin
- Tetraspanin
- Transthyretin-like protein 33
- Neuroligin-like protein glit-1
- Tetraspanin
- Tetraspanin
- Tetraspanin
Sequence:
MATERDGGGCLRVAVSIFSIYYWLSALGHVFLGLWMLLDPKRNYILDLVHFSENDPLLKASAYVSLVCGCAQLLVGFLGLCGAVNRSRFLLLAFVMFLIGTFLADVAMGTLSLFYKDKFSNNYMGVYLKNLTYNRYSRDRWVLPLMDTIQFYVYSVKENVREIVKSKYGVMTSEPENKMVTEFIDKLQFYEKCCGSLGPTDYISSRWSQSTNQDSEEIESPLFPVSCCTQITGASALNPLAKSYARCQQIGANRQWRHAVGCSERLMSWFNEQIWIFVGFGFGSALTMMLGICLSCCLISKIRIYHVIRDDY
Protein: Protein transport protein sec23-1 (O74873)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Protein transport protein sec31
- Protein transport protein sec24
- Protein transport protein sec13
- Uncharacterized protein C4.03c
- COPII coat assembly protein sec16
- Protein transport protein sec23-2
- Small COPII coat GTPase sar1
- Large ribosomal subunit protein uL11A
- Large ribosomal subunit protein uL11B
- Protein transport protein sec22
Sequence:
MNFEEIEERDGVRFTWNVFPSTRIESSRTIVPIASIYKPLNERPDLPPVLYEPVTCKAPCKAVLNPYCHIDTRAKFWICPFCLQRNMLPPQYKDISNTSLPIELLPEYSTIEYTLPRPPQLTPVFLFVVDVCQDEENLQALKDSLIISLSLLPPECLVGLVTFGTMVDVYELGYTECSKSYVFRGSKDYTSKQIQEMLGLPTSNVSPVALQQARSFQGSAAPSRFLLPIQQCEFQLTNILEQLQPDSWPVANDRRPQRCTGTALNISVSMMESVCPNSGGHIMLFAGGPSTVGPGTVVSTELREPIRSHHDIERDQAKHVKKALRFYEGLTKRVSANGHAVDILAGCLDQIGIMEMKSLASSTGGYLVLSDSFTTSIFKQSFQRIFGRDSLNNMLLGFNATMEVLTTKELKISGLIGHAVSLNKKSQNVGDIEIGLGNTNSWKMCGISPKSTYAIYFEVATQSASAPQGDSRGLVQYLTLYQHSSNTFRLRVTTVARAFADGGSPLIVNSFDQEAAAVAMARIAAFKAEVDDGPDVLRWTDRMLIKLCQKFAEYRKDDPSSFRLSSQFTLYPQFMYYLRRSPFLQVFNNSPDETAFYRHMLNHEDVNNSLIMIQPTLQSFSFEHPGGVPVLLDAVSVKPDVILLLDTFFHILIFHGDTIAQWRNAGYQNQPEYQNLKELLEAPRVEAAELLIDRFPIPRFIVCDQGGSQARFLLSRLNPSETHNTTSMYGAPPAHAILTDDVSLQTFMSHLKKLAVAVS
Protein: RIC8 (Q7SD74)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Interaction partners:
Sequence:
MASIGVSGPAKLQAVTTLIHKLTEDLKSTSLSPEERDKALEELKVYGRDPRNADPIFTKQGIETLTKHAFDSPSETTSRNALRVLCNAMLLIPETRQRFVDLGYESKACEKLKNDNWDDEFLATRVIFFSTYGTTVDLAKLIDEHHLAESMVANLARHASRISEHAKNKTKPDPMELMALGETLRLLFNVTSKCPSKLDCFTAAVPHIVTLLLSLDIPPPKGTPPLESPLSPLVNALMNLKLDSEEARSCLYPKDAPSSLAEKLITLLDLSLKAYSDQELDATVTPLVCIISSIYENAPADSPVRDFIRKSLLPSEEERNKVLGKGDTLPAKLLANMTNPIAPEFARAVSHLLFNVSDKDANKFVENIGYGYASGFLFQNNIPVPEGLGGDAEKGESSQAGQSSRRAVNPITGQFLDTETFPDMPEMTMEEKEREAERLFVLFERARKLGIVNVENPVAKAVQEGRFEELPDDYEEDSD
Protein: Meiotic recombination protein REC8 homolog (Cohesin Rec8p) (Q8C5S7)
Organism: Mus musculus (Mouse)
Function: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II.
Subcellular location: Nucleus {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}. Note=In meiotic chromosomes, localized along axial elements in prophase from the leptotene to diplotene stages. At later prophase stages, diakinesis and metaphase I, localized along interstitial axes of chromosomes including both centromere and arm regions. No longer detected in arm regions in anaphase I but persists on centromere regions until metaphase II. {ECO:0000269|PubMed:12034751, ECO:0000269|PubMed:12759374, ECO:0000269|PubMed:16855401, ECO:0000269|PubMed:22346761}.
Interaction partners:
- Cohesin subunit SA-3
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1B
- Double-strand-break repair protein rad21-like protein 1
- Structural maintenance of chromosomes protein 1A
- Separin
- Cohesin subunit SA-1
- Cohesin subunit SA-2
- Shugoshin 2A
- Double-strand-break repair protein rad21 homolog
Sequence:
MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLNVNVVKTCEEILNYVLVRVQPPVAGLPRPRFSLYLSAQLQIGVIRVYFQQCQYLVEDIQHILEHLHRAQLRIRIDMEEADLPSLLLPNCLAMMETLEDAPEPFFGKMSVDPRLPSPFDIPQIRHLLEAATPEKTRKETLPEATPDPRKPDRTLATVQSPEVITLQEAEPIRMLQIEGEQDLPEISRGDLELLIAEKDDAILLEERQRGRLLRQRRASLPLDESREEPRALEGAGLVSALSPPAPAQVEGIQEALPGQVFPPEVQKMTGWEPGALLTEVTPPQELRLPAPPSTEKRLPSLQRPLPRRHRRRQLLFWDKETQISREKFEEQLQTGAHCWEYPVAQPPKRMLTSPAELFRTPTLSGWLPPELLGLWTHCAQVPQRMLRQRPQLETEETVEEERAADEEERRKTEALSEIEVLREAQEPSGPLMLSSELSLEAAEDEKSRTSLIPPEWWAWSEEGQPEPPALPMLPELPEVPMEMPPRPELSSEAVLRAVALKLQANKELDFSSLVPPLSPRKLASRVFYLLLVLSTQKILLVEQQKPYGPLLIRPGPKFP
Protein: Ceramide synthase 4 (CerS4) (EC 2.3.1.-) (LAG1 longevity assurance homolog 4) (Sphingosine N-acyltransferase CERS4) (EC 2.3.1.24) (Q9HA82)
Organism: Homo sapiens (Human)
Function: Ceramide synthase that catalyzes formation of ceramide from sphinganine and acyl-CoA substrates, with high selectivity toward long and very-long chains (C18:0-C22:0) as acyl donor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D6J1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingolipid delta
- Sphingolipid delta
- Sphingomyelin phosphodiesterase 2
- Ceramide kinase
- 3-ketodihydrosphingosine reductase
- Alkaline ceramidase 1
- Acid ceramidase
- Alkaline ceramidase 2
- Ceramide glucosyltransferase
- Sphingomyelin phosphodiesterase
Sequence:
MLSSFNEWFWQDRFWLPPNVTWTELEDRDGRVYPHPQDLLAALPLALVLLAMRLAFERFIGLPLSRWLGVRDQTRRQVKPNATLEKHFLTEGHRPKEPQLSLLAAQCGLTLQQTQRWFRRRRNQDRPQLTKKFCEASWRFLFYLSSFVGGLSVLYHESWLWAPVMCWDRYPNQTLKPSLYWWYLLELGFYLSLLIRLPFDVKRKDFKEQVIHHFVAVILMTFSYSANLLRIGSLVLLLHDSSDYLLEACKMVNYMQYQQVCDALFLIFSFVFFYTRLVLFPTQILYTTYYESISNRGPFFGYYFFNGLLMLLQLLHVFWSCLILRMLYSFMKKGQMEKDIRSDVEESDSSEEAAAAQEPLQLKNGAAGGPRPAPTDGPRSRVAGRLTNRHTTAT
Protein: Leucine-rich repeat protein kinase family protein (Leucine-rich repeat receptor-like protein kinase) (C0LGT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MEQLKVLPLLFLSWVMFLQSTHQLPNSQTQVLYQLRKHLEFPKALESWGNYYGDLCQIPATAHMSITCQGNSITELKVMGDKLFKPFGMFDGSSLPNHTLSEAFIIDSFVTTLTRLTSLRVLSLVSLGIYGEFPGKIHRLNSLEYLDLSSNFLFGSVPPDISRLVMLQSLMLDGNYFNGSVPDTLDSLTNLTVLSLKNNRFKGPFPSSICRIGRLTNLALSHNEISGKLPDLSKLSHLHMLDLRENHLDSELPVMPIRLVTVLLSKNSFSGEIPRRFGGLSQLQHLDLSFNHLTGTPSRFLFSLPNISYLDLASNKLSGKLPLNLTCGGKLGFVDLSNNRLIGTPPRCLAGASGERVVKLGGNCLSIIGSHDQHQEFLCEEAETEGKQFQGRKVGILIAVIGGAVLVLVFFVLVILLLLCTNRCSSCCSREKSVPQTRLKVVTDNSHTSLSSEVLASARLISQTAKLGAQGVPSCRSFSFEDLKEATDDFDSSRFLGEGSLGKLYRGTLENGSSIAIRCLVLSRKFSSQSIRGHLDWMAKLNHPHLLGFLGHCTQTSGEHDPVATILYLVYEYMPNGSYRTHLSESFSEKILTWPDRLAILIEIAKAVHFLHTGVMPGSFNNQLKTNNILLDEHKIAKLSDYGVSAIIEENEKLETKSETHKSKKKAKREDDVYNFGFILLESLIGPVPTTKGEAFLLNEMTSFGSQDGRQKIVSPTVLTTSSQESLSIAISIANKCVLLEPSARPSFEDVLWNLQYAAQMQSAADAERKSDTSS
Protein: Mannitol-1-phosphate 5-dehydrogenase (M1PDH) (MPD) (MPDH) (EC 1.1.1.17) (Q8NJJ1)
Organism: Aspergillus niger
Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH. Required for protection of conidiospores against exogenous stresses such as high temperatures and an oxidative environment.
Interaction partners:
Sequence:
MGKKAIQFGGGNIGRGFVAEFLHKAGYEVVFVDVMDKMVEALQQNKSYKVTEVSEEGEHTTTITNYRAINSKTHESDVIQEIATADVVTCAVGPHILKFIAPVIAKGIDARTESKPVAVIACENAIGATDTLHGFIKQHTSQDRVESLYDRAQFANSAIDRIVPQQAPNSGLDVRIEKFYEWAVEKTPFGSVGHPDIPAIHWVDNLEPYIERKLFTVNTSHATTAYFGHFRGKKMIADALEDEEIRGLVHKVLEETASLIVAKHDISEEEQKEYVKKIVSRISNPYLEDKVERVGRAPLRKLSRKERFIGPASQLAERGMKYDSLMDAVEMALRFQNVPGDDESAELANILNEQRAEDATIHLTGLDEEHPLYPAVLERVRKVQQGTK
Protein: Serine protease 23 (EC 3.4.21.-) (Q9D6X6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAGIPGLFILLVLLCVFMQVSPYTVPWKPTWPAYRLPVVLPQSTLNLAKADFDAKAKLEVSSSCGPQCHKGTPLPTYEEAKQYLSYETLYANGSRTETRVGIYILSNGEGRARGRDSEATGRSRRKRQIYGYDGRFSIFGKDFLLNYPFSTSVKLSTGCTGTLVAEKHVLTAAHCIHDGKTYVKGTQKLRVGFLKPKYKDGAGGDNSSSSAMPDKMKFQWIRVKRTHVPKGWIKGNANDIGMDYDYALLELKKPHKRQFMKIGVSPPAKQLPGGRIHFSGYDNDRPGNLVYRFCDVKDETYDLLYQQCDAQPGASGSGVYVRMWKRPQQKWERKIIGIFSGHQWVDMNGSPQDFNVAVRITPLKYAQICYWIKGNYLDCREG
Protein: Putative endonuclease C1F12.06c (EC 3.1.-.-) (Q10348)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative 2-hydroxyacid dehydrogenase UNK4.10
- Protein mmf1, mitochondrial
Sequence:
MNNDNLHDKLTIWRQQQIELKGMLQLIPKFQSLNEIRYVVGLDISFDKSSPKAVSALVIYDLEQRMIIYKDYLCIEKLEEDYVPGFLSFREIKWYLPLLNHIPHQFRIDIILVDGNGVLHPVGFGLACHLGVLLNLPVVGVAKNYLHCVGLTESLDAHRETLKKHVLKKTTDHPILIHSIDQSSEILGAAVWTSSNSKRPVYVSIGNQMNLEQSIQLVQKCSSSHSRVPEPIRQADIYAKFVLSQSKRNKKN
Protein: ATPase, AAA family (Q72BF0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase, putative
- Ribosomal RNA small subunit methyltransferase E
- Glycosyl transferase, group 2 family protein
- FtsK/SpoIIIE family protein
Sequence:
MSVRQPLPERLRPTVLEGFVGQTHLTQRIEALLRANRLPSLLLFGPPGCGKSTLALLLAKARSANVLRLSAPEAGLQHLRKQLHGVDILVLDELHRFSKAQQDFFLPLLESGDITMLATTTENPSFSVTRQLLSRLHVLRLRPLGRAELLELGRRGAVAQEVQIEDDVLDLLASMSHGDARTMLNLLEYVAALPEDKRDIEGVRSAMPEIVSRHDKDGDNHYELASALIKSIRGSDPDAALYYLACLLEGGEDPRFVCRRLILSASEDVGLADPQALPLAVACMQAVEYVGMPEGFIPMAQTTVHLALARKSNSTYAAYINAARELKTQGRKGVPLHLRNPSTRLQKEWGYGKGYRYPHSYPEGWIEQEYLPEGLEDRRFYAPRENGEEPRLSAWWRKLQRQRPPRRGSGE
Protein: Complex 1 LYR protein domain-containing protein (Q381P1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSALLPREAVALLYRRYLKAANSIPNVTIRMLLLQQIRSGFRRNRGITSPSAQRELINQAHKDLQVLEDERLSRTLYINRLGLVSCLDWEVRRTEYNFTPESQNFIAAFLMLGFMLIAVVAMNAKPIEVRHPDISEMVGAMAMRLEANSPEELRQIRERQIRTGLERQQHRLSLEHRVLATFHDAPGVRLEPPSLRNPYGIVSNEG