wanglab/gogpt-training-data huggingface dataset:
Protein: Putative ribosome biogenesis protein C8F11.04 (U3 snoRNP-associated protein C8F11.04) (Q9UT32)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in rRNA-processing and ribosome biosynthesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized RNA-binding protein C1827.05c
- ATP-dependent RNA helicase has1
- Pescadillo homolog
- Ribosome biogenesis protein erb1
- GTPase grn1
- Ribosome biogenesis protein ytm1
- Ribosome assembly factor mrt4
- Probable rRNA-processing protein ebp2
- Uncharacterized NOC2 family protein C1142.04
- 25S rRNA
Sequence:
MALKELLGSDAPLEKVCSALLEYESKRKSSENIDSESKKTNLLEDEQDDIEPVWLQLATLKFIGNNRKLIPYKIAIKNPVIPSSSEACLIVKDPQRVYKDLVNEAGLSKVVTRVIGLSKLKAKWNSYEQKRQLRDQFDIFLADDRVIPMLPRILGKTFYQKSKVPVPVKISKGTAEQLKREVVSAYGATYFNSAPCSSFMIKCGHVSNTSTELAENVESILQFVSKHIVPDGAKGIASIHLKTSQSIAIPLWNNPNLKELIASSRKVVTKETASSKRKSDEESLPSQKKQKKVEVAKESKDSKQQNVSDKKQVTVKEVPKKLSVKNAAKTTNRDEDSKGKKAKASPKVSQSSLKANGTTAIKKVKAGKNKVKH
Protein: DNA primase (EC 2.7.7.-) (P03193)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}. Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
Interaction partners:
Sequence:
MSAPVVIKALVASNTDIAEAILDAILSRPDEGFRLFCLCHNASPLHHVAGSLVELQLHLPKKRLTSQSRCGLVLTLHLPAEEAFPFLRGLTPLTADRLSTYLDRAGALRSLTPLVELLTLSAKKQPQGDARGRVAWLRPKIVGCLRRIYRVNISARWFISTFGSHEAQFVLVTAAYYFWGIPCTIETLAHLTELFTSESGQSLAAVTSLAELGEVFGSSAWAEQTEAFAHFAHEKLRRDSREIRAVARTIDAYRGRLPLASADLVRYVYLAHAQCFNEGTFKRYSQLTSMGEIGCLPSGGVVLPSLLDRGFAEHMRTYFTRETYLAEHVRVQQLKIRMEPPAPYTWDPDPDDGLMRAWAGLSVDVARELVELARWHADEGPTYPPTLQGFLCLAGQATCRGQWNPKEQFLPPTVLRRVQRLPVFLCHFADRHYFVMTAADPFSSHLAEVVSTPTNCRLPDTCLTRALSYTPVYYSQNSLSEQLFVSRHEYFNPRLPVCNLVLDLDLKIKGAPWSLEEIYDLCRTVRREVLRLMRRLGPVSRAHPVYFFKSACPPADPDNMEDVLPFCICTGKLGFRVITPLPRGHAIVGTSAVQGFVSVLQKLMGLTACLRRMRHKIKEIGAPLFDSGVYHAGRCIRLPHTYKVDRGGGLSRQLRLFVCHPEEEDKHSYVKNALNIQNLLHHSLHVGWPAPKTFCYHIADDGRDYLIQRTRETLPPTVENVCAMIEGHLGLDLVAWVSSCIWPSLMSTLATAVPEDKFPQFLHVTFEQTGPNLVQVCHARGRNFACLRHTHRASSKNVRVFLVLYYTSQAITVTFMSQCFAGRCGANQPTAHFSISVPASRIINRAEASQDSTTSQLARRRDRQDGSFSETLPN
Protein: THH1/TOM1/TOM3 domain-containing protein (Q54CF9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKIILIILIILINFIGIFVKCEFKIKSSTIKQKSAGVLDGTTLNFGYIDVELDDDLYRYDPLGCPNYDCTTLVENGDCTCDYTDMEECPKSFKNANCVNQCAMFAPNSSIPMCGTDPWTTLNVDQEQHIFSGTEGKEIFFRYKANPKICEGVAIIAYPIEGYFRGTFGSHPINQREMPSANYQTYNVFNLCPTDNQPFSNYLSWTPDTYYITIIPMSEGNITFSLRIHSGQVPPTPSTPITPCTRNLSSHICLDDGVPYVGEILGPAYEYFTFQTTKPAYYILSAPRLAQDLNLVISEDPENTKPIFGNRQSKYELAEESDDYLLVYIDQPTLLYIGLYCNFNTNYSFSITSQGQYYSTKITSLPASAGAFALTKSARLKLPNGSFLTCPTWYLCLSLTTQYPLEDGNPLWPVPPYFLQSSSYESINYEDVFLPNPMKPKSYQMTVLLSSKISTSSTSIFYSIDLISNSTLEFISTLFNSKGEPLRGSTTMKNVDLLATCNYTDFQLILNAMEETQSILFNVTDLNGLNNWRYRLEALTIRDNWIGCSNQASSLLDTVEVSKNVSTTYCPYGIDDKAKSIDPCCNSSFSFFQCCVPKVSLIPTVQFVSTIDDKIENQCSSFECTQSVLSEYYKSLSNADECTVPDYITRNLKLSAAETVRACKVPTRIPCDNDDHCKNTTLTKCDLFSRYCIPNLENIDKIYIECVLRNLSPSVLYAFAQISSQSVNDSLVQSFYNENIQDDCISETFVDSDILRNAMFYTSPSIKFDRCYPPVVCLDSSCVLEHDICFDQLYTVFQEFDFPADFNCSLYGFCQIESSTCYGVYEIGSACSQLCDATTSYCGHCSSENQTYCHQITTLTDETTCKSNSACLLPNGEYQLGVTKEQCESLGQCSDGCGYECSGYIGCVIENSYNSTDCTAHTGAVWNPQYDVCTFVSATSPSTCSSNSYSWIDCSSHSPDECYPITCSVQRVPCTTKDSCIGSGGTCSDQFFSSSSNTYFYPDGVGKCIRGHFSYRTGSFPSCDYNNENDSPMGCFPSHPNHTDKISCETIGGGKWWAPAINKTQCLSKKACKILDINSDNLPFNFRFNEMDEQQCTGCYQSNNQWTEMFSWSAARWIPGVFIENLDWIENNSFKAYSHPKKTFNYRSFYTNLMNSVDTLTADYLRSETFCRMERIQSNLNSISCSCSGGSECFTESIPLVGQTKPCFGESSTFSFDYGEIIFESESIKQGCPILLISQYSKEIFTSTAPESLPSNFVSYQVPEKYGVLNDKDAIVGVLIGDGIYIKAQFSIINKLTVCSIIPESQRTTSKFPVYDFATLISNTDDDYDDYHIFDGELIILDSVVFNKTAKDGSLMICSNFSNFNPKSSVQAFFPVIRVHGNWNDVSKQVFDESTRGLLFTLATFYLLVGLWAIFQLGVIVFKQINLPKVNFQLVNGLTLIVTIFILMRSLYFFILPNGHLAGSPTSDYILVILPTFIYFTAFTVIIVLWYVIVFLVLKKNRSAESLSRRVSKLVLYVNIVIYLLFIACCLVFTKTQSNPTNDCGSRIIIPAKSSIPQKAISITYAVIQAIISVLLGAAFVYLGSSLFFVMHKTRKALGGSSINSSHYNRIFLLTLICSIGFILHCVFILVLVSGHSSIAFSFVGLIITEIIPTLTILYCYDPFKKIETKSKSSEISM
Protein: Secreted and transmembrane protein 1 (Protein K-12) (Q8WVN6)
Organism: Homo sapiens (Human)
Function: May be involved in thymocyte signaling.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted.
Interaction partners:
- T-cell antigen CD7
Sequence:
MQTCPLAFPGHVSQALGTLLFLAASLSAQNEGWDSPICTEGVVSVSWGENTVMSCNISNAFSHVNIKLRAHGQESAIFNEVAPGYFSRDGWQLQVQGGVAQLVIKGARDSHAGLYMWHLVGHQRNNRQVTLEVSGAEPQSAPDTGFWPVPAVVTAVFILLVALVMFAWYRCRCSQQRREKKFFLLEPQMKVAALRAGAQQGLSRASAELWTPDSEPTPRPLALVFKPSPLGALELLSPQPLFPYAADP
Protein: Tryptophan 5-hydroxylase 1 (EC 1.14.16.4) (Tryptophan 5-monooxygenase 1) (P17532)
Organism: Mus musculus (Mouse)
Function: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.
Interaction partners:
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- Pterin-4-alpha-carbinolamine dehydratase 2
- Tryptophan 2,3-dioxygenase
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Dihydropteridine reductase
- Sepiapterin reductase
- Tryptophan 5-hydroxylase 2
- L-amino-acid oxidase
Sequence:
MIEDNKENKENKDHSSERGRVTLIFSLENEVGGLIKVLKIFQENHVSLLHIESRKSKQRNSEFEIFVDCDISREQLNDIFPLLKSHATVLSVDSPDQLTAKEDVMETVPWFPKKISDLDFCANRVLLYGSELDADHPGFKDNVYRRRRKYFAELAMNYKHGDPIPKIEFTEEEIKTWGTIFRELNKLYPTHACREYLRNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEETVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKIACKQECLITSFQDVYFVSESFEDAKEKMREFAKTVKRPFGLKYNPYTQSVQVLRDTKSITSAMNELRYDLDVISDALARVTRWPSV
Protein: Neurexin-3-beta (I2HAJ7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRQKFDDTGQYLTIWLVFTVSLFSVVDSIILTGAPDSYARYPKWAHSFENSLSMELKTRQSDGMLLYTDDGGTHGNFYSLTIVEGHIQLDFRLGDNSNEFGQRRPVNTIRIEEVRIDDDKWHTLTIFQSWENVKLELDYTLVFKILNQRSFVFGNILKNSDVFIGGLPPNMHMLPVMSSPLRRYARHLAVNVRNLMYRQYPQGVTSPQLLESVGTRTNEDDHCKSKSMSSREQFVCLNDGECYSSNDGPHCDCQFSDHDGRNCEIEKNDGELTFGGDEWVGYDVSLNISAAVRAKKENLTLTFKTVHGTSMLFYAGDEKSYLHVMLQDGAIIASSKFDGSDARIIRMFNSFPSQRYDDDSWHTIILERSLQMHSEEMVAIHMTLIVDGRRDEIRQYAPELDWISNSFGFLGSIPKHNPSKEVNRVSFRGCMKKVRYDIDATRILLVNLADQSYGGSVVKTEGDISYSCKNPSQRSDVLSFTETSSYLTLPRWNSLSSGSLSFHFRTTSSDGLILYHGVMQHNATDYVAFELIDSHLFMIINLGSGVVRLQTTSMKVSDGEWHHVQLDRLSRTGSVIVDAIKIDFSTPGVSANLIIDDPIFIGNVPNNSLVYPSSVWSIALQKGYTGCIKNIRMNGVSTKIGQEFEASNSTGIELGCSLSNELDICEPNPCQNFGKCSKNLNSFDCDCSNTNFEGKQCELEQTAVEVNGEESKVHVLAHTKVSQVEHIKIRFRTTSSRGVLFDTGANGKNDKITVFLNDSQLNLFLQDSSTNNTFSWGKSLSDNHWHELQVRRLGQKLLLYLDGFWSHSIYLQNPISVEIDEVGAAFSVHSSAPPPRDEHFKGFLSKLVFNGNDYLAKTKMNSAQLSKSSSRESKGQRNVKTRIASISFTNSTGYVAFSSDKISGLTGSFRVQFKFQTLMRSALLFFTLPKHDYDQSFRLQMLNGRLKYTYRTSGQEFHTTSPKLPHRQHLSDMRWHNVLIYQDEKTHDHVLLVDNSSTTLIIDKIKKVESKMSGKLYFGSNPLGVSRPSNGFRGCISTLRINENALDLYEDADSRMKVNRGCSGPIARCIEDACANHGRCIQLWSSIRCDCSLTAHSGDRCQNPSTTVRFDGSPSAIFYEYAPNERPTTSKDYFVFSFRTTQPNGVLISIECAADQDYFTIFLNKGYLNAHYNLGNRDHTTSYHTRILNDGFPHVIKISRTEANMTIQVDKLPSLRYRPKRASDLVLLNMQTRISIGAAFNTRHLDQKRLLRHRRNTEIFDSYQGEISGVNVNGLMILDLYENGSNRIHTIGAPQTTAVSEQVSSESEEDDELAEMMMAHSIDENPNEALIESLAPSCLSLEEQQSCFIDTDDSTGFFSPVLPTVANFPTTRQTEHIDNEVTALITSSLAPQKTRPKSTPHFTVYPVRPTTPMGDTITTTMQAATVTDFPRTPLIMCSSLAVIIAIAAVVFFVFKCRQNPPNSEHYTMAMKSQSGYTAIAPELSPPMNHDRSNDSCTQPLLAKPHINGNGYEPLKGAVIANGNGATATMMRNGNGNGVAKKKDFKEWYV
Protein: Cysteinyl leukotriene receptor 2 (CysLTR2) (Q920A1)
Organism: Mus musculus (Mouse)
Function: Receptor for cysteinyl leukotrienes. The response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTC4 = LTD4 >> LTE4.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Cysteinyl leukotriene receptor 1
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Leukotriene C4 synthase
- Neurotensin/neuromedin N
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein subunit alpha-14
Sequence:
MEVTGTPSSYSNRNCTIENFKKEFYPIIYLIIFFWGALGNGFSIYVFLQTCKKSTSVNVFMLNLATSDFLFISTLPFRADYYFRGSNWIFGDLACRVMSYSLYVNMYTSIYFLTVLSVVRFLATVHPFRMFHVTSVRSAWILCGIIWVFIMASSALLLVNGQEEKDNIISCLELSPQKFKSLLIMNHIAVAVGFLLPFLTLTVCYLLIIRILLKAEIPESGPRAAHRKALTTIVIAMITFLLCFLPYHALRTLHLVTWDKDSCGDVLHKATVITLTMAAANSCFNPFLYYFAGENFKARLRAIFSKVHL
Protein: 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2 (At3BETAHSD/D2) (EC 1.1.1.418) (4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-2) (Reticulon-like protein B19) (AtRTNLB19) (Sterol-4-alpha-carboxylate 3-dehydrogenase 2, decarboxylating) (Q67ZE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3beta-hydroxysteroid-dehydrogenase/decarboxylase involved in sterol synthesis. Catalyzes the formation of 3-oxosteroids from 3beta-hydroxysteroids-4alpha-carboxylate. Involved in the regulation of inflorescence internodes and leaves growth, probably by affecting auxin transporter activity possibly by altering sterol composition in the membranes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43050}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Methylsterol monooxygenase 1-1
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 2-2
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-3
- Reticulon-like protein B21
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Ergosterol biosynthetic protein 28
- Reticulon-like protein B12
Sequence:
MSPAATETERWCVVTGGRGFAARHLVEMLVRYEMFCVRIADLAPAIMLDPQEGNGVLDEGLRSGRVQYISADLRDKSQVVKAFQGAEVVFHMAAPDSSINNHQLQYSVNVQGTQNVIDACVDVGVKRLIYTSSPSVVFDGVHGILNGTESMAYPIKHNDSYSATKAEGEELIMKANGRNGLLTCCIRPSSIFGPGDRLLVPSLVAAARAGKSKFIIGDGNNLYDFTYVENVAHAHVCAERALASGGDVSTKAAGQAYFITNMEPIKFWEFMSQLLDGLGYERPSIKIPAFIMMPIAHLVELTYKVLGPYGMTVPQLTPSRVRLLSCSRTFDSTKAKDRLGYAPVVPLQEGIRRTIDSFSHLTAGSQSKREGPSKASRILGGGKVADTLLWKDLKQTLIAIFILISIYYNFVATGSTVVTALSKALLVASVFLFLHGILPEKIFGYTVEKIPASQFHLSKDSSHDLSLSVISSWNTTVKALRSLCQGNDWSFFFKVVFVLLALSLAGAISLHSIFVIGLPIAFLAFLVYEKKEQEIDSIVVSFKSFACKHKSDVYEKLFGSKKHD
Protein: Meprin A subunit beta (EC 3.4.24.63) (Endopeptidase-2) (Meprin B) (P28826)
Organism: Rattus norvegicus (Rat)
Function: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16820}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q16820}. Secreted {ECO:0000250|UniProtKB:Q16820}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000250|UniProtKB:Q16820}.
Interaction partners:
- Meprin A subunit alpha
- Xaa-Pro aminopeptidase 2
- Lysosomal Pro-X carboxypeptidase
- Neprilysin
- Angiotensin-converting enzyme 2
- Dipeptidyl peptidase 4
Sequence:
MDARHWPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINEDLGLDLFEGDIKLEASGRNSIIGDNYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEENYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYITIVWDRILSGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIITKISDFEDVIGQRMDFSDYDLLKLNQLYSCTSSLSFMDSCDFELENICGMIQSSQDSADWQRLSQVLSGPENDHSNMGQCKDSGFFMHFNTSTGNGGVTAMLESRVLYPKRGFQCVEFYLYNSGSGNGQLNVYTREYTAGHQDGVLTLQREIRDIPTGSWQLYYVTLQVTEKFRVVFEGVGGPGASSGGLSIDDINLSETRCPHHIWHIQNFTQLLGGQTTVYSPPFYSSKGYAFQINLDLTSPTNVGLYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPKMTDDNGSYLWDRPSKVGVEAFFPNGTQFSRGRGYGTSVFITQERLKSREFLKGDDVYILLTVEDISHLNSTAAVPGPVPTTSTVHNACSEVECQNGGICTLQEGRAECKCPAGEDWWYMGKRCEKRGSTKDTIVIAVSSTVTVFAVMLIITLISVYCTRRKYRKKASAKTAAMNLENQHAF
Protein: Pre-mRNA-splicing factor cwf21 (Complexed with cdc5 protein 21) (O14161)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor cwf2
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-splicing factor brr2
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor cwf22
Sequence:
MSYNGIGLPTPRGSGTNGYVMRNLSHVKKYDKNTNLQSNRNAKALEKRVQDPSISEHECRRQIESKLLLYREQLLEEVSSQHSTDAAASDSNTNFGTENPKPPKAIIKDEQSQSKTKSLDEADVEILVQKYREQLLKELQLQKSTEKGKNFESILQPQKRKETRGFHSKNDDDGRLEERDDLRSSVDDDYYDYPRYSERKSLNSKRHVDNYNENRRRHYDSYSSYDELERRRSSNESYSRRSELPRRDYNRHDERERYSYHRRRERSNSPSYTKNESIPVVDRDSSPEGGEIV
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 (Complex I-B12) (CI-B12) (NADH-ubiquinone oxidoreductase B12 subunit) (O43676)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
Sequence:
MAHEHGHEHGHHKMELPDYRQWKIEGTPLETIQKKLAAKGLRDPWGRNEAWRYMGGFAKSVSFSDVFFKGFKWGFAAFVVAVGAEYYLESLNKDKKHH
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q380Z0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- diphosphoinositol-polyphosphate diphosphatase
- TAP42-like protein
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MDTIDQFLETVGKGVCPRESEVMKLCNKARSILDGESNTHVIRAPCTIVGDIHAQFFDLIEMFRVGGDVPDVNYVFMGDYVDRGHHGVETFLLLLALKVKYTSRVALLRGNHESRQITQVYGFYDECLRKYGSVNVWRYCTDVFDLLPLVCVVEEKILCVHAGLSPMISTVSQMEAIERRCEVPHEGAMCDLLWSDPEEIEGWGLSPRGAGYLYGEDVVRTFLESNKLDLLCRSHQLVMEGYKVMFNDALVTVWSAPNYCYRCMNVASILELDEHLNKNFKLFEAAPDDARESSKPTVPDYFL
Protein: Increased rDNA silencing protein 4 (Q59SR6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity).
Interaction partners:
- phosphoinositide 5-phosphatase
Sequence:
MSGNSAANAAALAAFNGIGKKKKESTTKLNGTDNNTNHLGVIGSTSNQTKQHQQQQQQPQALRTPLPAHPSRKKSNKFSQLKRLNTAPAMASLQPALQIASPSISPTQPSAPASALDSDPDYFTLSPHTIPSKNEIAKSPQTPQDMIRNVRQSIELKAIPNNAQAKRLSVDYSPQEMLKNLRHSLHSRTKTSPMLTTSDKMGQTMLAEMRDRLENTRRIASNSVASLSLSPNLDFNKSTSDVSNLSHHYDVDTVSTDSFASFNSSINDRHLPHGISIDVTNHDSDEDEIDDREREEDHEPLDNGELKSTNNKVTVSSRLRRKPPPGEDFQMQLNDKSRDTISSGSYSLNPDEVYSFTDPDSYENLVSEVEVGETTRLFPQFPDANHYHQHSSKFRKKHQKVKPINGIYYRDMDSSNTSDTEESTSNLPSRSTTPLLGQPQQQVHFRSTMRKANTKKDKKSRFNELKPWKNHNDLNYLTDQEKKRYEGIWASNKGNYMSQVVIKLHGVNYETQKDPKEEAKMEHSRTAALLSAAAVEDSNYNGNNSLHNLDSVEINQLICGPVVKRIWKRSRLPSDTLEKIWNLIDFRRDGTLNKNEFLVGMWLVDQCLYGRKLPKKVDNVVWDSLGGIGVNVTVKKKK
Protein: Chaperone Ric-8A (Synembryn-A) (Q9NPQ8)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation.
Subcellular location: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q80ZG1}. Cytoplasm {ECO:0000250|UniProtKB:Q80ZG1}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide exchange factor MSS4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
Sequence:
MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRKRLAELLVSVLEQGLPPSHRVIWLQSVRILSRDRNCLDPFTSRQSLQALACYADISVSEGSVPESADMDVVLESLKCLCNLVLSSPVAQMLAAEARLVVKLTERVGLYRERSFPHDVQFFDLRLLFLLTALRTDVRQQLFQELKGVRLLTDTLELTLGVTPEGNPPPTLLPSQETERAMEILKVLFNITLDSIKGEVDEEDAALYRHLGTLLRHCVMIATAGDRTEEFHGHAVNLLGNLPLKCLDVLLTLEPHGDSTEFMGVNMDVIRALLIFLEKRLHKTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGEMLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVTMFDKLSRNRVIQPMGMSPRGHLTSLQDAMCETMEQQLSSDPDSDPD
Protein: Transmembrane emp24 domain-containing protein 9 (p24 family protein alpha-2) (p24alpha2) (Q5I0E7)
Organism: Rattus norvegicus (Rat)
Function: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein {ECO:0000269|PubMed:9472029}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein {ECO:0000269|PubMed:9472029}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein {ECO:0000269|PubMed:9472029}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway.
Interaction partners:
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 5
- Transmembrane emp24 domain-containing protein 3
- Transmembrane emp24 domain-containing protein 7
- Surfeit locus protein 1
- Transmembrane emp24 domain-containing protein 1
- Transmembrane p24 trafficking protein 6
- Vesicle-trafficking protein SEC22b
Sequence:
MAAVRGVRVVGTSPGLLLGRGMRAFLLLLCLAARGGALYFHIGETEKKCFIEEIPDETMVIGNYRTQLYDKQREEYQPATPGLGMFVEVKDPEDKVILARQYGSEGRFTFTSHTPGEHQICLHSNSTKFSLFAGGMLRVHLDIQVGEHANDYAEIAAKDKLSELQLRVRQLVEQVEQIQKEQNYQRWREERFRQTSESTNQRVLWWSILQTLILVAIGVWQMRHLKSFFEAKKLV
Protein: tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) (tRNA 2,2-dimethylguanosine-26 methyltransferase) (tRNA(guanine-26,N(2)-N(2)) methyltransferase) (tRNA(m(2,2)G26)dimethyltransferase) (Q9P804)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nuclear/cytoplasmic compartments. {ECO:0000250}.
Interaction partners:
- tRNA
- tRNA pseudouridine synthase 4
- tRNA
- tRNA
- Multisite-specific tRNA:
- Putative tRNA pseudouridine synthase C16C4.06c
- tRNA N
- ATP-dependent RNA helicase has1
- tRNA
- tRNA
Sequence:
MYEANMLRLSQRISNAVNHFSTAMMSGASASLTEGSAIIPFSNPNEVFYNPVQQFNRDLSVTAIRAWSETRSKKIVAKSHHRHQLLDQNSELSQENLTKCDTTHDFEKNCSEKTDSTSADNIAGFTILEALSATGLRSIRYAKELPNVKRILANDLLENAVKTIEKNVNYNNVSDIVIPNKGDANAVMHMNKFHYDVIDLDPYGSAAPFLDAAVQSVSKDGLLCITCTDSAVLAGNAYPEKCFSNYGGSSLRSNFCHEQAVRHLLYAIAASAAKYGRAIKPLLSLSIDFYFRVFVQIKAKPVLVKNLQSQSLLIYHCSGCGSFAEQPLGKTSPGRLPGTTKFSNASGPPVSANCEHCGYVHHVGGPLWGGPLHDAEFLKKMRAIAEDLDPEVYGTKRRILGMLALADEELPDVPFYFVLSQICSVLRSQSPPQNIFVSALLNAGYRVSGSHAKSNAIKTNAPWSFVWDVLRSWIKDHPVKLENISKTSAGAAILEKTPTAEVDFTFRPDSEFASKKEGYTRYQMNPTENWGPKSKPGKRTIAEVDSKS
Protein: CCND1 protein (Cyclin D1 (PRAD1: parathyroid adenomatosis 1)) (Cyclin D1, isoform CRA_c) (Q6FI00)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI
Protein: SLAIN motif-containing protein 2 (Q8CI08)
Organism: Mus musculus (Mouse)
Function: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with microtubules. Detected at the plus end of growing microtubules (By similarity). {ECO:0000250}.
Interaction partners:
- Cytoskeleton-associated protein 5
- Ubiquitin-like protein FUBI
Sequence:
MEDVNSNVNADQEVRKLQELVKKLEKQNEQLRSRSGAVQGAGLLGPGSPARVGVSTPSSGAASPRGFPLGLGAKASGGAGSGPRRTSSEDLRDATSLLAAGEGGLLDEVEPLRPDELERLSGWEEEEESWLYSSPKKKLTPMQKSVSPLVWCRQVLDYPSPDVECAKKSLIHKLDQTMSALKRQNLYNNPFNSVSYSNSYSPNASSPYSSGFNSPSSTPVRPPIVKQLILPGNSGNFKSSSDRNPPLSPQSSIDSELSASELDEDSIGSNYKLNDVTDVQILARMQEESLRQEYAASTSRRSSGSSCNSTRRGTFSDQELDAQSLDDEDDSLQHAVHPALNRFSPSPRNSPRPSPKQSPRNSPRSRSPARGIEYSRASPQPMISRLQQPRLSLQGHPTDLQTSNVKNEEKLRRSLPNLSRTSSTQVDSVKSSRSDSNFQVPNGGIPRMQPQASAIPSPGKFRSPAAPSPLALRQPVKAFSNHGSGSGSQETTQFTQTTSSPGPPVVQNSAPANPSSNINSATLTRPAGTTAMRSGLPRPSAPSAGGIPVPRSKLVQPVRRSLPAPKSYGSMKDDSWKDGCY
Protein: Proteasome regulatory non-ATP-ase subunit 7 (Q381I3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 26S proteasome regulatory subunit RPN3
- Proteasome regulatory non-ATP-ase subunit 9
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- 26S proteasome regulatory non-ATPase subunit
- Proteasome regulatory ATPase subunit 1
- Probable 26S proteasome regulatory subunit rpn-6.2
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
Sequence:
MPPQQPVGIMDNEEEFPVEEPPPMDPLIKLLHLRHTYTSQYVDEAVREEVKAAMLKIAHEHNMAPYLRFASEMFCWTVDEEQLRAMDAINATKLEELDARIKDAQENLGDVEVRDGLLARCHHFARIGDMEECLKFNNECSGKTLAAGSKLDLCFQRILLGLAFSDNEVAANGICSAHRLMKEGDWERRNRLKVYEGLFYVYIRDFKKGSELLLDSISTFAASELMDFNEFILVTVVASLPVLSRSQLKKCILDSPEVHSANIKNVFHLVTAIYECRYKEVFPTLDAVCQQLRGIVYLSQHVNYFFREVRVLVFKQFLDSYSSVTLKSMSNAFGIPSPVLDSMLGTLISNERIACKMDRVSDSITTYRGDTTNLDYHRIVKNGDLLLNRIQKLSRLAEV