wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome B5 isoform C (AtCb5-C) (Q9ZNV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases, including fatty acid desaturases.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22773744}; Single-pass membrane protein {ECO:0000269|PubMed:22773744}.
Interaction partners:
- NADH--cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase-like protein
- Very-long-chain aldehyde decarbonylase CER1
- Bax inhibitor 1
- Dihydroceramide fatty acyl 2-hydroxylase FAH1
- Probable lysophospholipase BODYGUARD 1
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Probable steroid-binding protein 3
- Very-long-chain aldehyde decarbonylase CER3
- Ergosterol biosynthetic protein 28
Sequence:
MANLISFHDVAKHKCKNDCWILIHGKVYDISTFMDEHPGGDNVLLAVTGKDASIDFEDVNHSKDAKELMKKYCIGDVDQSTVPVTQQYIPPWEKESTAAETTKEESGKKLLIYLIPLLILGVAFALRFYNNK
Protein: Small ribosomal subunit protein eS32 (60S ribosomal protein L41) (Large ribosomal subunit protein eL41) (P62948)
Organism: Rattus norvegicus (Rat)
Function: Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62947}.
Interaction partners:
Sequence:
MRAKWRKKRMRRLKRKRRKMRQRSK
Protein: Uncharacterized protein, isoform B (X2J927)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
Sequence:
MAPKKSTIVLNVEQFIHDIEERPAIWNRNFHCNKAFLEQMWDELSGAHKLPTDHMRHRLPKNEQDQSFYFSQQSEDCEKTVVEPDLTNGLIRRLQDSDEDYDEEEMEADGEASEATMEETMPTPPAAHQMNQVSTTPLATGALRAQEEAHQHALIKAGLLRAQLMELEKEAEDLSRKPPPPQQMTSPVAPSLQVLVEPPAAHCSPPPMVTTTSAQVQQPGSAAVLAPATTTSASSVSSNGAPMGGKRSVSPPPLYNKAHHPLATLAAAHLAAKDRNEDFGPTSAVGGNGDHLSFTQHSYANGLIPALKLKRPRLSEDSNFNGSSTMDTPLVPEDDDYHYLLSLHPYMKQLTAAQKLRIRTKIQKLIFKELYKEDLEESK
Protein: Carbonic anhydrase 4 (EC 4.2.1.1) (Carbonate dehydratase IV) (Carbonic anhydrase IV) (CA-IV) (P48284)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible hydration of carbon dioxide into bicarbonate and protons and thus is essential to maintaining intracellular and extracellular pH. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1737787}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1737787}.
Interaction partners:
Sequence:
MQLLLALLALAYVAPSTEDSHWCYEIQAKEPNSHCSGPEQWTGDCKKNQQSPINIVTSKTKLNPSLTPFTFVGYDQKKKWEVKNNQHSVEMSLGEDIYIFGGDLPTQYKAIQLHLHWSEESNKGSEHSIDGKHFAMEMHVVHKKMTTGDKVQDSDSKDKIAVLAFMVEVGNEVNEGFQPLVEALSRLSKPFTNSTVSESCLQDMLPEKKKLSAYFRYQGSLTTPGCDETVIWTVFEEPIKIHKDQFLEFSKKLYYDQEQKLNMKDNVRPLQPLGNRQVFRSHASGRLLSLPLPTLLVPTLTCLVASFLH
Protein: V-type proton ATPase subunit G3 (V-ATPase subunit G3) (Vacuolar H(+)-ATPase subunit G isoform 3) (Vacuolar proton pump subunit G3) (Q9SZH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit c''2
- V-type proton ATPase subunit c''1
Sequence:
MDSLRGQGGIQMLLTAEQEAGRIVSAARTAKLARMKQAKDEAEKEMEEYRSRLEEEYQTQVSGTDQEADAKRLDDETDVRITNLKESSSKVSKDIVKMLIKYVTTTAA
Protein: DNA-directed RNA polymerase I subunit RPA49 (RNA polymerase I subunit A49) (DNA-directed RNA polymerase I subunit E) (RNA polymerase I-associated factor 1) (RNA polymerase I-associated factor 53) (Q8K202)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:8641287, ECO:0000269|PubMed:9254723}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- RNA polymerase I-specific transcription initiation factor RRN3
Sequence:
MATLESPGMDDQAGDTETEALQSARWLYCGEPDDRQKAVLVQFSNGKLQNPGDMRFTLYNSTDLVNPRQRSHRIVAAETDRLSYVGNNFGTGALKCNALCRHFVGILNKTSGQMEVYDAELFNMQPLFAGMGTEVIKLGGQHLYLLAFCQPSKNLAEAGDLLLSRHRQGHCIAVLLDDDAIEREPPLENQNKTFRDKLDSCIEAFGSTKQKRSLNSRRMNKVGSESLNLSVAKAAESIIDTKGVNALVSDAMQDDLQDGVLYLPPCYADAAKPEDVYRFEDILSPAEYDALESPSEAFRKVTSEDILKMIEENSHCSYVIEMLKSLPIDEVHRNRQARSIWFLDALIRFRAQKVIKGKRALGPGIPHIINTKLLKQFTCLTYNNGRLQNLISSSMRAKITSYAIILALHINNFQVDLTALQKDLKLSEKRMIEIAKAMRLKISKQKVSLADGREESHRLGTLSVPLPPAQNSDRQSKRRKMN
Protein: Probable conserved membrane protein (O06311)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable conserved lipoprotein LpqU
- Probable conserved transmembrane protein
- Fluoride-specific ion channel FluC 1
- Uncharacterized protein Rv3630
- Possible lipoprotein LpqQ
- Possible conserved transmembrane protein
- Probable transport accessory protein MmpS1
- Conserved protein
Sequence:
MSNAPEPDRSAGESGSEPAGERSADPGEERTESYPLVPHDAETETVVITTSDNDAAVTQPEAQRERRFTAPGFDAKETQVIVTAHEAATEVFQTNQAPTTPPRMPTGMPPKTAVPQSIPPRTEATSVRQRTWGWALAVVVIVLALAAIAILGTVLLTRGKHSKMSQEDQVRQAIQSLDIAIQTGDLTALRSLTCGSTRDGYVDYDERDWAETYRRVSAAKQYPVIASIDQVVVNGAHAEANVTTFMAFDPQVRSTRSLDLQFRDDQWKICQSSSN
Protein: Protein HEADING DATE 3B (ELF3-like protein 1) (OsELF3-1) (OsELF3) (Protein HEADING DATE 17) (Q9SNQ6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the regulation of flowering time under short day (SD) and long day (LD) conditions. Functions as floral promoter by negatively regulating GHD7, a repressor of the photoperiodic control of flowering. Acts as floral activator in the LD photoperiodic pathway. Involved in blue light-induced activation of EHD1 expression to promote flowering under SD conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:22888152}.
Interaction partners:
- Phytochrome B
- Protein GIGANTEA
- Cryptochrome 2
- Os02g0573200 protein
- E3 ubiquitin-protein ligase
- ELF3-like protein 2
- Os01g0566050 protein
- Os04g0589400 protein
- Os04g0452100 protein
- Os01g0314700 protein
Sequence:
MATRGGGGGGGGKEAKGKVMGPLFPRLHVNDAAKGGGPRAPPRNKMALYEQFTVPSHRFSGGGGGGGVGGSPAHSTSAASQSQSQSQVYGRDSSLFQPFNVPSNRPGHSTEKINSDKINKKISGSRKELGMLSSQTKGMDIYASRSTAEAPQRRAENTIKSSSGKRLADDDEFMVPSVFNSRFPQYSTQENAGVQDQSTPLVAANPHKSPSTVSKSSTKCYNTVSKKLERIHVSDVKSRTPLKDKEMEAAQTSKNVEVEKSSSFHASKDMFESRHAKVYPKMDKTGIINDSDEPHGGNSGHQATSRNGGSMKFQNPPMRRNEISSNPSSENTDRHYNLPQGGIEETGTKRKRLLEQHDAEKSDDVSRLLEQHDAENIDDVSDSSVECITGWEISPDKIVGAIGTKHFWKARRAIMNQQRVFAVQVFELHKLVKVQKLIAASPHVLIESDPCLGNALLGSKNKLVEENLKAQPLLVATIDDVEPSLQQPEVSKENTEDSPPSPHDTGLGSGQRDQAATNGVSKSNRRATPVASDNKQNNWGVQLQPPQNQWLVPVMSPLEGLVYKPYSGPCPPAGSILAPFYANCTPLSLPSTAGDFMNSAYGVPMPHQPQHMGAPGPPSMPMNYFPPFSIPVMNPTAPAPVVEQGRHPSMPQPYGNFEQQSWISCNMSHPSGIWRFHASRDSEAQASSASSPFDRFQCSGSGPVSAFPTVSAQNNQPQPSYSSRDNQTNVIKVVPHNSRTASESAARIFRSIQMERQRDD
Protein: MRGB2 G protein-coupled receptor (Q7TN47)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSCGIMSCTMIFLSLIIAIVVLVGNAIVIWLLGFQMCRNAFSIYILNLAGADFLFIGFQIGYCFYIIFDIYTIPIKLPLFFIVMLNFAYLCGLSILSAVSIERCLCVMRPFWYRCQLPRHTSAVICTMLWVLSLVLSLSEGKECGFLPGTNISDWCKTIDLIITSWLIVLFVVLLVSSLALVITIFCGLYRIPVTRLYVVIVFTVLFFLLFGLPYGIYLFLLVWAETFYYVFPCGFLPVTIFLSCINTCANPIIYFLVGSVRHHRFQRKSLKLLLQQARQDTPETEEYVEMGSLGRSREVNSLQGTESCFDQA
Protein: Heat shock factor A2b (A0A024DB95)
Organism: Triticum aestivum (Wheat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Heat shock protein 90
- Uncharacterized protein
- Heat shock factor binding protein
- Heat shock factor binding protein
- Heat shock factor binding protein
- Heat shock factor binding protein
- HSP70
- Endoplasmin homolog
- Endoplasmin homolog
- Endoplasmin homolog
Sequence:
MDPVPGLVKEEEEEGAHGRGDSPAVGAAPRPMEGLHDAGPPPFLTKTYDMVDDPNTDSIMSWSAGNNSFVVWDPHAFATVLLPRHFKHSNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQRHLLKNIRRRKPPAHTASNQQSLGSYLEVGHFGYDAEIDRLKRDKQLLMAEVVKLRQEQQNTKARLKAMEDRLRGTEQKQQQMTSFMARILRNPEFLKQLIAKNGMRKELHDAISKKRRRRIDGGPEAYAVGASSSSLEQELPVVFDSHGSVELLAEGSVPVELLADGIPPDLEGSVELLADEIPPGLEGSVALLADGLEGSVELLVDGIPSDLDGSGIDSNGVTEPQDYGLGTCEAQQNRALGLFHDNFWEELLNKGLSVENDEPVNVDGMDVLSEKMGYLIPNSPTLST
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (A0A8I6G914)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDSLAGLVLCGVSLLLYGLVEGAMDLILINSLPLVSDAETSLTCIASGWHPHEPITIGRDFEALMNQHQDPLEVTQDVTREWAKKVVWKREKASKINGAYFCEGRVRGQAIRIRTMKMRQQASFLPATLTMTVDRGDNVNISFKKVLIKEEDAVIYKNGCEAQKWGPDCNRPCTTCKNNGVCHEDTGECICPPGFMGRTCEKACEPHTFGRTCKERCSGSEGCKSYVFCLPDPYGCSCATGWRGLQCNEACPYGHYGPDCKLRCHCTNEEMCDRFQGCLCSQGWQGLQCEKEGRPRMTPQIEDLPDHIEVNSGKFNPICKASGWPLPTSEEMTLVKPDGTVLQPNDFNHTDHFSVAIFTVNRILPPDSGVWVCSVNTVAGMVEKPFNISVKVLPEPLHAPNVIDTGHNFAIINISSEPYFGDGPIKSKKLFYKPVNQAWKYIQVMNEIVTLNYLEPRTDYELCVQLVRPGEGGEGHPGPVRRFTTASIGLPPPRGLSLLPKSQTALNLTWQPIFTSSEDEFYVEVERWSQQTRSDQQNIKVPGNLTSVLLNNLLPREQYSVRARVNTKAQGEWSEELRAWTLSDILPPQPENIKITNITDYTALVSWTIVDGYSISSIIIRYKVQGKNEDQHIDVKIKNATITQYQLKGLEPETTYHVDIFAENNIGSSNPAFSQEIRTLPAPKDLGGGKMLLIAILGSAGMTCITVLLAFLIMLQLKRANVQRRMAQAFQNVREEPAVQFNSGTLALNRKAKNNPDPTIYPVLDWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYIAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVNTTLYEKFTYAGIDCSAEEAA
Protein: Kinesin-like protein KIF15-B (Kinesin-like protein 2-B) (Xklp2-B) (Q498L9)
Organism: Xenopus laevis (African clawed frog)
Function: Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. Required for centrosome separation and maintenance of spindle bipolarity during mitosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Localizes during metaphase on spindle microtubules, with a strong enrichment at spindle poles. Localizes to the minus ends of spindle pole and aster microtubules in a dynein- and dynactin-dependent manner. Detected diffusively in the cytoplasm. Localized at the centrosome during the interphase and throughout mitosis (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MPPGTKGDPSNVTQPLPCLPSAEEDAIKVFVRIRPPVEGTLTGVDGEQGSCLTALSSTTIRLHSKPEPKMFTFDHVANVDTTQESVFSSVAKNIVESCMNGYNGTIFAYGQTGSGKTFTMLGPSESDNFTHNLRGVIPRSFEYLFFLINREKEKAGDGKSFLCKCSFIEIYNEQIFDLLDSASAGLFLREHIKKGVFVVGAVEQVVTSAAEAYQVLSMGWRNRRVASTSMNRESSRSHAVFTVTIESMEKTNDIVNIRSSQLNLVDLAGSERQKDTQTEGVRLKEAGSINRSLSCLGQVITALVDVANGRQRHICYRDSKLTFLLRDSLGGNAKTFIIANVHPGSKCFGETLSTLQFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKKLKEQLSQLLSGQMPGDISVARAPSVGDNMDYMNTFIEAMMLLERSDSEKKALLQKVIQLEDLCNKKEKFIQSNKMIVKFREDHIVRLEKAHREGQISLSNNEQDNFIAELKEEIRTLKEQVEHHPRVAKYALENHSLREENKRIGSLQSVKRAQEVSAQMMAELEKAFLEASVSEKDRQVAPMHSTPIQLDNSSLMSAARMRERMLQLESELATSKQEYEEFKELTKKKQVEQESELQSLMKSNQHLENILDAIKENKRHEVSQLNRMHAETIKNMTTPTKAYNLRSRLVPRLSLDGISNGLTDTPKSGDVMDDIINEPIPPEMSEQAYEAIAEELRIVQEQVTALQVKLDEEESKNIKLEQQVNKLELCSTQIQELFNSERSNWNKEQQAFIAQIKSLEKQQQDNKNQEDVLKSEVHDLRVVLQSADRELSAVKGEYSLFREKQEKELSQLSARHMAVQLQLDNFRLEHETLLEEKRSLQDAFDNLEEVMKFETDQLKQELSDSKHENETLRAELSNLLELLETEKERRQKLTSQLEEDKESKTKELLQVVDENMHLRKQCSELVTKCEHQVTELQRLEHSLTSSKEMIADLEKKNTADKEVVVDLMNQIQVHRTTIIHKTESIDLLTRELEDINSKYSIVLLAKEECKTVNEEQEKQIEELRESLERKQSADNIEKELLCDDLAHATEELGKLTEAFNKQETMLHACEKELVEKEQLISELTNKVKLMTDLEITKTEQEKIKPSHSNSNSPVVLAQTPRTPVGNPYESEFANLQNRNTNLAVLISELNEERTLKNEEIIKLKMQLCETENMHLEIQNLQGICKELKSQLENCKKGMKDGNEQKPSDMQDLKREIEKEVSERMEKGKATEHILKLQAELEETRNLLCAKDHSLNELNNEMERTRSLEAKAFTEKEQIRSVLEAKYEETEKLSQELDMLRKQVSFLAEENGKILGHQNPNQKIQYLVKLKKENDKLLEEAEKLRIENLFLKETKKCEHCD
Protein: HLA class I histocompatibility antigen, alpha chain F (CDA12) (HLA F antigen) (Leukocyte antigen F) (MHC class I antigen F) (P30511)
Organism: Homo sapiens (Human)
Function: Non-classical major histocompatibility class Ib molecule postulated to play a role in immune surveillance, immune tolerance and inflammation. Functions in two forms, as a heterotrimeric complex with B2M/beta-2 microglobulin and a peptide (peptide-bound HLA-F-B2M) and as an open conformer (OC) devoid of peptide and B2M (peptide-free OC). In complex with B2M, presents non-canonical self-peptides carrying post-translational modifications, particularly phosphorylated self-peptides. Peptide-bound HLA-F-B2M acts as a ligand for LILRB1 inhibitory receptor, a major player in maternal-fetal tolerance. Peptide-free OC acts as a ligand for KIR3DS1 and KIR3DL2 receptors. Upon interaction with activating KIR3DS1 receptor on NK cells, triggers NK cell degranulation and anti-viral cytokine production. Through interaction with KIR3DL2 receptor, inhibits NK and T cell effector functions. May interact with other MHC class I OCs to cross-present exogenous viral, tumor or minor histompatibility antigens to cytotoxic CD8+ T cells, triggering effector and memory responses. May play a role in inflammatory responses in the peripheral nervous system. Through interaction with KIR3DL2, may protect motor neurons from astrocyte-induced toxicity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16709803, ECO:0000269|PubMed:23851683, ECO:0000305|PubMed:27455421}; Single-pass type I membrane protein. Early endosome membrane {ECO:0000269|PubMed:23851683}. Lysosome membrane {ECO:0000269|PubMed:23851683}. Note=For cross-presentation transits from the cell surface through endosomal pathway to lysosomes, where the peptide is generated from internalized exogenous antigen. {ECO:0000269|PubMed:23851683}.
Interaction partners:
- Leukocyte immunoglobulin-like receptor subfamily B member 1
- Beta-2-microglobulin
- HLA class I histocompatibility antigen, alpha chain E
- HLA class I histocompatibility antigen, A alpha chain
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Killer cell immunoglobulin-like receptor 3DL2
- HLA class I histocompatibility antigen, C alpha chain
- HLA class I histocompatibility antigen, B alpha chain
- HLA class I histocompatibility antigen, alpha chain G
- HLA class II histocompatibility antigen, DM alpha chain
Sequence:
MAPRSLLLLLSGALALTDTWAGSHSLRYFSTAVSRPGRGEPRYIAVEYVDDTQFLRFDSDAAIPRMEPREPWVEQEGPQYWEWTTGYAKANAQTDRVALRNLLRRYNQSEAGSHTLQGMNGCDMGPDGRLLRGYHQHAYDGKDYISLNEDLRSWTAADTVAQITQRFYEAEEYAEEFRTYLEGECLELLRRYLENGKETLQRADPPKAHVAHHPISDHEATLRCWALGFYPAEITLTWQRDGEEQTQDTELVETRPAGDGTFQKWAAVVVPPGEEQRYTCHVQHEGLPQPLILRWEQSPQPTIPIVGIVAGLVVLGAVVTGAVVAAVMWRKKSSDRNRGSYSQAAV
Protein: Calbindin-32 (P41044)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH08630p
Sequence:
MDSAAAAAAKRVQIEKAHNFMRQYRDPESRELKKLSANQFMDVWAHYDKDGNGYIEGTELDGFLREFVSSANATDISPEAVTDTMLEELKSCFMEAYDDNQDGKIDIRELAQLLPMEENFLLLFRFDNPLESSVEFMKIWREYDTDNSGYIEADELKNFLRDLLKEAKKINDVSEDKLIEYTDTMLQVFDANKDGRLQLSEMAKLLPVKENFLCRQVFKGATKLTKEDIEKVFSLYDRDNSGTIENEELKGFLKDLLELVKKDDYDAQDLAAFEETIMRGVGTDKHGKISRKELTMILLTLAKISPDDEE
Protein: Cytosolic Fe-S cluster assembly factor Nubp2 homolog (Q9VPD2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03039}.
Interaction partners:
- GH14121p
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Iron-sulfur cluster assembly enzyme IscU
- Choline/ethanolamine transporter FLVCR1
- GH01724p
- Cysteine desulfurase, mitochondrial
- Probable cytosolic iron-sulfur protein assembly protein Ciao1
- Anamorsin homolog
- Cytosolic Fe-S cluster assembly factor Nubp1 homolog
- Probable cytosolic Fe-S cluster assembly factor CG17683
Sequence:
MLDKVKNVIVVLSGKGGVGKSTVSTQLSLALRKNGFKVGLLDIDLCGPSVPYLLGLEGRDIFQCDDGWVPVYTDESQTLAVMSIGFLLKNREDPVIWRGPKKTMMIRQFLTDVRWDELDYLIIDTPPGTSDEHITVMECLKEVGCHGAIIVTTPQEVALDDVRKEITFCKKTGINILGIVENMSGFVCPHCTSCTNIFSSNGGVSLATYAQVPHLGTLPIDPRVGILAGTTTSVLDELPDSTTAEVLTHIVEKLKTMLVS
Protein: Uncharacterized protein (Q387Y0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYPKNKPLPPEAAGRAAELSNRNPPPVIVESNSSSRTRAFASSVPPAPPMPVAPCGEINGTSLIRHTPGNDLLHQHASFNQTVPGNIMNAQRLSPVGSGSFQMSNNSLSSSVPHGPGVMGHPIKPMFPPSVRPPPPYAAVSPNSSGIIEERMLDTFGGTRSSHSMTWGRLNQTPPPPPPPPPPPFMAELPPYPEAAAAAVPPPHRWAHGNDTLGGPKVKINGESAAHTSQSDKNGEVPSTEVEGRKSESDVCGEGSELLLQQYRSDVRFLTKLVVALLERMHPANSCISGTKTEDVQKDGSDNSTAEDSSAGEGTSSALKKQLRELENVITQLQAREEAAMSPNTQRLFDRVLSIPQLTALASRVGGASGGALMPHRSVSSFGGSDDVLSLRVSSEVKAYMRAVDFETTRPLMLNVVVATDSAASSRTPSRTTSLQGVSAPCAKEETTTPL
Protein: Cystathionine beta-lyase (CBL) (EC 4.4.1.13) (Beta-cystathionase) (Cysteine lyase) (Cysteine-S-conjugate beta-lyase) (O94350)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Probable cystathionine gamma-synthase
- Cysteine synthase 1
- Probable 3-mercaptopyruvate sulfurtransferase
- Adenosylhomocysteinase
- Cysteine synthase 2
- Homoserine dehydrogenase
- Homoserine kinase
- Aspartate aminotransferase, cytoplasmic
- Homocysteine synthase
Sequence:
MPSDCKYSVDTELVHVEGNEDQYHASSVPIYQSATFKQPCLEHMGKFDYTRSGNPTRSVLQVHLAKLMKAKHAFVTSNGMSALDMILRCCKSNSHVVAGHDLYGGSDRLLSFNQRQYGFKVDNVDTSDLAAFEAALRPDTNLVLIESPTNPRISICDIRAIVKITRSKAKDALLVMDNTMLSPVLCNPLDFGYDIVYESATKYLSGHHDLMGGVIATKSDEIAKSVFFNINAMGAAMAPFECFLLLRGIKTMGLRVERAQQNAIEIAKFLKSKGLQVNFPGLDPDAKSTAIFYSFARGPGAVMSVFTGDVEVSKTIVNTTKLFEISVSFGAVNSLISMPAYMSHASIKKEVRDARGLSEDLIRICVGIENVDDLKADLENALAQANFKQN
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (Sm-E) (SmE) (P62304)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:23246290, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000305}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm8
- Pre-mRNA-processing factor 17
- 116 kDa U5 small nuclear ribonucleoprotein component
- Splicing factor 3B subunit 1
- U6 snRNA-associated Sm-like protein LSm2
- Splicing factor 3A subunit 3
- Pre-mRNA-processing factor 19
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm6
Sequence:
MAYRGQGQKVQKVMVQPINLIFRYLQNRSRIQVWLYEQVNMRIEGCIIGFDEYMNLVLDDAEEIHSKTKSRKQLGRIMLKGDNITLLQSVSN
Protein: Pleckstrin homology domain-containing family H member 3 (PH domain-containing family H member 3) (Q7Z736)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLPGGLWWLLCCRRGFTLLHRDYGDGELSGDGDEDEDEETFELRTPSPAGGGRGPLEVTLTQPVRSGPVSNRLQSWEETWSLIPEKGLPEDDPDIVVKGWLYREPRGGGARPWLPPRRAWFVLTRDSLDQFSSSGKGARRLGSLVLTSLCSVTGPERRRKETGLWSVTVSGRKHSVRLCSPRQAEAERWGVALREVIASKAPLETPTQLLLRDIQESCGDPEAVALIYLRNPILRHTSGALYAPLLPLPYGVSAPGPGYAPLREEAVRLFLALQALEGARRPGPLMQGVLQTCRDLPALRDELFLQLAKQTSGPAGPPGLPATQDPAALRYWQLLTCMSCTFRPGGAVRGHLLGHLERTEQALPDSELAEYARFIRKALGRTRGRELVPSLAEISALSQRQELLCTVHCPGAGACAVAIDSHTTAGEVARELVGRLGLARSRNAFALYEQRGAQERALAGGTLVADVLTRFENLAAEEAGLEDSPDSGWRLCLRLHGPLHPEGLSPDGHELPFLFEQAHALLLRGRPPPPDDTLRALAALRLQSLQRDFSPRVPLPRLDRLLPPPAPPREDPPRPTPRPPPSAALLAGALWSPGLAKRRAERARRGGAGRTAGSIAREGGGGAGTAAAVLGGWKRLRGMGRAEAMAAYLALAAQCPGFGAARYDVLELSTEPGRGAPQKLCLGLGAKAMSLSRPGETEPIHSVSYGHVAACQLMGPHTLALRVGESQLLLQSPQVEEIMQLVNAYLANPSPERPCSSSSPPCQDLPDTSPPSQRPGLDEPQGQSGCLGQLQD
Protein: Phosphoserine aminotransferase (EC 2.6.1.52) (Phosphohydroxythreonine aminotransferase) (PSAT) (P23721)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- D-3-phosphoglycerate dehydrogenase
- Phosphoserine phosphatase
- Erythronate-4-phosphate dehydrogenase
- 4-hydroxythreonine-4-phosphate dehydrogenase
- Threonine synthase
- 3-phosphoshikimate 1-carboxyvinyltransferase
- Cysteine synthase A
- Serine hydroxymethyltransferase
- Bifunctional chorismate mutase/prephenate dehydratase
- T-protein
Sequence:
MAQIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDETPDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGPAGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPPTFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKANRSRMNVPFQLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKALTDFMVEFERRHG
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Q54QQ0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein purH
- AMP deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Bifunctional purine biosynthetic protein purD
- Cytosolic purine 5'-nucleotidase
- Adenylosuccinate lyase
- Glutamine amidotransferase domain-containing protein
Sequence:
MEKINKILQGTNSEYKSEWFVDGFDCFELFQQRHGYTYDDLIMLPGHINFSADDVSLKTKLTKNISLNAPLVSSPMDTVTEHLMAINMALLGGIGIIHYNNTVEEQVVEVKKVKRFKNGFITDPIVLSPTHKLSDVDMIKQKYGFSGIPITDTGRIGGKLVGIVTSRDTDFIKDRSTTLSEVMTTDLITGQQNCTLEEANSILKSCKKGKLPIVNDKGELVALASRDDLVKNRDFPMATKDHENKKLLVGAALGTRETDKERLAALSDAGVDVVILDSSQGDSTYQREMIRFIKRNYPKIDVIGGNVVTTSQCESLIQAGVDGLRVGMGVGSICTTQEVMACGRPQATAVFKCALYSSQYNVPIIADGGIRTIGHIIKGLSLGASSVMMGSMLAGTEEAPGDYFYKDGMRLKKYRGMGSLEAMVKGGDQRYFSETDKIKVAQGVSGSVVDKGSVKKFVPYLIQGIKHGLQDLGCNSVTNLRESVYGGKVRFEVRTAAAQVEGSVHSLFSYEKHFI