wanglab/gogpt-training-data huggingface dataset:
Protein: Protein kinase doc (EC 2.7.11.1) (Death on curing protein) (Toxin doc) (Q06259)
Organism: Escherichia phage P1 (Bacteriophage P1)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Phosphorylates EF-Tu on 'Thr-383' in vitro; can use ATP or GTP. Also dephosphorylates in the presence of ADP or GDP. Can only phosphorylate before the ternary aminoacyl-tRNA EF-Tu-GTP complex is formed; interaction with cognate antitoxin phd prevents phosphorylation and dephosphorylation of EF-Tu. Overexpression results in inhibition of growth in liquid cultures and a decrease in colony formation by inhibiting translation, stabilizing mRNA and polysomes; these effects are overcome by concomitant expression of antitoxin phd. Binds 70S ribosomes and the 30S ribosomal subunits, the binding site is the same as for the antibiotic hygromycin B. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid; doc and phd proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss. Overexpression of doc can induce the mRNA interferase activity of host RelE in vivo.
Interaction partners:
Sequence:
MRHISPEELIALHDANISRYGGLPGMSDPGRAEAIIGRVQARVAYEEITDLFEVSATYLVATARGHIFNDANKRTALNSALLFLRRNGVQVFDSPELADLTVGAATGEISVSSVADTLRRLYGSAE
Protein: Bomanin Short 2 (Bomanin-2) (Immune-induced peptide 2) (DIM-2) (O77150)
Organism: Drosophila melanogaster (Fruit fly)
Function: Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance to bacterial and fungal infections.
Subcellular location: Secreted {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
Interaction partners:
- Daisho1
- Bomanin Short 3
- Bomanin Short 1
- Bomanin Bicipital 1
- Bomanin Tailed 2
- Bomanin bicipital 2, isoform A
- Dorsal-related immunity factor Dif
- GNBP-like 3
- Embryonic polarity protein dorsal
- Bomanin Short 5
Sequence:
MKFFSVVTVFVFGLLALANAVPLSPDPGNVVINGDCKYCNVHGGK
Protein: Galactose-1-phosphate uridylyltransferase (EC 2.7.7.12) (A0A1D8PCM2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Galactokinase
- Bifunctional protein GAL10
- UTP--glucose-1-phosphate uridylyltransferase
- Gal102p
Sequence:
MSLDHLLNPLTSTPTYIKMTQEFDFTNHSHRRLNLLTNKFVLCSPHRAKRPWQGAKEEIKKSALPEYDPKCYLCPGNIRATGDMNPKYDATYIFPNDYPAVRLDQPEYKEDEQDKQNTLKSRLLQTQGVRGKCFVICFSPKHNLTLPLMKDEEINNVVNAWQDLYGNLLQESNQGIAPYKYLQIFENKGAAMGCSNPHPHGQAWCLDVIPTEVKDELDNMSEYYKKYNSHLLGDYVELELQEKKRIVAENDSFIVVVPYWALWPFETLLISKTHLKSIQEFNDKQKLDLAAILKILTTKYDNLFNTSFPYSMGIHQAPFKCTHEQNECSWFHMHFYPPLLRSATVKKFCVGFEMLGEPQRDLTSEQAAARLQELNGDVHYMNKPQA
Protein: At2g28120/F24D13.9 (Major facilitator superfamily protein) (Nodulin-like protein) (Q9ZUV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 5
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 7
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 6
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 3
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 4
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- Josephin protein-like protein
- WAT1-related protein At4g08300
- Ubiquitin carboxyl-terminal hydrolase 27
Sequence:
MGNDETVRFLIHFFNGRWFMVFASFLIMACAGATYLFGTYSKDIKSTLGYDQTTLNLLGFFKDLGANVGVLSGLIAEVTPTWFVLTIGSAMNFVGYFMIWLTVTGKVAKPKVWQMCLYICIGANSQNFANTGALVTCVKNFPESRGVMLGLLKGYVGLSGAIFTQLYFAIYGHDSKSLILLIAWLPAAVSLVFVYLIREKKVVRQRNELSVFYQFLYISIFLALFLMAMNIAEKQVHFSKAAYAASATICCALLFVPLTVSVKQELEVWNMMKLPIEEPSEVKVEKPKKELDLDQDKAAKVNGEEKETKSCFSTVFSPPPRGEDYTILQALLSTDMIILFVATFCGLGSSLTAVDNLGQIGESLGYPNHTVSSFVSLVSIWNYFGRVFSGFVSEYLLAKYKLPRPLMMTLVLLLSCAGHLLIAFPVPGSVYIASILMGFSFGAQLPLLFAIISELFGLKYYSTLFNCGQLASPLGSYILNVRVTGMLYDKEALKQLTARGLTRKDVKDLTCLGSQCYKLPFLILAAVTFFGALVSLGLAIRTREFYKGDIYKKFRESPESESELVPDSRKAVEFVGK
Protein: Galactosidase beta 1 (E7EQ29)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTLPGSCGQVVGSPSAQDEASPLSEWRASYNSAGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVCSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV
Protein: NAD-dependent malic enzyme 2, mitochondrial (AtNAD-ME2) (NAD-malic enzyme 2) (EC 1.1.1.39) (Q8L7K9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of sugars and amino acids metabolisms during the night period.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:21841088}.
Interaction partners:
- Malate dehydrogenase 1, mitochondrial
- Malate dehydrogenase 1, cytoplasmic
- Pyruvate, phosphate dikinase 1, chloroplastic
- Malate dehydrogenase 2, cytoplasmic
- Malate synthase
- Malate dehydrogenase, chloroplastic
- Fumarate hydratase 1, mitochondrial
- Malate dehydrogenase 3, cytoplasmic
- Fumarate hydratase 2
- Malate dehydrogenase 1, peroxisomal
Sequence:
MMWKNIAGLSKAAAAARTHGSRRCFSTAIPGPCIVHKRGADILHDPWFNKDTGFPLTERDRLGIRGLLPPRVMTCVQQCDRFIESFRSLENNTKGEPENVVALAKWRMLNRLHDRNETLYYRVLIDNIKDFAPIIYTPTVGLVCQNYSGLYRRPRGMYFSAKDKGEMMSMIYNWPAPQVDMIVITDGSRILGLGDLGVQGIGIPIGKLDMYVAAAGINPQRVLPIMLDVGTNNEKLLQNDLYLGVRQPRLEGEEYLEIIDEFMEAAFTRWPKAVVQFEDFQAKWAFGTLERYRKKFCMFNDDVQGTAGVALAGLLGTVRAQGRPISDFVNQKIVVVGAGSAGLGVTKMAVQAVARMAGISESEATKNFYLIDKDGLVTTERTKLDPGAVLFAKNPAEIREGASIVEVVKKVRPHVLLGLSGVGGIFNEEVLKAMRESDSCKPAIFAMSNPTLNAECTAADAFKHAGGNIVFASGSPFENVELENGKVGHVNQANNMYLFPGIGLGTLLSGARIVTDGMLQAASECLASYMTDEEVQKGILYPSINNIRHITAEVGAAVLRAAVTDDIAEGHGDVGPKDLSHMSKEDTVNYITRNMWFPVYSPLVHEK
Protein: 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (CIP21) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7) (P54775)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P43686}. Nucleus {ECO:0000250|UniProtKB:P43686}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-3
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 11
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 13
Sequence:
MEEIGILVEKIQDEIPALSVSRPQTGLSFLGPEPEDLEDLYSRYKKLQQELEFLEVQEEYIKDEQKNLKKEFLHAQEEVKRIQSIPLVIGQFLEAVDQNTAIVGSTTGSNYYVRILSTIDRELLKPNASVALHKHSNALVDVLPPEADSSIMMLTSDQKPDVMYADIGGMDIQKQEVREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTAAFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQNVNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFSTITSKMNLSEEVDLEDYVARPDKISGADINSICQESGMLAVRENRYIVLAKDFEKAYKTVIKKDEQEHEFYK
Protein: F(1)-ATPase inhibitor IF(1), mitochondrial (ATPase inhibitory factor 1) (IF(1)) (IF1) (P01097)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a one-to-one complex with ATPase to inhibit the enzyme activity completely.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12809520}.
Interaction partners:
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 4
- F
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit delta, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
Sequence:
MLPRSALARSLQLQRGVAARFYSEGSTGTPRGSGSEDSFVKRERATEDFFVRQREKEQLRHLKEQLEKQRKKIDSLENKIDSMTK
Protein: Nedd8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (Ubiquitin-activating enzyme 3 homolog) (Q9V6U8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the dimeric Uba3-APP-BP1 E1 enzyme. E1 activates Nedd8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a Nedd8-Uba3 thioester and free AMP. E1 finally transfers Nedd8 to the catalytic cysteine of UbcE2M. Required for Cul1 and Cul3 neddylation. Negatively regulates full-length ci stability and hedgehog signaling.
Interaction partners:
- Ubiquitin-like protein NEDD8
- Nedd8-activating enzyme E1 regulatory subunit
- Nedd8-conjugating enzyme UbcE2M
- Cullin homolog 1
- Deneddylase 1, isoform C
- Cullin 3, isoform F
- DCN1-like protein 1
- COP9 signalosome complex subunit 5
- E1 ubiquitin-activating enzyme
- Cullin-5
Sequence:
MSVHSPNPGLILQSKRFNGLRNILEREGPFCKDGFAASSENLEFLQTKCQVLIIGAGGLGCELLKDLALMGFGNLHVIDMDTIELSNLNRQFLFRRTDIGASKAECAARFINARVPTCRVTPHFKKIQDFDESFYQQFHLVVCGLDSIVARRWINGMLLSMLRYEEDGTIDTSSIVPMIDGGTEGFKGNARVILPGFTACIECTLDLFPPQVNYPLCTIANTPRLPEHCIEYVKIIQWEKQNPFGVPLDGDDPQHIGWIYERALERSNEFNITGVTYRLVQGVVKHIIPAVASTNAAIAAACALEVFKLATSCYDSMANYLNFNDLDGIYTYTYEAEKSENCLACSNTPQPLPIEDPNTTTLEDVIKLLCDSPRFQLKSPALTTVMKDGKRRTLYMSGVKSIEEATRKNLTQSLGELGLHDGQQLTVTDATSPSAMTLQLKYQSNEVEMV
Protein: Nucleolar protein 13 (P53883)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11452019, ECO:0000269|PubMed:14562095}. Note=Also found in nucleoplasm.
Interaction partners:
- Nucleolar protein 58
- Ribosome assembly factor MRT4
- Ribosome biogenesis protein 15
- Ribosome biogenesis protein RPF2
- Nucleolar protein 4
- Nucleolar complex protein 2
- 25S rRNA
- Pumilio homology domain family member 6
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein ENP2
Sequence:
MSETELSKEDAVTKKDNEEQVKKALLDPTKKRKAEDEIEIDLKSSIPLSKKQKRLLRRGKVTLEELNAKYNIDPKSIEEYKEDAEKKKSGASEKDAQGEESTINTPTGDESGEVVKKKKKDENKYGVWIGNLSFDTTKDDLVRFFIAKTKDNEDEKSRVTEQDITRLSMPRVAAKNSNAMKNKGFCYMFFKNVEQMKAVLELSESHLNGRNMLIKDSENYSGRPDKDDLVAMSKNPPSRILFVGNLSFDVTDDLLRKHFQHCGDIVKIRMATFEDSGKCKGFAFIDFKNEEGSTNALKDKSCRKIAGRPLRMEYGEDRSKRQVRKKVENVSRNNSSSFDISNNKGYDRAGQDNGSKPEYKRSNANRRPPVDSNNRTKSSVALATAQRGSAAIVPSQGKKVKFD
Protein: NAD(P)-binding domain-containing protein (Q57YG3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Electron transfer protein, putative
- Acyl carrier protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Reiske iron-sulfur protein, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MSLLVAGATGAIGRRVVFEALRREEFIRVAALTRSCPSEDVAALFGFSLEGINGNKTEKEASSLLTREQIARLHTVTFDWEDFCRFWEEQRENADKTHRKTQSSAEVRYRDIFSGHTYVAMCLGTTRRDAGSATKFKRCDYDYVVAFAEAVKRFSGSTLLNYAQVSAQLANKNSCFLYPQTKGRADASVEELQLSRLSIYRPGLLDRAEKTRAVEKIAKWFVRGLPVETCGKAIVIDFLHCSDVVATEAETSTSSVHCAGKKQELSQRSGVVCYFGNNEIIKEASALSTP
Protein: Cell death abnormality protein 12 (Q8STE5)
Organism: Caenorhabditis elegans
Function: Involved in programmed apoptosis and necrosis. Required for the cell corpse engulfment process. Has roles in the formation of actin halos and distal tip cell migration. Negatively regulates the unc-6/Netrin receptor unc-5 to control distal tip cell migration along the anterior-posterior axis of the body. Plays no role in amphid axon outgrowth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11703939}. Note=Punctate localization. {ECO:0000269|PubMed:11703939}.
Interaction partners:
- CED-5
- Cell death abnormality protein 2
- Cell death protein 6
- Ras-related protein ced-10
- ABC transporter ced-7
- Cell death abnormality protein 1
- Rac-like GTPase
- Bifunctional arginine demethylase and lysyl-hydroxylase psr-1
- LMBR1-like membrane protein
- Cell death protein 3
Sequence:
MAFHMPLKELQPVDTSLPEHVVKGAVVIDKEFTIWNHRAVIPSNALHTVFITINLLEQKLTDVVKMAARSMNLSEDDSYGLMADKPKRFITDDNLNSLGSGFILTLCASPDHYVKRITEILTEGNNISQMENAVKTLDEFSLDPALIEAFYRCSSLELLFSLIRDDRVCMSSTLLSTCLRALSSMLELAVGDFTWKSVPNDVVVSMASLVTGKAKREEANTLLAALQMLEQLVIGDDTTRDWILEEVPIETLIRHVEKSDERIALCALSLMNSMIRRCPDDEKRFELIKSLEVVPFRNAVHSSLLRGGGGVRNLNAIEQLVEVQRSLISAYETSPPTDAEVQKILDIESSEDVSEEIREMWKSQIGEHRCGRLAAISMVQFAEKSPQDLRMLISENTMRIEGGKWQLIPMWMRCCDIAAELFRVIPGRDELDRLIVVLFSTETPFPAVFACIVHLFHRTWREMQAKGGEMEKVACVVLEQLRHVLKRREIQDVEELSADLETFSYRAMQEIWREEQLGKENIQLHSEAVIQLKSKLRPKMEELVRINHLNYLKLGAVFRKPQKSKSLAKLAFWHWKLDASEKMLTITGCDGENYVEGVQRDDIRQVWIKDIADVTNNDEIDRKASSSRFTSSPSTQMLRGIRVQLKTTNDMKEGEVLMALTSDETQSVIWLEGLAELIGSKAVKSETDAMVERMLKMELRVRLLNVKLTNPEEKPEIPPIPDDIKSFISKF
Protein: Mitochondrial S-adenosylmethionine carrier protein (SAM carrier) (Solute carrier family 25 member 26) (Q5U680)
Organism: Mus musculus (Mouse)
Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S-adenosylmethionine (SAM) into the mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q70HW3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cysteine desulfurase
Sequence:
MDAPGFTASLVAGGVAGVSVDLILFPLDTIKTRLQSPQGFNKAGGFRGIYAGVPSAAVGSFPNAAAFFLTYEYVKSLLHTDSTSHFKPVKHMLAASTGEVVACLIRVPSEVVKQRAQVSASSKTLQIFLTILSEEGIQGLYRGYKSTVLREIPFSLVQFPLWESLKALWAWRRGHVVDSWQSAVCGAFAGGFAAAVTTPLDVAKTRIMLAKAGSSTAVGNVLSAMHGVWRSQGLAGLFAGVLPRMAAISMGGFIFLGAYDQARSLLLEVGRKSP
Protein: Mitochondrial adenyl nucleotide antiporter SLC25A25 (Short calcium-binding mitochondrial carrier protein 2) (SCaMC-2) (Solute carrier family 25 member 25) (A2ASZ8)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:15054102}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGMLDCARRILAKEGVAAFYKGYIPNMLGIIPYAGIDLAVYETLKNTWLQRYAVNSADPGVFVLLACGTISSTCGQLASYPLALVRTRMQAQASIEGAPEVTMSSLFKQILRTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKITLGVQSR
Protein: Small nuclear ribonucleoprotein-associated protein (Q9FI15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037187}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein SmD1b
- U1 small nuclear ribonucleoprotein C
- DEAD-box ATP-dependent RNA helicase 45
- Small nuclear ribonucleoprotein SmD3a
- Small nuclear ribonucleoprotein SmD3b
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein SmD1a
- Small nuclear ribonucleoprotein E
Sequence:
MSMSKSSKMLQFINYRMRVTIQDGRQLIGKFMAFDRHMNLVLGDCEEFRKLPPAKGNKKTNEEREERRTLGLVLLRGEEVISMTVEGPPPPEESRAKSGSVTAVAGPGIGRAAGRGVPTGPLVQAQPGLSGPVRGIGGPAPGMMQPQISRPPQIIRPPGQMPPQPPFAGQGGPPPPYGMRPPYPGPPPPQYGGQQRPMMIPPPGGMMRGPPPPHGMQGPPPSRPGMPPPGGAPMFAPPHPGMPPAPPNHHNQQH
Protein: Pregnancy-specific beta-1-glycoprotein 11 (PS-beta-G-11) (PSBG-11) (Pregnancy-specific glycoprotein 11) (Pregnancy-specific beta-1-glycoprotein 13) (PS-beta-G-13) (PSBG-13) (Pregnancy-specific glycoprotein 13) (Q9UQ72)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Chorionic somatomammotropin hormone 2
- Chorionic somatomammotropin hormone 1
- Pregnancy-specific beta-1-glycoprotein 3
Sequence:
MGPLSAPPCTEHIKWKGLLLTALLLNFWNLPTTAQVMIEAQPPKVSEGKDVLLLVHNLPQNLTGYIWYKGQIRDLYHYITSYVVDGQIIIYGPAYSGRETVYSNASLLIQNVTREDAGSYTLHIIKRGDGTRGVTGYFTFTLYLETPKPSISSSNLNPREAMETVILTCNPETPDASYLWWMNGQSLPMTHRMQLSETNRTLFLFGVTKYTAGPYECEIWNSGSASRSDPVTLNLLHGPDLPRIFPSVTSYYSGENLDLSCFANSNPPAQYSWTINGKFQLSGQKLFIPQITPKHNGLYACSARNSATGEESSTSLTIRVIAPPGLGTFAFNNPT
Protein: Phosphoethanolamine N-methyltransferase 2 (PMT-2) (EC 2.1.1.103) (S-adenosyl-L-methionine:phosphomethylethanolamine N-methyltransferase) (Q22993)
Organism: Caenorhabditis elegans
Function: Catalyzes the last two methylation reactions in the synthesis of phosphocholine, by converting phospho-monomethylethanolamine (N-methylethanolamine phosphate) into phospho-dimethylethanolamine (N,N-dimethylethanolamine phosphate) and the latter into phosphocholine. Phosphocholine is a precursor for phosphatidylcholine, a major component in membranes and a precursor itself in the production of glycoconjugates secreted by parasitic nematodes to avoid host immune responses.
Interaction partners:
- Methyltransf_11 domain-containing protein.
- Putative choline-phosphate cytidylyltransferase
- Choline kinase B1
- ethanolamine kinase
- Sigma non-opioid intracellular receptor 1
- Choline kinase A2
- Ethanolamine-phosphate phospho-lyase homolog 1
- 7-dehydrocholesterol reductase
- Choline kinase B2
- ethanolamine-phosphate cytidylyltransferase
Sequence:
MSSLSIPRQSLYYVNKVTEGRSVSNVQVVSPCQKQGQTYVTAFTPLTSNVQVHTSLEQLSTIRNADVLIFNNALSQIITNADLLTDFLKNATNATAIGGTVIIREDLKDCSDKRQVARLTDYFDVFRTTDSDGNNTGLDLYTVDQVEHSNYVEQNFLDFIFVFRKKVFAPTTDATITFRDFLDKTQYTNTGIDAYEWMFGVNFISPGGYDENLKIIKRFGDFKPGQTMLDIGVGIGGGARQVADEFGVHVHGIDLSSNMLAIALERLHEEKDSRVKYSITDALVYQFEDNSFDYVFSRDCIQHIPDTEKLFSRIYKALKPGGKVLITMYGKGYGEQSDKFKTYVAQRAYFLKNLKEIADIANKTGFVNVQTENMTPRFKEILLEERGHLEQNEAEFMSKFTQRERDSLISGWTDKLGYIEKDNHNWNFFLAQKPFPK
Protein: Septin interacting protein 2, isoform C (Q7KTL4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKLLEKHLPKKPVKMDETKDMRYSLEIDEDLRRPLEARAKKVLAVNSASQRTVNLGEDTMYEAGDLEHLDDGDDSFSAFERMCDKTGSDPDSTLFQYLHSEDRSQVMARARDHSTDDQKEIDALRRMLEAVGTEDDLLENESPVKGAECTHLEDIEAPSRFWDNTLAGMDETSSDSGLTPKALTKVSPVKMVGLLRPSTIIEDSELESSDVSSHTSFQSARTLKTNASSSYETATDTSLSGTLLNVDELFYAAIAKAKPPGMSKGEELELLSDLHGSLRELASLPKDEVEEEEDDIEDTIIELSSSDDEEVQLVPEVKQEDTSRVSSVHGKDHTEQKPAEKSVENKENSLHFNDTMEEMEYMMQKGMEYMAGGAPSVAAVKADCPVLPKTKQSTFVVSPKPEPKSPAVAFLQPSIPLRSSNQPQTVVGSSSTGRKPLNVGLTMEWTKKKFFSAASGIPQRRQNQIKQPYANIVSPIRTYTQKSGTAPLMSTFRPTSSDMLSTLAISELEQESRLCHPKALFATKDETPKSSEAESLIINGIDSAADLLPKKAYISSEIKHVVDERTPLPMPKVPQIQKYLNSAVEPTVMRHDGKMKMPGEAVRNPSSSHIPRRANHSLADLSLASGDVSLYTIRDAQKF
Protein: Uncharacterized protein YMR178W (Q03219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Adenylyl-sulfate kinase
- Riboflavin kinase
- Sulfite reductase subunit beta
- Mitochondrial FAD carrier protein FLX1
- Flavin adenine dinucleotide synthase
- Sulfate adenylyltransferase
Sequence:
MVKVTAACIIIGDEVLNGKVVDTNSTFFAKYCFDHGIQLKEIATIGDDETQIVDTVRRLVKNYDFIISTGGIGPTHDDITYECMAKSFNLPCELDEECKERMRHKSDPEARLDADALKAHYQMATMPKGTNVKNYYVCDDLWVPICSISHKMYILPGIPQLFARMLKAFTPTLKKIYNLDKDPREYVRYFVRTHLTESQISKELKLIQDESTKVSEAIKIGSYPHFGMGFNTVSILGEKKDDSYLKSIVNRVVNNLEGEVISSELENKFSNQES
Protein: Translation initiation factor eIF2B subunit epsilon (GCD complex subunit GCD6) (Guanine nucleotide exchange factor subunit GCD6) (eIF2B GDP-GTP exchange factor subunit epsilon) (P32501)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a catalytic component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD6 and GCD7 repress GCN4 expression at the translational level by ensuring that ribosomes which have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail to reach the GCN4 start site.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56287}.
Interaction partners:
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 2 subunit gamma
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2 subunit beta
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit alpha
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 5
- Protein DSS4
- eIF-2-alpha kinase GCN2
Sequence:
MAGKKGQKKSGLGNHGKNSDMDVEDRLQAVVLTDSYETRFMPLTAVKPRCLLPLANVPLIEYTLEFLAKAGVHEVFLICSSHANQINDYIENSKWNLPWSPFKITTIMSPEARCTGDVMRDLDNRGIITGDFILVSGDVLTNIDFSKMLEFHKKMHLQDKDHISTMCLSKASTYPKTRTIEPAAFVLDKSTSRCIYYQDLPLPSSREKTSIQIDPELLDNVDEFVIRNDLIDCRIDICTSHVPLIFQENFDYQSLRTDFVKGVISSDILGKHIYAYLTDEYAVRVESWQTYDTISQDFLGRWCYPLVLDSNIQDDQTYSYESRHIYKEKDVVLAQSCKIGKCTAIGSGTKIGEGTKIENSVIGRNCQIGENIRIKNSFIWDDCIIGNNSIIDHSLIASNATLGSNVRLNDGCIIGFNVKIDDNMDLDRNTKISASPLKNAGSRMYDNESNEQFDQDLDDQTLAVSIVGDKGVGYIYESEVSDDEDSSTEACKEINTLSNQLDELYLSDDSISSATKKTKKRRTMSVNSIYTDREEIDSEFEDEDFEKEGIATVERAMENNHDLDTALLELNTLRMSMNVTYHEVRIATITALLRRVYHFIATQTLGPKDAVVKVFNQWGLLFKRQAFDEEEYIDLMNIIMEKIVEQSFDKPDLILFSALVSLYDNDIIEEDVIYKWWDNVSTDPRYDEVKKLTVKWVEWLQNADEESSSEEE
Protein: Conidiophore development protein hymA (O60032)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for conidiophore development.
Subcellular location: Cytoplasm.
Interaction partners:
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MAFFFNRGRSRQPSDVVRSIKDLLLRLREPSTASKVEDELAKQLSQMKLMVQGTQELEASTDQVHALVQAMLHEDLLYELAVALHNLPFEARKDTQTIFSHILRFKPPHGNSPDPPVISYIVHNRPEIIIELCRGYEHSQSAMPCGTILREALKFDVIAAIILYDQSKEGEPAIRLTEVQPNVPQRGTGVFWRFFHWIDRGTFELSADAFTTFREILTRHKSLVTGYLATNFDYFFAQFNTFLVQSESYVTKRQSIKLLGEILLDRANYSVMMRYVESGENLKLCMKLLRDDRKMVQYEGFHVFKVFVANPDKSVAVQRILINNRDRLLRFLPKFLEDRTDDDQFTDEKSFLVRQIELLPKEPIEPSRSAREPSRSTANTTTVA