wanglab/gogpt-training-data huggingface dataset:
Protein: Ceramide transfer protein (hCERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11) (Q9Y5P4)
Organism: Homo sapiens (Human)
Function: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Golgi apparatus {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:29858488}. Endoplasmic reticulum {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Note=Preferentially localized to the Golgi apparatus. {ECO:0000305|PubMed:16895911}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein A
- Casein kinase I isoform gamma-2
- Vesicle-associated membrane protein-associated protein B/C
- Serum amyloid P-component
- Collagen alpha-3
- Phosphatidylcholine transfer protein
- Collagen alpha-1
- Serine/threonine-protein kinase D3
- Pleckstrin
- Pleckstrin-2
Sequence:
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
Protein: Glycine-rich protein (T7N9.15) (Q9LFX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAATASSEASEGPVMGLINKRLRALRKKYNRITQMEESISQGKTLNKEQEEVLRSKPAVVILIDELEKIRAPLSAAVTEEISLATQLNRASSDQTTASEQKEVTDIPQEVSGGDDGAKLEDLVNFLYFGSLFDVKSQNEFTSIMLTRTHERSCCLSYDYVTDDATDLLGDRDLDSISQLWSLMVSRPVDSSLSHKNALERCVEHAKLWLANSEQPIESNCNTSYAALREKLKKIMASDYFTTTPEMKAPVDVAAAAGNYTSYQVPVDVEASGHYQQKEEDASNSKEVESVVNDQSQQDEHQKVELVTEGEVVHGQQEQGYTQVGGAENAKRDYVPRGSYQNQRGRRGARRGGGGYQNGRGGRGGGGGYQNGRYESYDQSGGNGYQRNYYNNRGRGRGGGGGGGNGHSYNNYQDPNVAVAS
Protein: [PSI+] induction protein 2 (Q12057)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Not known. Seems to be able to provoque the non-Mendelian trait [PIN(+)] which is required for the de novo appearance of the [PSI(+)] prion.
Subcellular location: Membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein BCH2
- Protein BCH1
- Chitin synthase 3
- RNA-binding protein PIN4
- Guanine nucleotide-binding protein subunit gamma
- [PSI+] inducibility protein 3
- Cell wall assembly regulator SMI1
- Bud site selection protein 7
Sequence:
MNVCKLKEIVPLFPRSSFTDGVVSTGKSFRSWDTCMDNKACKIIAIVGIVLACILVIWLIGGLLTCFRQGVTGIGQFICWCCRCSNDRNGNNTMPVNEGFSRVNMGVAPPSTVIYQPIQQPESAYYRNDAKNDTFYDEVKTPSNEVYELEEDFDLEKQKEKTRKKQQKERNKEGRSPSRVAPLVYEEENFEGSSPQPQYDARNSFIQNAANTGSNNAHVASQSPIFDISDYGENYYYDNNNINNNLQGNSYNTPSSNHRSPYPTENYQSYQGYKPNQSDRYY
Protein: Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4) (P97471)
Organism: Mus musculus (Mouse)
Function: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13485}. Nucleus {ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation. {ECO:0000250|UniProtKB:Q13485}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 9
- Lymphoid enhancer-binding factor 1
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 5
- Ski-like protein
- Forkhead box protein H1
- TGF-beta receptor type-1
- TGF-beta receptor type-2
Sequence:
MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPAESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPVVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD
Protein: Annexin (Q27512)
Organism: Caenorhabditis elegans
Interaction partners:
- Actin
- Calreticulin
- SCP domain-containing protein
- SCP domain-containing protein
- Tetraspanin
- Tetraspanin
- Tetraspanin
- Sperm vesicle fusion protein fer-1
Sequence:
MSLRKFVMSGIQDVLDNKLGGLGGNNKQQQPSSQQSSQEPSNMNSGGGYPNQQPSYGGYGQPPQQPGYGNGSYDPYGQPQQQPYPGGGGQPPYPGSNSNQGGGGYPGQGGAPYPGGSGGYPQAPQYGFSGGQGSAPQPNQGGYPPQQQQYPPQQGYQQGGQQQGGGGFFPNQGYGQPVMIGTPSVFPVQGFNSNADAEVLRKAMKGLGCNNSKVISILCQRTNWQRQEISKAFKVMYGKDLIKELKGELHGDFEDLILALMDAPAIYDAKQLHRAMEGLGTKESVLIEIMTSRTNAQIQQVRDAYKMLFKKDLERDLIGETSGHFKRLLVSLCAGGRDESSQTDGLRANQDARRLLQAGEKRLGTDESTFNAILASQNFSQLRLVFEEYQKASNHSIEKAIEFEFSGDIRDGLLAVIAVIRNRPAYFAKLLHDSMKGLGTRDNDLIRLCVTRAEYDMGDIRNMFQSLYRTSLENMIKGDCSGAYKEGLIALVNGNRG
Protein: DNA damage-inducible protein I (P0ABR1)
Organism: Escherichia coli (strain K12)
Function: Involved in SOS regulation. Inhibits RecA by preventing RecA to bind ssDNA. Can displace ssDNA from RecA.
Interaction partners:
- Protein RecA
- LexA repressor
- Uncharacterized protein YebG
- Protein UmuD
- Regulatory protein RecX
- DNA repair protein RecN
- Protein UmuC
- DNA damage-inducible protein D
- Recombination-associated protein RdgC
- DNA replication and repair protein RecF
Sequence:
MRIEVTIAKTSPLPAGAIDALAGELSRRIQYAFPDNEGHVSVRYAAANNLSVIGATKEDKQRISEILQETWESADDWFVSE
Protein: 40S ribosomal protein S4 (C8VAM4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 40S ribosomal protein S24
- Large ribosomal subunit protein eL39
- 60S ribosomal protein L23
- Large ribosomal subunit protein uL22
- 40S ribosomal protein S15
- 60S ribosomal protein L30, putative
- GBLP_NEUCR Guanine nucleotide-binding protein beta subunit-like proteinGbeta like protein
- 60S ribosomal protein L11
- 60S ribosomal protein L35Ae
- Small ribosomal subunit protein uS2
Sequence:
MPRGPKKHQKRLSAPSHWLLDKMSGTYAPKASPGPHKLRDCLPLIVFIRNRLKYALNGRETKAIMMQRLIQVDGKVRTDPTYPAGFMDVITIEKTGENFRLIYDTKGRFTVHRIQAEEAEYKLCKVKKVQLGKGGIPFLVTHDARTIRYPDPAIKVNDTVKVDIATGKITDFCRFDTGVVCMVTGGRNMGRVGVVTHRERHDGGFNIVHVKDAIDNTFATRESNVFVIGQDKPWISLPKGKGVKLSIAEERDRRRAYALAQ
Protein: Transmembrane protein 214 (Q6NUQ4)
Organism: Homo sapiens (Human)
Function: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23661706}; Multi-pass membrane protein {ECO:0000269|PubMed:23661706}.
Interaction partners:
- Exonuclease 3'-5' domain-containing protein 2
- CCR4-NOT transcription complex subunit 2
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha isoform 1
- Translocation protein SEC63 homolog
- Translocation protein SEC62
Sequence:
MATKTAGVGRWEVVKKGRRPGVGAGAGGRGGGRNRRALGEANGVWKYDLTPAIQTTSTLYERGFENIMKRQNKEQVPPPAVEPKKPGNKKQPKKVATPPNQNQKQGRFRSLEEALKALDVADLQKELDKSQSVFSGNPSIWLKDLASYLNYKLQAPLSEPTLSQHTHDYPYSLVSRELRGIIRGLLAKAAGSLELFFDHCLFTMLQELDKTPGESLHGYRICIQAILQDKPKIATANLGKFLELLRSHQSRPAKCLTIMWALGQAGFANLTEGLKVWLGIMLPVLGIKSLSPFAITYLDRLLLMHPNLTKGFGMIGPKDFFPLLDFAYMPNNSLTPSLQEQLCQLYPRLKVLAFGAKPDSTLHTYFPSFLSRATPSCPPEMKKELLSSLTECLTVDPLSASVWRQLYPKHLSQSSLLLEHLLSSWEQIPKKVQKSLQETIQSLKLTNQELLRKGSSNNQDVVTCDMACKGLLQQVQGPRLPWTRLLLLLLVFAVGFLCHDLRSHSSFQASLTGRLLRSSGFLPASQQACAKLYSYSLQGYSWLGETLPLWGSHLLTVVRPSLQLAWAHTNATVSFLSAHCASHLAWFGDSLTSLSQRLQIQLPDSVNQLLRYLRELPLLFHQNVLLPLWHLLLEALAWAQEHCHEACRGEVTWDCMKTQLSEAVHWTWLCLQDITVAFLDWALALISQQ
Protein: Mitochondrial amidoxime reducing component 1 (H7BYZ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XFWLVINQEGNMVTARQEPRLVLISLTCDGDTLTLSAAYTKDLLLPIKTPTTNAVHKCRVHGLEIEGRDCGEATAQWITSFLKSQPYRLVHFEPHMRPRRPHQIADLFRPKDQIAYSDTSPFLILSEASLADLNSRLEKKVKATNFRPNIVISGCDVYAEVTLCPFGSFLGFDFFFKDSWDELLIGDVELKRVMACSRCILTTVDPDTGVMSRKEPLETLKSYRQCDPSERKLYGKSPLFGQYFVLENPGTIKVGDPVYLLGQ
Protein: Matrilin-2 (O00339)
Organism: Homo sapiens (Human)
Function: Involved in matrix assembly.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MEKMLAGCFLLILGQIVLLPAEARERSRGRSISRGRHARTHPQTALLESSCENKRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDHVFLVANFSQIETLTSVFQKKLCTAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTTCRIQDLCAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRCVAVDYCASENHGCEHECVNADGSYLCQCHEGFALNPDKKTCTKIDYCASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTCRRINYCALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKTCSRVDYCLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGRRCKKCTEGPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNKHLFYAEDFSTMDEISEKLKKGICEALEDSDGRQDSPAGELPKTVQQPTESEPVTINIQDLLSCSNFAVQHRYLFEEDNLLRSTQKLSHSTKPSGSPLEEKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRLRYR
Protein: Monacolin J acid methylbutanoyltransferase (EC 2.3.1.238) (Lovastatin biosynthesis cluster protein D) (Lovastatin hydrolase) (Simvastatin synthase LovD) (SV synthase) (Q0C8M0)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Monacolin J acid methylbutanoyltransferase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
- Cystathionine beta-synthase
- Tryptophan synthase
- Tryptophan synthase
- Tryptophan synthase
Sequence:
MGSIIDAAAAADPVVLMETAFRKAVKSRQIPGAVIMARDCSGNLNYTRCFGARTVRRDECNQLPPLQVDTPCRLASATKLLTTIMALQCMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLLTHTSGLSYVFLHPLLREYMAQGHLQSAEKFGIQSRLAPPAVNDPGAEWIYGANLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARRADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSGPGSYMKVLHSLLKRDGLLLQPQTVDMMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRSFGLGGIIALEDLDGEDWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLEPWNDPVCRDLTRTFEHAIYAQYQQG
Protein: KIR2DS4 (F2VZG2)
Organism: Pan troglodytes (Chimpanzee)
Interaction partners:
Sequence:
MSLMVVSMACVGFFLLQGAWPHEGVQIKPSLLALPGHLVKSEETVILQCWSDVMFEHFLLHREGKFNDTLHLIGEHHDGVSKANFSIGPMMPVLAGTYRCYGSVPHSPYQLSAPSDHLDIVITGLYEKPSLSAQPGPTVQAGENVTLSCSSRSSYDMYHLSREGEVHERRLPAVRSIKGTFQADFPLGPATHGGTYRCFGSFRDAPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSNKKKCCRNGPRACREQNSEPGGF
Protein: Cac2p (A0A1D8PNS7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone chaperone ASF1
- Uncharacterized protein
- Histone chaperone RTT106
- Histone acetyltransferase type B subunit 2
- Histone-binding protein RBBP4-like N-terminal domain-containing protein
- Histone transcription regulator 3 homolog
- Proliferating cell nuclear antigen
- Ecm15p
- Histone H2A.Z-specific chaperone CHZ1
- Histone H4
Sequence:
MEATILTVHWHNDNQPIYSVDFQPEQSGLVNSSPTKSAESTRLATGGGDNNIRIWKITSSNSVEYMSTLQKHSQAVNAVRFNPRGDILASAGDDGTLLLWKKSENIIKTLESEEDEDLKESWQVVGTIRSSTAEIMDICWSPNGEQIVTGSMDNILRVYQLEFSPGKITGTFIRSFSDHTHYIQGVFWDPLNKFIVSQSADRSVNVYQISPSESNSIEINFRHKFQKFGNLYLYYPETLQSFFRRLAFSPDGSILVTPAGLEETSSNETLNNVLYIYSRASLFTSPIYKITGLSKPAIAVSFNPVKYKSDGPSTLKLPYKLVFAVATQDGVVLYSTQDNFKPLGLVSNLHYSSITDLKWTVDGSRVIISSTDGFCSTINFPGSAFGERYIGVPHDNDILSGEILQAKTESKAEPVPSSEIPNEKSPNSKSDNSKTSIPTIDLFFDKNQKVKKRITPTLIS
Protein: Adenosine transporter 1, putative (Q581D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLGFYSVPEFVVYVTFIFFGMSVMNVTNAIYSIPFFFKEYYKFAQGDADVQPKDEGFWKHMFTYYNVVVYTMQVLLEAFMLTPLGRRFPIRWRLTFGLAVPIVEIIVILVIPVVRTSEDAAKAAMMMIAFIGGVSKTLCDSGNAALVGPFPTKFYGAVVWGLGISGLLTSFMSIIIKVSMDDSFSSLLTQSRIYFGLIMLLQVIACILLVLLRKNPYAMRYAAELRFDAKKSGTKDSNGLVDVADARGTGPADEECEREADERSDINVMNATTDPDTMRDTDQLENMTNAKQMLDASVMVVAKRIWPMLVSCFFVFFATLLVFPGVFFAVKTDVPSGWYFTIVAAMYNLGDFLSRLVLQFKRLHPSPRGVVIGTFSRLLVIPLLALCVYDVISGPWVPYVLCLIWGLTNGYFGGMSMIYGPRTGSLTTAGQRSLAAICINLALLLGLFGGAMSAMAVIKALPH
Protein: Uncharacterized protein ZSWIM9 (Q86XI8)
Organism: Homo sapiens (Human)
Interaction partners:
- Zinc finger SWIM domain-containing protein 1
Sequence:
MERPEPPPGTAAGQEEQELRERAFFSWAEFSRFFDAWCQQRLALFFVKSSMHLARCRWASAPPLYTLIDVLKYSYVRLVCKDVRAPSRPAVGPPQPGCPAFIIVKLSPLRDRLVVTECQLTHSHPACPLEFAYYFRPGHLLANACLPVRTTNKISKQFVAPADVRRLLSYCKGRDHGVLDALHVLEGLFRTDPEAKVKLVFVEDQAVVETVFFLTSRTRALLRRFPRMLLVDRLPGLQGALDLLAVLCVDGSGRARQAACCVARPGTPSLLRFALASLLQSAPDVKGRVRCLTAGPEVAAQLPAVRQLLPCARVQICRAQGLETLFSKAQELGGAGREDPGLWSRLCRLAGASSPAAYDEALAELHAHGPAAFVDYFERNWEPRRDMWVRFRAFEAARDLDACALVRGHRRRLLRRLSPSRGVAQCLRDLVAMQWADAAGEAVPEGPDGGGPWLEDEPGRGAQGENERVRGLETGDWGGAPKEGSIWRGAQMEKEWARALETRDWGGAQFEGEKGRALQIRDWRGGRLENQKPRGLEGGVLRGSKLEKGHLRGPEIRDWRGPQLEGEKDWGLEGYVWRGSQLEDQALRGLEGYTWRVAQLEDRRSTTDLRGTQFDYERGKGESTEDR
Protein: Membrane progestin receptor delta (mPR delta) (Membrane progesterone P4 receptor delta) (Membrane progesterone receptor delta) (Progesterone and adipoQ receptor family member 6) (Progestin and adipoQ receptor family member 6) (Q6TCH4)
Organism: Homo sapiens (Human)
Function: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(s) mediated pathway. Involved in neurosteroid inhibition of apoptosis. May be involved in regulating rapid P4 signaling in the nervous system. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23161870}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Membrane progestin receptor epsilon
- Membrane progestin receptor alpha
- Membrane-associated progesterone receptor component 1
Sequence:
MLSLKLPQLLQVHQVPRVFWEDGIMSGYRRPTSSALDCVLSSFQMTNETVNIWTHFLPTWYFLWRLLALAGGPGFRAEPYHWPLLVFLLPACLYPFASCCAHTFSSMSPRMRHICYFLDYGALSLYSLGCAFPYAAYSMPASWLHGHLHQFFVPAAALNSFLCTGLSCYSRFLELESPGLSKVLRTGAFAYPFLFDNLPLFYRLGLCWGRGHGCGQEALSTSHGYHLFCALLTGFLFASHLPERLAPGRFDYIGHSHQLFHICAVLGTHFQLEAVLADMGSRRAWLATQEPALGLAGTVATLVLAAAGNLLIIAAFTATLLRAPSTCPLLQGGPLEGGTQAKQQ
Protein: Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative (Q5LNC1)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Phenylacetate-CoA ligase, putative
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid-binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid-binding protein, putative
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
Sequence:
MKMKLATVALGALMAAGPALADLTFPSLSYRTGPYAAGGIPFADGYADYFTLLNERDGGIGGVKANVLECETGYNTEKGVECYESTKGQGALVYQPLSTGITYQLIPKATADGIAIHSMGYGRTSAKNGNVFSHVFNYPANYWDGASGAVNYLLEINGGDIKGKKIALVYHNSAYGKEPIRTLEELSKKHGFDLSTLPVDHPGQEQKSQWLQIRRDKPDYVLMWGWGVMNQVAVQEAANIRFPMENFIGIWWSGSENDVLPAGDAANGYKALTFHNVGTAFPLFDDLQKYVIDAGKAAGAGDQVGTVLYNRGLYAAMLAAEAAKKAQEISGKADITAADMRDGMEALEMTEAKMAELGLPNFGPTFSVSCGNHGGDALVGVTQWDATSKTWSLISDFKPTDGDVIGALIEEDSSAYASENNISPRCN
Protein: U6 snRNA-specific terminal uridylyltransferase (TUTase) (EC 2.7.7.52) (PAP-associated domain-containing protein) (U6 snRNA-interacting protein) (Q23652)
Organism: Caenorhabditis elegans
Function: Acts as a specific terminal uridylyltransferase for U6 snRNA. Responsible for the addition of UTP at the 3' end of U6 snRNA which stabilizes U6 snRNA. Does not have activity towards modified uridine containing 3'-monophosphorylation or 2'-O-methylation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000305|PubMed:25753661}.
Interaction partners:
- Spliceosome associated factor 3, U4/U6 recycling protein
- Thioredoxin-like protein
- U6 snRNA-associated Sm-like protein LSm8
- PAP-associated domain-containing protein
- Poly
Sequence:
MSSNLQLVETFDSRQFVVARWNRNDTTAMVPSAIAVVVFVESVEYKLGCKEKIGYSPTPEDQDQFMILQMESIDEANRICHDSIAKGFAINNTKIVFTPLLGLNGFRLQDAIDFMKTSQPHFNNDELLEVLTMAICQELPERLKILEDGFSFIEQGVSELIQNSACEMFGSFASPVRRNGYSDIDINVESVSAPGQRVSTNVRPLNEVVANPKCLITHPLTKSELETYPQEEIIKILYRCFNENSAFKTKFEMRFLPARTPIIVFKNIEVEGMNVSYDLSVHNQISVEKASLLHEFIVKDKSKGSRMKNAMMFIVHWAKSNKLLSGDYPEEKLEVKTKLNSYIINQLVIHFVQAATNKVHVNPQAKRDSRVNEYNFDTLFGDYCKFFRELFKYYANFDFTNKAIYGKKAMQKKTLSSAHGGVEESPLMLMDPMDITHNISAKVTEDAVKLLNGLIRNALFILKQNHFHINYLLETNTMATMLMKSREPKISISTRVTDGAEHQYLSVQLPAVVITSSDLFLLLTRVLRFNVCPNEQGPSVVDLCTPTGAIFLVTSRAWVGRRNTKRALKNSRHDLTPLQIDVMCSDKYDYEEDIAELRISMSTVPGTRIRLACIDIMRGQVSEVRDAIHFLIDQFINNNYDDLEKNGVQTISRIPIAAPTWP
Protein: Manganese/iron superoxide dismutase C-terminal domain-containing protein (Q585I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- 30S Ribosomal protein S17, putative
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
- Mitochondrial ribosomal protein S18
- Uncharacterized protein
- Uncharacterized protein
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
Sequence:
MLRRTVTSLRNARELHRLLPALLPLLDPPVPTGASVCAAHLIVATGHVSKQREPHMSNCPVLERKIPLSEIASDDNFLKHPCVPCLKHRINFLASEDFCYDFVERCGCGTDGALPPEWRCIVERQFGSMAALVEELVIHASNRREAGWTWLVYDAQQAGERPLLVVNMPAQRSPLLLGLWPLAVVNVTEAVLVEAVRAESSGSVAAAPPPPWCRAARASLYDTKAAAEAFAMTAPMSEGVGKKLSEIREKVARDAVSRMNWGFILQQLKKAETYYASSDRGEKIRVHRMKLEREAVTKAMSGLRDSGATFLTHDTVEVTTTPSANSEPSSPERVPGVQAKQPQTEGMDPCENKASAEPDPKCTQLPDGTWQYSYRNGDVTLLKPDGTRVFRKRELTTTAYPDGSMLFQYANNTSILDRADGVRVTTFEDGTTKEEMIRR
Protein: 26S proteasome non-ATPase regulatory subunit 8 (Q9V436)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory complex subunit p50
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 13
- Regulatory particle triple-A ATPase 4
Sequence:
MANVESLYKELTAEWSKRPPNTVKCGQLLDQLKVALVKMAFLPTDGNDAQSSKKQLILARSVLEVAVEHSVLSKDLLAFERYMAQLKCYYYDYAKIIGESESKYKLLGLNLLYLLSGNRVSDFHTELELLSVDVIQHNQFIRPILALEQYIMEGRYNKIFQAKSTVPVEVYSYFMDLLLETVRDEIGACIEKSYDKISAKDAAKRLNLRVPDEIKAFGAKRQWKLEASGDYSFTDRSVKPKELLPSEELAEQVLSYARDLEMIV
Protein: Trimethylguanosine synthase (EC 2.1.1.-) (Cap-specific guanine-N(2) methyltransferase) (snRNA/snoRNA cap hypermethylase) (Q12052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the two serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylates the m3G cap on TLC1 telomerase which affects telomere silencing and telomere length regulation. Required for pre-mRNA splicing, pre-rRNA processing and small ribosomal subunit synthesis. Involved in nucleolar structural organization.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11983179, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein G
- Nucleolar protein SWM2
- Splicing factor MUD2
- Small nuclear ribonucleoprotein-associated protein B
- Protein NAM8
- Nuclear cap-binding protein subunit 2
- U1 small nuclear ribonucleoprotein A
Sequence:
MGRTFIHASKIKHAARKRKHHSNFRTLIKLLNNDAYKIESSKPLKNGKLFKYWKNRRRLFSKIDSASIYMTDELWFSVTPERIACFLANFVKACMPNAERILDVFCGGGGNTIQFAMQFPYVYGVDYSIEHIYCTAKNAQSYGVDDRIWLKRGSWKKLVSKQKLSKIKYDCVFGSPPWGGPEYLRNDVYDLEQHLKPMGITKMLKSFLKLSPNVIMFLPRNSDLNQLSRATRKVLGPFAKCKVLYVKENGYMKGIFCMWGECFFNYEPASTENSRRESSEKEELSSENEELSKRKKHESTTTTKDNTVDIYDVNG
Protein: Testis-specific Y-encoded-like protein 6 (TSPY-like protein 6) (Q8N831)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLPESPHSPATLDYALEDPHQGQRSREKSKATEVMADMFDGRLEPIVFPPPRLPEEGVAPQDPADGGHTFHILVDAGRSHGAIKAGQEVTPPPAEGLEAASASLTTDGSLKNGFPGEETHGLGGEKALETCGAGRSESEVIAEGKAEDVKPEECAMFSAPVDEKPGGEEMDVAEENRAIDEVNREAGPGPGPGPLNVGLHLNPLESIQLELDSVNAEADRALLQVERRFGQIHEYYLEQRNDIIRNIPGFWVTAFRHHPQLSAMIRGQDAEMLSYLTNLEVKELRHPRTGCKFKFFFQRNPYFRNKLIVKVYEVRSFGQVVSFSTLIMWRRGHGPQSFIHRNRHVICSFFTWFSDHSLPESDRIAQIIKEDLWSNPLQYYLLGEDAHRARRRLVREPVEIPRPFGFQCG