wanglab/gogpt-training-data huggingface dataset:
Protein: Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase) (P35915)
Organism: Gallus gallus (Chicken)
Function: Mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis. Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38060}. Peroxisome {ECO:0000250|UniProtKB:P38060}. Note=Unprocessed form is peroxisomal. {ECO:0000250|UniProtKB:P38060}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- Uncharacterized protein
- AU RNA binding methylglutaconyl-CoA hydratase
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Uncharacterized protein
- Acetoacetyl-CoA synthetase
- Uncharacterized protein
- Uncharacterized protein
Sequence:
AFPQRVKVVEVGPRDGLQNEKSVVPTPVKIRLIDMLSETGLPVIEATSFVSPRWVPQMADHAEVMQGINKLPGVSYPVLTPNLKGFQAAVAAGAKEVSIFGAASELFTKKNINCSIEESLERFSEVMNAARAASIPVRGYVSCVLGCPYEGNISAAKVAEVSKKMYSMGCYEISLGDRIGIGTPGSMKEMLAAVMKEVPVGALAVHCHDTYGQALANILVALQMGVSVVDASVAGLGGCPYAQGASGNVATEDLVYMLNGLGIHTGVDLQKLMDTGTFICNALNRRTNSKVSQAACRL
Protein: Nuclear cap-binding protein subunit 1 (80 kDa nuclear cap-binding protein) (AtCBP80) (NCBP 80 kDa subunit) (Abscisic acid-hypersensitive protein 1) (ABA-hypersensitive protein 1) (Protein ENSALADA) (Q9SIU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs). The CBC complex is involved in miRNA-mediated RNA interference and is required for primary miRNA processing. In the CBC complex, ABH1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Involved in flowering regulation, possibly by regulating pre-mRNA splicing of FLC gene. Acts as a negative regulator of abscisic acid signaling in guard cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:12427994}. Cytoplasm {ECO:0000269|PubMed:12427994}. Note=Predominantly nuclear.
Interaction partners:
- Serrate RNA effector molecule
- Nuclear cap-binding protein subunit 2
- Small nuclear ribonucleoprotein Sm D2
- Regulator of nonsense transcripts 1 homolog
- THO complex subunit 2
- Regulator of nonsense transcripts UPF3
- Small nuclear ribonucleoprotein E
- U1 small nuclear ribonucleoprotein C
- Small nuclear ribonucleoprotein SmD3a
- Small nuclear ribonucleoprotein E
Sequence:
MSNWKTLLLRIGEKGPEYGTSSDYKDHIETCFGVIRREIERSGDQVLPFLLQCAEQLPHKIPLYGTLIGLLNLENEDFVQKLVESVHANFQVALDSGNCNSIRILLRFMTSLLCSKVIQPASLIVVFETLLSSAATTVDEEKGNPSWQPQADFYVICILSSLPWGGSELAEQVPDEIERVLVGIQAYLSIRKNSSTSGLNFFHNGEFESSLAEKDFVEDLLDRIQSLASNGWKLESVPRPHLSFEAQLVAGKFHELRPIKCMEQPSPPSDHSRAYSGKQKHDALTRYPQRIRRLNIFPANKMEDVQPIDRFVVEEYLLDVLFYLNGCRKECASYMANLPVTFRYEYLMAETLFSQILLLPQPPFKTLYYTLVIMDLCKALPGAFPAVVAGAVRALFEKISDLDMESRTRLILWFSHHLSNFQFIWPWEEWAFVLDLPKWAPKRVFVQEILQREVRLSYWDKIKQSIENATALEELLPPKAGPNFMYSLEEGKEKTEEQQLSAELSRKVKEKQTARDMIVWIEETIYPVHGFEVTLTIVVQTLLDIGSKSFTHLVTVLERYGQVFSKLCPDNDKQVMLLSQVSTYWKNNVQMTAVAIDRMMGYRLVSNQAIVRWVFSPENVDQFHVSDQPWEILGNALNKTYNRISDLRKDISNITKNVLVAEKASANARVELEAAESKLSLVEGEPVLGENPAKMKRLKSTVEKTGEAELSLRESLEAKEALLNRALSETEVLLLLLFQSFLGVLKERLPDPTKVRSVQDLKSIGAEDDKPSAMDVDSENGNPKKSCEVGEREQWCLSTLGYLTAFTRQYASEIWPHMEKLESEVFSGEDVHPLFLQAISSALQFPLH
Protein: Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (T9) (p90) (CD antigen CD71) [Cleaved into: Transferrin receptor protein 1, serum form (sTfR)] (P02786)
Organism: Homo sapiens (Human)
Function: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake. Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway. When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion. When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17081065}; Single-pass type II membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.; SUBCELLULAR LOCATION: [Transferrin receptor protein 1, serum form]: Secreted {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Serotransferrin
- Hereditary hemochromatosis protein
- Beta-2-microglobulin
- Ferritin heavy chain
- Hemojuvelin
- Heat shock cognate 71 kDa protein
- Natural resistance-associated macrophage protein 2
- Iron-responsive element-binding protein 2
- Ferroportin
- Hepcidin
Sequence:
MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPKRCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF
Protein: Trans-3-hydroxy-L-proline dehydratase (T3LHyp dehydratase) (t3HypD) (EC 4.2.1.77) (Trans-L-3-hydroxyproline dehydratase) (B9K4G4)
Organism: Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4) (Agrobacterium vitis (strain S4))
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline. Displays neither proline racemase activity nor 4-hydroxyproline 2-epimerase activity.
Interaction partners:
Sequence:
MRTNKVIHVIGVHAEGEVGDVIVGGVSPPPGDTLWEQSRFIASDETLRNFVLNEPRGGVFRHVNLLVPPKDPRAQMGFIIMEPADTPPMSGSNSICVSTAILDSGIISMQEPLTHMVLEAPGGVIEVTAECANGKAERINVLNVASFVTRLAAALEVEGLGTLTVDTAYGGDSFVIVDAIGLGFSLKPDEARELAELGMKITAAANEQLGFVHPCNADWNHISFCQMTTPITRENGILTGKSAVAIRPGKIDRSPTGTGCSARLAVMHARGEIGIGETYIGRSIIDSEFKCHIDSLTEIGGLSAIRPVISGRAWITGVSQLMLDPTDPWPSGYQLSDTWPAI
Protein: Heat shock 70 kDa protein 2 (Heat shock cognate 70 kDa protein 2) (Heat shock cognate protein 70-2) (AtHsc70-2) (Heat shock protein 70-2) (AtHsp70-2) (P22954)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21418353}. Cytoplasm, cytosol {ECO:0000269|PubMed:28004282}. Nucleus {ECO:0000269|PubMed:28004282}.
Interaction partners:
- Heat shock protein 90-1
- Heat shock protein 90-5, chloroplastic
- Heat shock 70 kDa protein 17
- Chaperone protein dnaJ 2
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Heat shock protein 90-3
- Heat shock protein 90-2
- Heat shock protein 90-6, mitochondrial
- Ankyrin repeat family protein
- Chaperone protein dnaJ 20, chloroplastic
Sequence:
MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPVNTVFDAKRLIGRRFSDASVQSDRQLWPFTIISGTAEKPMIVVEYKGEEKQFAAEEISSMVLIKMREIAEAFLGTTVKNAVVTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKQDITGQPRALRRLRTACERAKRTLSSTAQTTIEIDSLYGGADFYSPITRARFEEMNMDLFRKCMEPVEKCLRDAKMDKSTVHEIVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTTLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVFEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGKKNKITITNDKGRLSKEDIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIRDEKIGEKLPAADKKKVEDSIEEAIQWLDGNQLGEADEFEDKMKELESVCNPIIAKMYQGGAGGEAGGPGASGMDEDEAPPASGGAGPKIEEVD
Protein: Rabphilin-3A (Exophilin-1) (Q9Y2J0)
Organism: Homo sapiens (Human)
Function: Plays an essential role in docking and fusion steps of regulated exocytosis (By similarity). At the presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle membrane in a GTP-dependent manner where it modulates synaptic vesicle trafficking and calcium-triggered neurotransmitter release (By similarity). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability. Also plays a role in the exocytosis of arginine vasopressin hormone (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P47709}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P47709}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P47709}. Membrane {ECO:0000250|UniProtKB:P47709}; Peripheral membrane protein {ECO:0000250|UniProtKB:P47709}.
Interaction partners:
- Ras-related protein Rab-3A
- Synaptosomal-associated protein 25
- Ras-related protein Rab-27A
- Ras-related protein Rab-8A
- Unconventional myosin-Va
- Ras-related protein Rab-27B
- Ras-related protein Rab-3B
- Melanophilin
- Ras-related protein Rab-3C
- Glutamate receptor ionotropic, NMDA 2A
Sequence:
MTDTVFSNSSNRWMYPSDRPLQSNDKEQLQAGWSVHPGGQPDRQRKQEELTDEEKEIINRVIARAEKMEEMEQERIGRLVDRLENMRKNVAGDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETNNRLHSVWLCKICIEQREVWKRSGAWFFKGFPKQVLPQPMPIKKTKPQQPVSEPAAPEQPAPEPKHPARAPARGDSEDRRGPGQKTGPDPASAPGRGNYGPPVRRASEARMSSSSRDSESWDHSGGAGDSSRSPAGLRRANSVQASRPAPGSVQSPAPPQPGQPGTPGGSRPGPGPAGRFPDQKPEVAPSDPGTTAPPREERTGGVGGYPAVGAREDRMSHPSGPYSQASAAAPQPAAARQPPPPEEEEEEANSYDSDEATTLGALEFSLLYDQDNSSLQCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETRFSLKKLKPNQRKNFNICLERVIPMKRAGTTGSARGMALYEEEQVERVGDIEERGKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQLGISAKGERLKHWYECLKNKDKKIERWHQLQNENHVSSD
Protein: RAC-alpha serine/threonine-protein kinase (EC 2.7.11.1) (RAC-PK-alpha) (G9BWQ1)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MNDVAVVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDLEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEEMMDFRSGSPSENSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFPEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFASIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEGVDSERRPHFPQFSYSASGTA
Protein: Ferric uptake regulation protein (Ferric uptake regulator) (P33086)
Organism: Yersinia pestis
Function: Fur acts as a repressor, employing Fe(2+) as a cofactor to bind the operator of the iron transport operon.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Thioredoxin 1
- DNA-directed RNA polymerase subunit alpha
- Glutamate synthase large chain
- Similar to Vibrio cholerae hypothetical protein VC2666 TR:Q9KNR5
- Similar to Campylobacter jejuni alkyl hydroperoxide reductase subunit C AhpC or Cj0334 TR:Q9ZI13
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor RpoD
- RNA polymerase sigma-32 factor
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
Sequence:
MTDNNKALKNAGLKVTLPRLKILEVLQNPACHHVSAEDLYKILIDIGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSNESIESLQREIAKQHGIKLTNHSLYLYGHCETGNCREDESAHSKR
Protein: Zinc finger protein 704 (Q6ZNC4)
Organism: Homo sapiens (Human)
Function: Transcription factor which binds to RE2 sequence elements in the MYOD1 enhancer.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ERQ3}.
Interaction partners:
- Inhibitor of growth protein 2
- Ubiquitin-like protein FUBI
- Histone deacetylase complex subunit SAP30
Sequence:
MTFTFQSEDLKRDCGKKMSHQHVFSLAMEEDVKTADTKKASRILDHEKENTRSICLLEQKRKVVSSNIDVPPARKSSEELDMDKVTAAMVLTSLSTSPLVRSPPVRPNESLSGSWKEGGCVPSSTSSSGYWSWSAPSDQSNPSTPSPPLSADSFKPFRSPAQPDDGIDEAEASNLLFDEPIPRKRKNSMKVMFKCLWKNCGKVLSTAAGIQKHIRTIHLGRVGDSDYSDGEEDFYYTEIKLNTDSVADGLSSLAPVSPSQSLASPPTFPIPDSSRTETPCAKTETKLMTPLSRSAPTTLYLVHTDHAYQATPPVTIPGSAKFTPNGSSFSISWQSPPVTFTGIPVSPTHHPVGTGEQRQHAHTVLSSPPRGTVSLRKPRGEGKKCRKVYGMENRDMWCTACRWKKACQRFLD
Protein: Protein YIPF6 (YIP1 family member 6) (Q8BR70)
Organism: Mus musculus (Mouse)
Function: May be required for stable YIPF1 and YIPF2 protein expression.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96EC8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96EC8}. Note=Evenly distributed between cis- and trans-Golgi apparatus. Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. {ECO:0000250|UniProtKB:Q96EC8}.
Interaction partners:
- Protein YIPF1
- Protein YIPF2
- Trehalase
- Catalase
- Protein YIPF3
Sequence:
MAEAEDSPGEQEAAASKPLFAGLSDVSISQDIPIEGEITIPSRARAQEHDSSTLNESIRRTIMRDLKAVGRKFMHVLYPRKSNALLRDWDLWGPLILCVTLALMLQKSSIDGKNDGGGPEFAEVFVIIWFGAVTITLNSKLLGGNISFFQSLCVLGYCILPLNIAMLICRLLLLAGQGPINFMIRLFVVLLMFAWSVVASTAFLADSQPPNRKALAVYPVFLFYFVISWMILTFTP
Protein: Ataxin-10 (Neuronal beta-catenin-like protein) (Spinocerebellar ataxia type 10 protein homolog) (Q9ER24)
Organism: Rattus norvegicus (Rat)
Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15201271}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UBB4}. Midbody {ECO:0000250|UniProtKB:Q9UBB4}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P28658}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P28658}. Note=Localizes to the midbody during telophase. {ECO:0000250|UniProtKB:Q9UBB4}.
Interaction partners:
- IQ calmodulin-binding motif-containing protein 1
Sequence:
MAAPRMPPSRLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSTQAVELACRDPSQVEHLASSLQLITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLVLLFRELRVEQDSLLTAFRCGLQFLGNVASRNEDSQSIVWVHAFPELFMSCLNHPDKKIVAYCSMILFTSLNSERMKDLEENLNIAINVIEAHQKHPESEWPFLIITDHFLKSPELVEAMYGKLSNQERVTLLDIMIAKIVGDEQLTKDDISIFLRHAELIANSFVDQCRNVLKLTSEPQTEDKEALVTIRLLDVLCEMTSNTELLGYLQVFPGLMERVIDVLRVIHSVGKDSTNIFSPSDSLKAEGDIEHMTEGFKSHLIRLIGNLCYKNKENQDKVNELDGIPLILDSSNIDDNNPFMMQWVVYAVRNLTEDNSQNQDFIAKMEEQGLADASLLKKMGFEVEKSGDKLILKSNNDIPPP
Protein: Zinc finger protein ztf-16 (H2L008)
Organism: Caenorhabditis elegans
Function: Positively regulates the expression of ver-1 in the amphid sheath glia of amphid sensory neurons. Together with ehn-3, plays a role in somatic gonad development and is required for proper gonadal primordium assembly and somatic gonad precursor cell morphology.
Subcellular location: Nucleus {ECO:0000269|PubMed:22298710}.
Interaction partners:
- ShKT domain-containing protein
- Protein ver-1
- Serpentine Receptor, class Z
- C2H2-type domain-containing protein
- Homeobox protein ttx-1
- EF-hand domain-containing protein
- Delta-like protein
- Sex-determining transformer protein 1
- Forkhead transcription factor fkh-6
- Cell fusion protein aff-1
Sequence:
MDELNACTECGFTTTVFSEFQGHIEKHENEHSRSSSGEMSNSQTIEWGDGIQSSTPSPRSTPPSDPTPSPDSDEHLEHHISITEITNTLIKKEPGTKGQKTVHVCPHCNFTTCMSQHMKSHLEAHERHQGQMYQCDICKMQFSQKANMHRHRMRHSGVKPYECRFCKKRFFRKDQMQEHSMTHIKTGFGFDCPVSQCNMQFSQHNALRAHLEETHTISSTNPASCKRCNLMFANSRRLLLHFQTRHDDSESSPKKENTPKRKKLSNGNALPMDPANMSITEQLQRMVKSEFSPPNTDTSDNSTSSEFDKIPPSFPMANPDILLMCLNQMNQFNGFGENIPRPMLNIPNIPLPALHNIPAVAAIVKQDQVQLWSEQTSSSVSVSAPSPSEQSHSPPANESSLSLTEKEKSPTPEKEDEENVECCHCGMMFYDNTMYLLHKSLHSDGDPFKCALCGTQCGEKYMFTTHVIFADHSTQATTSA
Protein: Meiotically up-regulated gene 137 protein (O94478)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis and sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum.
Interaction partners:
- Protein hob1
- Calcium-transporting ATPase 1
Sequence:
MVSRFFSWTNEKPLGDQRAHLPDSFLELEQEIAIREEGLSKLFQATTIWIDSILKKVDGEDKEKCLACENLGKVMINHSKELPQDSSYGITLSQLGKANLKIGEHQTSLAYKARVCYLDFLKRYLVQAKDFHSARKKLESRRQAYESLLQKSFKEKKEDSRLEEDIRLALYKFEESTEQVKNRMIALKDVEADQYQQLTELIVYELNFFKESTGILNTIFNSQNSLTPQKKIQSSERSVENEFLASPMDPSLSKLFTKTTNTEKISPTPFSTPKRKSKKETVFVKAIYSFTGRNEKELDLHTGDVIQVSEQLGPDWYMGEKVNSKAEKLGNSGMFPVNYCTRIYDLHVQKSHETRSLERARSIRRIVSDDPRDYCSPIKQSPIQNLKFLDSDNSLLSSQNVEASSQPIKIRKPLPEIPNK
Protein: 2-oxoglutarate and iron dependent oxygenase domain containing 1 (A0A0A0MTR2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGKRPAEPGPARVGKKGKKEVMAEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDPFLHCVIPNFIQSQDFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILFEDFRSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLKPEKFTKVCEALEHGHVEWSSRGPPNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNFTGLKLHFLAPSEEDEMNDKKEAETTDITEEGTSHSPPEPENNQMAISNNSQQSNEQTDPEPEENETKKESSVPMCQGELRHWKTGHYTLIHDHSKAEFALDLILYCGCEGWEPEYGGFTSYIAKGEDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWDFSFIYYE
Protein: Complement component C6 (E9Q6D8)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTRHLTLCFILLVMLIDKSEACFCDHYPWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLCIKQETRECNLQTCPINCVLGDYGTWSDCDPCTEKQVKVKSVLRPSQFGGQPCTEPLVTFQPCVPSKLCKIEETNCKNKFLCDSGRCIPSKLECNGENDCGDNSDERNCGRTKPVCTRIYTPIPSVQLMGTGFHFLAGEPRGEVLDNSFTGGICKLVKTSRASNPYRVSANLENVNFEVQTIEDDLKTEFYKNLISFEKNKNEDSLSVDERTKFFPIPIFHFSEKNEHSHYSSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKATDLQLSDVFLKALVHLPLEYNSAVYSRIFDDFGTHYFTSGSLGGKYDLIYQFSRQELQNSGLTEEEAQNCVQYETKKLKFLYMEIHKEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSQQAAALAWEKGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLVRNIPCAVTKRNNLRRALQEYAAKFDPCQCAPCPNNGRPRLSGTECLCVCQSGTYGENCERRSPGYKSDAVDGNWGCWSSWSACNAAYRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVSIMENVGQPCINDDEEMKEVDLAEPEAESGCSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQRTSCLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDSWTPPISNSLTCEQAILTKSKDLCPPGQKQSGSKCICMSPEEDCSAYSEDLCIFDGGSSQYFTSSACKFLAGKCLNNTQSHFVHSGSCQEGLQLEWGLERLKLAVNSTKRVSCGYNTCYDWENCSAHTSNCVCLLPPQCSKDENQLYCVKIGSSMREKTVNICTLGAVRCANIKVEILNPGRCPD
Protein: RNA helicase (EC 3.6.4.13) (A0A0G2JY21)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MWMKKICSLLTEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPADRHPQCLCLSPTYELALQTGKVIEQMGKFHPELKLAYAVRGNKLERGQKVGEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: Ninja-family protein AFP2 (ABI five-binding protein 2) (ABI5-binding protein 2) (Q9LMX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a negative regulator of abscisic acid (ABA) response during germination through the ubiquitin-mediated proteolysis of ABI5/DPBF1.
Subcellular location: Nucleus {ECO:0000269|PubMed:18484180}.
Interaction partners:
- Protein ABSCISIC ACID-INSENSITIVE 5
- Probable glutamate carboxypeptidase AMP1
- Protein phosphatase 2C 37
Sequence:
MGEASRQQRAWNREMTVTTNLSLDIDKYPRDLLRGFMSENGGGRVFHGGETNCDDESTIELNLGLSLGGRFGVDKTPRKLKRSSSVLDTVPFNDSTVAEPENYTVGLERTTSLPAEMEEEWRKRKEMQSLRRMEAKRRRCEKQSFRVGNSDDQTVSFENERWVTASKSGFLQRHLVSSNRQVCGVDSDGGGATGGGSSSSLSELDNKNQQGSSNSCNDERSPKIVAGCSSNSGSQGTERPSVTRANKVNENENEKRVRSEDSVDRKGKGMATSTGLVDMPCVFTKGDGPNGRRVDGILYKYGKGEEVRIMCICHGSFLTPAEFVKHGGGGDVDRPLRHIVVNTSSSTF
Protein: Actin filament-associated protein 1-like 2 (AFAP1-like protein 2) (Q5DTU0)
Organism: Mus musculus (Mouse)
Function: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MERYKALEQLLTELDDFLKVLDQENLSSAAVLKKSGLSELLRLYTKSSSSDEEYIYMNKVSVNGEQNSASPDKVPEEQGPLTNGEPSQHSSAPQKSLPDLPPPKMIPERKQPTVPKIESPEGYYEEAEPFDRSINEDGEAVSSSYESYDEDENSKGKAAPYQWPSPEASIELMRDARICAFLWRKKWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLRGSSVVHKEKQVRKKGHKLKITPMNADVIVLGLQSKDQAEQWLRVIQEVSGLPSEGASEGNQYTPDAQRLNCQKPDIAEKYLSAAEYGITINGHPEIPETKDVKKKCSAGLKLSNLMNLGRKKSTSLEPPERSLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSSEEMGHWLGLLLSESGSKTDPEELTYDYVDAERVSCIVSAAKTSLLLMQRKFSEPNTYIDGLPSRDCQDDLYDDVEVSELIAVVEPAEEAAPAVDANSGSEPDRVYLDLTPVKSFLHSSSEAQAQASLPAVPHQDDVAETLTVDPKPGTTPEEPHTESPGDPEVQQRQPEVQESSEPIEPTPRITMVKLQAEQQRISFPANCPDTMASAPIAASPPVKEKLRVTSAEIKLGKNRTEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDKGVLAKLEQTLKKIDEECRMEESRRVDLELSIMEVKDNLKKAEAGPVTLGTTVDTTHLDNMSPRPQPKAATPNPPPDSTPVNSASVLKNRPLSVMVTGKGTVLQKAKEWEKKGAS
Protein: Nucleosome assembly protein NAP-1 (Q24150)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDAPAEGHVDPESCNEIEDEKSGSDCQSMPAYMNSVMRRQYLQQMVKMLPAPVQNRIVFLKNLQLQHLNIEAQFFEDVYKLEQKYQVQYQPLFDKRREIIEGKVDPAEEKPQWKEPESSTDNEADAEHFREALSSLKSIPKDAKGIPGFWLTVFRNTAIMSEMVQPHDEPAIRKLIDISIKYDNGHSYTLEFHFDKNEYFSNSVLTKQYVLKSTVDPNDPFAFEGPEIYKCTGCTINWEKKMNLTVKTIRKKQKHKERGAVRTIVKQVPTDSFFNFFSPPEVPSDQEEIDDDSQQILATDFEIGHFLRARIIPKAVLYYTGDIVDDEDDEDEEEYDENEEDEYDDDDAPPPKGPKSAGIKKQSPNDCPNQ