wanglab/gogpt-training-data huggingface dataset:
Protein: P antigen family member 4 (PAGE-4) (G antigen family C member 1) (PAGE-1) (O60829)
Organism: Homo sapiens (Human)
Function: Intrinsically disordered protein that potentiates the transcriptional activator activity of JUN. Protects cells from stress-induced apoptosis by inhibiting reactive oxygen species (ROS) production and via regulation of the MAPK signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12489849, ECO:0000269|PubMed:24559171, ECO:0000269|PubMed:25374899}. Nucleus {ECO:0000269|PubMed:24559171}. Mitochondrion {ECO:0000269|PubMed:25374899}. Note=Translocates to mitochondria in response to stress. {ECO:0000269|PubMed:25374899}.
Interaction partners:
- Transcription factor Jun
Sequence:
MSARVRSRSRGRGDGQEAPDVVAFVAPGESQQEEPPTDNQDIEPGQEREGTPPIEERKVEGDCQEMDLEKTRSERGDGSDVKEKTPPNPKHAKTKEAGDGQP
Protein: Protection of telomeres protein 1a (AtPOT1a) (AtPot1) (Protection of telomeres protein 1) (Q56Y52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the positive regulation of telomere length. Binds RNA non-specifically. Binds specifically single-stranded telomeric DNA. Not required to recruit telomerase to telomeres, but stimulates TER1 RNP repeat addition processivity.
Subcellular location: Nucleus {ECO:0000305|PubMed:17627276}. Chromosome, telomere {ECO:0000269|PubMed:17627276}. Nucleus, nucleolus {ECO:0000269|PubMed:30834599}. Cytoplasm {ECO:0000269|PubMed:30834599}. Note=Localizes to telomeres in S-phase (PubMed:17627276). Localizes to cytoplasmic foci (PubMed:30834599). {ECO:0000269|PubMed:17627276, ECO:0000269|PubMed:30834599}.
Interaction partners:
- Telomerase reverse transcriptase
- CST complex subunit CTC1
- Telomere repeat-binding factor 1
- CST complex subunit STN1
- CST complex subunit TEN1
- H/ACA ribonucleoprotein complex subunit 4
- Mediator of RNA polymerase II transcription subunit-like protein
- Telomere repeat-binding protein 1
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
- Small ribosomal subunit protein eS17y
Sequence:
MAKKRESPKLIKIKDAIKLINQQVSLIGIVLEQREPKQCRNNDWICTLRIIDDTYPSPGLTVNVFSKTLEQLPQIKNHDDMILFTRIKMQTFDSGERVNAACSRWVSSFALFEGVDFVCYQCSTNFHEEEALYKSAMDDLRKVFAGCSQVIKAMQSISYRTKPCSEVFSFLREIKIGKRFDLVCRILHADEDTSAVFVWDGTDAPPASILAKRSEEDKAFSSLSVHTLLSRDVLLSFPTVGTILRVHLSSHLFYRVKPGDWVKLYHLLCEVDRGSWVIKVTSSTKVHHLAQDDRLVEKIMRIYDKRLSSKLGHISFWCFPSPPGLTETDDNCAPFVTLMDIITFPKVTCKYRCIVRVVAAYPWQVEDFCSDENRRHHQVLLTLEDSTATLEAFLCNKDAEYFWGLGFQDTETLRKKRNWLLGIRESSNFVAPRNPPWIECCILSYYTNKADPWNTRLYRIFGTRLLH
Protein: (thale cress) hypothetical protein (A0A384KPL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNIVIENNPSSRRLSDLGVMSWPKWSCQPGKYALVFEERETCYLVKGKVKVYPKGSSEFVEFGAGDLVTIPKGLSCTWDVSLFIDKHYKFDPPTSP
Protein: Ribonuclease mitogillin (EC 3.1.27.-) (Allergen Asp f I) (Allergen I/a) (IgE-binding ribotoxin) (Major allergen Asp f 1) (allergen Asp f 1) (P67875)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.
Subcellular location: Secreted.
Interaction partners:
- Peroxiredoxin Asp f3
- Major allergen Asp f 2
- Allergen Asp f 4
- Superoxide dismutase, mitochondrial
- Crh-like protein 5
Sequence:
MVAIKNLFLLAATAVSVLAAPSPLDARATWTCINQQLNPKTNKWEDKRLLYSQAKAESNSHHAPLSDGKTGSSYPHWFTNGYDGNGKLIKGRTPIKFGKADCDRPPKHSQNGMGKDDHYLLEFPTFPDGHDYKFDSKKPKEDPGPARVIYTYPNKVFCGIVAHQRGNQGDLRLCSH
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (O18680)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Serine hydroxymethyltransferase
- Sarcosine dehydrogenase
- Glycine cleavage system P protein
- LD34157p
- Alanine--glyoxylate aminotransferase
- D-amino acid oxidase 2, isoform A
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- Glycine N-methyltransferase
Sequence:
MQCPFLNRFTASFIRNYAETLCQSYGSHCPVVGKTLVSGEKKLSLVAASVTRSHSTGANAHANAGGPATANATAPVSAPASADPGKASAKETFPYERFFNEQIMKKKRDHSYRVFKKVNRLAGDGLFPHALEYSERTEKPITVWCSNDYLGMSAHPGVKRAVQDALNRHGSGAGGTRNISGNSLHHERLESKLAELHQKEAALLFTSCFVANDSTLFTLAKLLPGCEIFSDAGNHASMIMGIRNSGVPKHIFRHNDVDHLHQLLKQTDKSVPKIVAFETVHSMTGAICPLEELLDVAHEHGAITFIDEVHAVGLYGDHGAGVGERDGVLHKMDIISGTLGKAFGNIGGYIAGTHNLVDMIRSYAAGFIFTTSLPPTVLCGALEAVNILASEEGRQLRHLHQRNVSYLKSLLKREGFPVEETPSHIIPIKIGDPLKSSQISNVLIEQFGHYLQSINYPTVARGQEKLRLAPTPFHTFEMMNALVTDLKKVWEMVDLSTNVPLSPNACMFCNSESCWHQDTSPDLECGIPNCPRLEISLAA
Protein: PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) (F6V107)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIK
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Methylisocitrate lyase) (MICA) (EC 4.1.3.30) (Threo-D(S)-isocitrate glyoxylate-lyase) (P28240)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20457600, ECO:0000269|PubMed:8870676, ECO:0000269|PubMed:9370278}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24520859, ECO:0000269|PubMed:24665361}. Vacuole {ECO:0000269|PubMed:17651441, ECO:0000269|PubMed:20457600}. Note=Localizes in extracellular vesicles during growth on lown glucose. When glucose is added to glucose-starved wild-type cells, levels of extracellular ICL1 get reduced. Targeted to the vacuole for degradation in 3-day-starved cells. {ECO:0000269|PubMed:20457600, ECO:0000269|PubMed:24520859, ECO:0000269|PubMed:24665361}.
Interaction partners:
- Malate synthase 1
- Malate synthase 2
- Aconitate hydratase, mitochondrial
- Alanine--glyoxylate aminotransferase 1
- Phosphoenolpyruvate carboxykinase
- Fructose-1,6-bisphosphatase
- Isocitrate dehydrogenase cytoplasmic
- Glyoxylate reductase 1
- Acetyl-coenzyme A synthetase 1
- Citrate synthase 3, mitochondrial
Sequence:
MPIPVGNTKNDFAALQAKLDADAAEIEKWWSDSRWSKTKRNYSARDIAVRRGTFPPIEYPSSVMARKLFKVLEKHHNEGTVSKTFGALDPVQISQMAKYLDTIYISGWQCSSTASTSNEPGPDLADYPMDTVPNKVEHLFKAQLFHDRKQLEARSKAKSQEELDEMGAPIDYLTPIVADADAGHGGLTAVFKLTKMFIERGAAGIHMEDQTSTNKKCGHMAGRCVIPVQEHVNRLVTIRMCADIMHSDLIVVARTDSEAATLISSTIDTRDHYFIVGATNPNIEPFAEVLNDAIMSGASGQELADIEQKWCRDAGLKLFHEAVIDEIERSALSNKQELIKKFTSKVGPLTETSHREAKKLAKEILGHEIFFDWELPRVREGLYRYRGGTQCSIMRARAFAPYADLVWMESNYPDFQQAKEFAEGVKEKFPDQWLAYNLSPSFNWPKAMSVDEQHTFIQRLGDLGYIWQFITLAGLHTNALAVHNFSRDFAKDGMKAYAQNVQQREMDDGVDVLKHQKWSGAEYIDGLLKLAQGGVSATAAMGTGVTEDQFKENGVKK
Protein: Uncharacterized protein (Q3UWC5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
AGEDFAKFVTLGQKGDKWFCITPCSAGYSTSKNCSYGKCQLQRSGPQCLCLITDTHWYSGENCDWGIQKSLVYGLGGAGVAVLLVILVILLVFSIRFRKDAQRQRSRVSEMYKWGEEEGRASPGTFHNFGFDHNEERENYMPLDSVYNTFQPSLNHINPERKIQIQRPQVVMTSL
Protein: Protein IRREGULAR XYLEM 15 (AtIRX15) (Q9SNE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for xylan biosynthesis, but not directly involved in catalyzing the addition of sugars to the growing polymer.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Also located in an unknown intracellular compartment that may have some role in the transport of cell wall polysaccharides into the cell wall. {ECO:0000269|PubMed:21251108, ECO:0000269|PubMed:21288268}.
Interaction partners:
- Probable beta-1,4-xylosyltransferase IRX10
- Probable galacturonosyltransferase 12
- Beta-1,4-xylosyltransferase IRX9
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Beta-1,4-xylosyltransferase IRX14
- Probable galacturonosyltransferase-like 1
- Cellulose synthase A catalytic subunit 8
- Cellulose synthase A catalytic subunit 4
- Probable glucuronoxylan glucuronosyltransferase IRX7
- Cellulose synthase A catalytic subunit 7
Sequence:
MKNGSGNTNTKLILLHPYIQKQTSTTRLWLLAFVSFFTIVFLLTLLYTRDTIPSKNTSVAAAVAAVVTGGSTPSASSPISNSNLPTSAINALLHYASRSNDSFHMSYGEMKSISDVLRRCAPPCNLLVFGLTHETLLWKSLNHNGRTVFIEENRYYAAYFEEIHPEIDVFDVQYTTKAHEAGELVTAAKEAAGNECRPVQNLLFSDCKLGLNDLPNHVYDVDWDVIFVDGPRGDAHEGPGRMSSIFTAAVLARSKKGGTPKTHVFVHDYYRDVERLCGDEFLCRENLVESNDLLAHYVLDKMDKNSTKFCNGRKKRSVSSLS
Protein: Phytoene synthase (Q4W8B5)
Organism: Brevundimonas sp. NBRC 101024
Interaction partners:
Sequence:
MSDAVLDHSRQSMEQGSKSFAAAARLFPAAIRDDAWMFYAWCRHCDDEIDGQVLGHGAVGIDPVLAGRKLVELRERTAAALAGEPQTDPVFTAFQRVAARHAIPAEEAMDLLQGFEMDVEGRRYDTLEDTLDYAYHVAGVVGVMMARIMGVQDAPTLRRAQDLGLAFQLTNIARDVVEDAKGGRVYLPGQWLDEAGVPRDQVDQPRHRQAVAHTAQRLVAAAEPYYASARWGLRDLNPRSAWAVATARGVYRAIGRHVSRSGATAWDGRTSVDKAGKLALVGRGALITLWCKTLDAWREPPPRPALWTHI
Protein: Capsid fiber protein (Gene product 8.5) (gp8.5) (Head fiber protein) (Protein p8.5) (B3VMP4)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Protein that forms the 55 capsid fibers. These fibers are not always present and may have been lost in some lab strains. They may enhance the attachment of the virions onto the host cell wall.
Subcellular location: Virion {ECO:0000269|PubMed:11562162, ECO:0000269|PubMed:409854}.
Interaction partners:
Sequence:
MMVSFTARAKSNVMAYRLLAYSQGDDIIEISHAAENTIPDYVAVKDVDKGDLTQVNMYPLAAWQVIAGSDIKVGDNLTTGKDGTAVPTDDPSTVFGYAVEEAQEGQLVTLVISRSKEISIEVDDIKDAGDTGKRLLKINTPSGARNIIIENEDAKALINGETTNTNKKNLQDLLFSDGNVKAFLQATTTDENKTALQQLLVSNADVLGLLSGNPTSDNKINLRTMIGAGVPYSLPAATTTTLGGVKKGAAVTASTATDVATAVKDLNSLITVLKNAGIIS
Protein: SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk) (P50745)
Organism: Rattus norvegicus (Rat)
Function: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase.
Interaction partners:
- Tyrosine-protein kinase JAK2
Sequence:
MAGRTQGKHRPRVRTCPSLVPFDNPCWPPSHQPLPLQVGAPGHRVTSFLSGRAWPSYIPKGKHGLPGPRYVPDPWSLGVLGHVAPLRVTTTIFLPGASPGVMLDPACQKTDHFLSCYPWFHGPISRVRAAQLVQLQGPDAHGVFLVRQSESRRGEYVLTFNLQGRAKHLRLVLTERGQCRVQHLHFPSVVDMLRHFQRSPIPLECGAACDVRLSGYVVVVSQAPGRKPKVVSRGGVTASTARTKLPSWLRLLHGVIHVISPGSSNTVLFPFSLPHWDSELGHPHLSSAGCPPGHGAEALRGQVTPPEQIFHLVPSPEELANSLRQLELESVSSARDSDYEMDSSSRSHLRAIDNQYTPLSQLCREANL
Protein: C3H1-type domain-containing protein (O02174)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPSSVSYSPSNPGIRIVKRKPKPEAVAAAAAVPTAIYSGKRHATDDGEDAGLAALKLKPNRGILRGPAISNLNQRGTRRLIFADTRGLPLVHVKEIERIAAIHSNVADYRCSERNEAAAFGQEMEVFEDVEWSLVPVKRSKPARSEMSESGLREERRIEEEGIMRGAMFGMCQLEDNPALNEQAAVDRANYTPTIIPTVSVPSEPTTLATIRDLPLPGRPPRVRPQDLLLQVKPNQGFHTLPLYHSQRPENPRRPMYAQQQQQQSAHQTPTPHIQQVFQETEPVTNYYTATTSVPETPEPAPAAQPASRFELPSNLKEMLNQLKKKGFVSSDETPSPTTSAPPPVDPLAAAMQTAQQMMLQQGNTYASEEVPQDYPMDGYVATFATPEMMAQERRQDSRNSEGWTQSGWKIPEPCVYFISRPGGCNRGDQCRFIHDEEMRRQKMAELPPRGPNHHHDNFRGGRGRGFRGGYNNRNNYNNHHDRDFRDNAGGNRGRFGDTEGFRGARYARGGFAPRNNSRFDQKPAYNDDGGHLGSPNAHGSQYQDPVPTKRARVSRFDRQGEDDAPGQDMDQRPPRRNRFDEQPPRRTFRSRFDQQADHDEMSQA
Protein: Neprilysin-4 (EC 3.4.24.11) (Q8T062)
Organism: Drosophila melanogaster (Fruit fly)
Function: Metalloendoprotease which cleaves peptides at the amino side of hydrophobic residues - such as the hormones Akh and Dh31, and the neuropeptides Allatostatins (AST1, AST2, AST3 and AST4), Crz, Drosulfakinins (DSK-I and DSK-II), Lk, sNPF and the tachykinin peptides TK-1, TK-2, TK-4 and TK-5. Functions in female fertility, memory formation and may also act in regulating insulin signaling and food intake. Likely to be involved in controlling feeding behavior and the expression of insulin-like peptides by cleaving various regulatory peptides that include certain Drosulfakinins, Allatostatins and tachykinin peptides. Required in females for normal patterns of egg laying and hatching. Required in the dorsal paired medial neurons for the proper formation of long-term (LTM) and middle-term memories (MTM). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep2 and Nep3, in normal LTM formation.
Subcellular location: [Isoform A]: Cell membrane {ECO:0000269|PubMed:19880729, ECO:0000269|PubMed:27919317}; Single-pass type II membrane protein {ECO:0000305}. Sarcoplasmic reticulum {ECO:0000269|PubMed:22583317}. Note=In larval muscles, localizes to both the cell surface and sarcoplasmic reticulum membranes that are continuous with the nuclear membrane. {ECO:0000269|PubMed:22583317, ECO:0000269|PubMed:27919317}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm {ECO:0000269|PubMed:19880729}.
Interaction partners:
- Adenylosuccinate synthetase
- Insulin-degrading enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
Sequence:
MSRHSQLKLAMPSVHGAPATAPGSPMNAKARSVKLGLGVNQRTGRVQWCPGLTCCKMLLLLPVVMLPLTLVLILIMRLDGMLAALQLNEQRMRDLRNSHSEVPVYMEDYEALLPEGSTYNDLINEEFILPASKRTQLQILAAERARRCQPYRYGNGESMELEERNTLMKDSRTSFLPLGIPRECLGSGIELDIKPIDEEAYQRQKKRYQDIAPYWLEKIRIRERREAERHAEEASAEISEATAALQSFWNEEGTREGIRMTQAKTMKRYMDNKVDPCVDFYKYACGNWERLHPIPKDKAGFDTFEMLRESLDLVLRNLLEKNTPVHSAAELRKSPVRNTLFKLNEQGEGEGEADQAAELTAERLRRHIVSKRQLLNRVLVRYKRYTNGTKRKRLIETPRERTKEEEAAPPVVLPKDKTKDKSDNEEQLHVPTDFLKPHQDAQLKAKNLYRSCVNSAVLAKRGLEPLHTLIRELGGWPVLESQWSESNFNWQVLAATLRRYNNDILIVQWVGADIKNSEENIVQFDQTGLGLPTREYFLQPSNAKYLQAYQRYMAEVMHKMGASKADAQRVASELVAFETQLAGITAPAEQRLNVTKLYKRMTLDQLQAVVPEIKWRAYLQSLQDREVLGTEEVVIYAVEYMSKLVTLLDETDPRTVSNYMMWRFVRHRINNVDDRFDDIKQSFYHALFGREESPQRWKVCIAQVNTNMGMAVGSMFVSRYFDNNSKRDTLRMTHDLQQAFRDILKTTDWLDDTTKQLAEEKVNAMSLKIGYPDFILNPSELNSKYAGIEIYPEKYFENTLNVLLHTAKTEQAKLHERVNKTNWQTAPAIVNAYYSRNKNQIMFPAGILQPPFYHRHFPKSLNFGGIGVVIGHELTHGFDDKGRLFDRNGNIHKWWTDSSIRGFDERARCIIAQYSNYTVEEVGIVLNGESTQGENIADNGGLRQAFHAYQRWLKEHPSEVSDEILPGLNMTGPQLFFLNFGQVWCGAMRPEAIRNKLNTAIHSPGRFRVIGTLSNSVDFAREFNCPLGSPMNPQKKCSVW
Protein: Keratin-associated protein 10-4 (High sulfur keratin-associated protein 10.4) (Keratin-associated protein 10.4) (Keratin-associated protein 18-4) (Keratin-associated protein 18.4) (P60372)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 10-7
- Keratin-associated protein 10-9
- Keratin-associated protein 10-8
- Keratin-associated protein 10-11
- Keratin-associated protein 10-5
Sequence:
MSVCSSDLSYSSRVCLPGSCDSCSDSWQVDDCPESCCEPPCCAPSCCAPAPCLSLVCTPVSRVSSPCCPVTCEPSPCQSGCTSSCTPSCCQQSSCQLACCASSPCQQACCVPVCCKTVCCKPVCCVPVCCGDSSCCQQSSCQSACCTSSPCQQACCVPICCKPVCSGISSSCCQQSSCVSCVSSPCCQAVCEPSPCQSGCISSCTPSCCQQSSCQPACCTSSSCQQACCVPVCCKTVCCKPVCSEDSSSCCQQSSCQPACCTSSPCQQACCVPVCCKPVCCKPVCSVPICSGASSLCCQQSSCQPACCTSSQSQQGCCVPVCCKPVSCVPVCSGASSSCCQQSSCQPACCTTSCCRPSSSVSLLCRPVCRPACCVPVPSCCAPTSSCQPSCCRPASCVSLL
Protein: Ryanodine receptor type 3 (Q9R273)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
NYWDKFVKRKVINKYGDLYGAERIAELLGLDKNALDFSPVEEAKAEAASLVSWLSSIDMKYHIWKLGVVFTDNSFLYLAWYTTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDDDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVREDMETKCFICG
Protein: Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (O73613)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- TNF receptor-associated factor
- TNF receptor-associated factor
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Uncharacterized protein.
- Mitogen-activated protein kinase kinase kinase 7-interacting protein 3 homolog isoform X1
- Protein kinase domain-containing protein
- Uncharacterized protein.
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Protein kinase domain-containing protein
Sequence:
MSATSAEMIETPPVLNFEEIDYKEIEVEEVVGRGTFGVVCKAKWRGKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCAQGVAYLHSMKPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPPQRPSMEEIVKIMTHLMQYFPGADVSLQYPCQYSDEGQSNSATSTGSCIDITSTNTSNKSDIHIEPGDFQASASNDTIKRIESKLAQHLKNQAKQTGESGRLSLPPSRGSSVESLSEIRGRPPSTLGTSEGKRMSADMSELEARISASTAYVKPKRGHRKTASFGNILDVPEIIITAGNGQQRRRSVQDLTIVGTESSQESRNSSRSSSPSVRMITTSGPTPDKPPRGLPWAPDESSDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELIAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
Protein: FI24038p1 (Zinc/iron regulated transporter-related protein 88E) (Q9VFA2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Zinc transporter ZIP11
- Zinc/iron regulated transporter-related protein 102B, isoform E
- Uncharacterized protein, isoform A
- IP18018p
- LD23375p
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter 63C, isoform F
- Zinc transporter 33D, isoform B
- RE54080p
- LD05335p
Sequence:
MSLPTDGLNMEITPSPTLAATSRGDLEKVLAMLVLGLGSLLFGLLPAFISERNRRRFPLTASLLLCFGAGILLATALVHILPEVREQMDSKFAEVAMCGGFFIIYFIDEFIHYFFGEAIQHTHAHDAETPATEPPRRPTNDNGYGAVDERAPLLSAEPNTSHGHSHHHSHDHDHNHPASASGCNDASVEDANARICHTSHTEPCAQSMTGTLGLFVALSLHSAIEGLAIGVQNSSTKVLFLLGAVACHKFVMGFCLGLEFRSNPQTSFRAQFVGISVFALGAVIGIGLGMLIVDVPAAWSSKTLPIVQALAGGTLFYVTVCEVIPREKARWHSNSTRRWAGFAQFATVLAGFATMCIINFYLSDED
Protein: Histone-lysine N-methyltransferase SUVR4 (EC 2.1.1.-) (EC 2.1.1.366) (Protein SET DOMAIN GROUP 31) (Suppressor of variegation 3-9-related protein 4) (Su(var)3-9-related protein 4) (Q8W595)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase that converts monomethylated 'Lys-9' of histone H3 (H3K9me1) to dimethylated 'Lys-9' (H3K9me2) in the absence of bound ubiquitin, and to trimethylated 'Lys-9' (H3K9me3) in the presence of bound ubiquitin. Acts in a locus-specific manner and contributes to the transcriptional silencing of pseudogenes and transposons. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associates with euchromatic regions. {ECO:0000250}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40y fusion protein
- Histone-lysine N-methyltransferase ATX5
- Putative inactive histone-lysine N-methyltransferase family member SUVH10
- Histone H3-like centromeric protein CENH3
- Histone H3-like 4
- Histone H3-like 3
- Histone H3-like 1
- Histone H3-like 5
- Histone H3-like 2
- Histone-lysine N-methyltransferase ATXR6
Sequence:
MISLSGLTSSVESDLDMQQAMLTNKDEKVLKALERTRQLDIPDEKTMPVLMKLLEEAGGNWSYIKLDNYTALVDAIYSVEDENKQSEGSSNGNRGKNLKVIDSPATLKKTYETRSASSGSSIQVVQKQPQLSNGDRKRKYKSRIADITKGSESVKIPLVDDVGSEAVPKFTYIPHNIVYQSAYLHVSLARISDEDCCANCKGNCLSADFPCTCARETSGEYAYTKEGLLKEKFLDTCLKMKKEPDSFPKVYCKDCPLERDHDKGTYGKCDGHLIRKFIKECWRKCGCDMQCGNRVVQRGIRCQLQVYFTQEGKGWGLRTLQDLPKGTFICEYIGEILTNTELYDRNVRSSSERHTYPVTLDADWGSEKDLKDEEALCLDATICGNVARFINHRCEDANMIDIPIEIETPDRHYYHIAFFTLRDVKAMDELTWDYMIDFNDKSHPVKAFRCCCGSESCRDRKIKGSQGKSIERRKIVSAKKQQGSKEVSKKRK
Protein: Regulator of ribonuclease activity A (P0A8R0)
Organism: Escherichia coli (strain K12)
Function: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribonuclease E
- Regulator of ribonuclease activity B
- ATP-dependent RNA helicase SrmB
- Cell division protein FtsN
- ATP-dependent RNA helicase RhlB
- Polyribonucleotide nucleotidyltransferase
- RNA-binding protein Hfq
Sequence:
MKYDTSELCDIYQEDVNVVEPLFSNFGGRASFGGQIITVKCFEDNGLLYDLLEQNGRGRVLVVDGGGSVRRALVDAELARLAVQNEWEGLVIYGAVRQVDDLEELDIGIQAMAAIPVGAAGEGIGESDVRVNFGGVTFFSGDHLYADNTGIILSEDPLDIE
Protein: Formin 3, isoform B (A8JNM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Profilin
- Cdc42 homolog
- Ras-like GTP-binding protein Rho1
- Cofilin/actin-depolymerizing factor homolog
- IP04855p
- Rho-related BTB domain containing, isoform B
- RE12101p
- AT17867p
- Anillin
- Protein spire
Sequence:
MDSRIGLDYIVENRDYIAKLGAALDTQNATVKKQVFELLSALCAYSPDGYARAIETLEFYKNLKKQRYRFKIVINELELSSAAAHPPLDYQAALLAFINCVIISAATLQERIRIRNEFIGLKVLPLLNNLRLLEAGNVESSASPSPPPSLSSESASSATSPVSGSASTSVTPSPSPLHLQRRLTFCGSLSRYSCAALQLVQNLKKVAQSVGDIIVQLDVFVEQQECDEAQSLQAPDGINLNSHLDVFYAILRQVADTPQEVPFLNILQHLLRIDPKEPLSDIIWDTTERLVHRATLLESHEDSVRLLRTPSSQKFACQSCRGSDASSPTRKPSQPVGVSAKTTPPPPPPPMAPAAPPPPPPPINGAAPPPPPPPMINGGALPPPPPPPSMQMASRPRTPDPLAAEAVATAILLPQQDTPAPKAKMKTINWGKIPHNKVLGKQNIWSIVASNHQDSPMQDIDWNEMEGLFCLQTASAQGSPKLGRDGSQAAAGSNGCDTLDRKSKKESTEITLLDGKRSLNVNIFLKQFRTSNDDIIQLIRQGAHEEIGAERLRGLLKIMPEVDELDMLKGFNGDKARLGNAEKFLLQLLEVPNYKLRIESMLLKEEFAANVAYLEPCINSMLYAGDDLLNNKTLQEVLYMVVVAGNFLNSGGYAGNAAGVKLSSLQKLTDIRANKPGMNLIHFVALQAEKRNPELLQFTGQLSNLESASKTTSEQINNEINTLDGRIRRIARQIEQPATDVDIKEQMADFLQAAESELSVLQAGMKQVESMRLKMSEFFCDDAATFRLEECFKIFHNFCDKFKQAVKENERRQQQEQQATLRRKQREEQLARRARQIGQAGTPVSDSEHSFLGDAIFDPRASPALSRRHLGSGEISNGFIRLEQDGASPDITPNGSLRRRRSRVLAEEDDLMEFLRSSTGPHHDGHNSRERKAAYGSLDRSWARRARSGSSSRKRPDLLNIDFGMDRERASSPAPLLQQQQQNVQERLQSPLASTAGTPTTAANTPTGSGSAIAQTPSNNEDAKPRISREWRQKIETWLQSNESDEKQNEEYRRKRRLVNANRRSLENETENERKLDPLPEEKILPSTTTATPTNTPTTTNPTNSTNRMDQESGKYQRVYADWKPSRTLEQTDVVANLQAIADAQPHDALRQHRRQRSQEQPSPIALQSIAEEDRRKSLIQKQGERDKSNERLQIYIRRSSSRELQPAKTEEHPLPPKSPKPQVSDDTFASLLSHHKTQNEMQGSSKDVDADNIETPPVSRRVIATPTTTVVTVSMTDKPKAATEEKINPAEQDAPGHFDRHALARRTRRYKRPTDYSSGNEEALTTSTAEAKTSPSKPEPPAPEKSKQKERTINKLEKVGRHISSINQEDVREAIRNLKSPTGTPERPWSPPRDITPSKLKLSASGHHELNDEGFEETQSLVSDTPSHGKGESTNSSCNEGVNETPARQRPMQKQKPTTTSISQMGSRLADRLQQARMKSSGSSGSAASKSQNQIPATQTATVKRSLSASRPLRMPNGQPLASAAPLRSASTVRRSPQEQQVLAGVERSSSRNSLRSSRSSINSGASTQTVVRRLPAVQRAGATVSVDSSPSKRPLAAQNLRPTQGRGVPASRSSSSGSSVGPSVILVRSKMSNTAPKSSIHGSTSFKENQSQSQPQSQSRMSAARSVVLVKNALNQQQQARMSANPSPQQRSTSSSRSVSSFMRPTASSATKRQK