wanglab/gogpt-training-data huggingface dataset:
Protein: Immunoresponsive gene 1,-like (Zgc:154020) (A0JMM8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cis-aconitate decarboxylase
- Macrophage-expressed gene 1 protein
- Aminomethyltransferase
Sequence:
MLSAVQRSSRYLTSFSAARGLHKSALDVAERPAPEETVTSSFGRFIQSVQPKNLTPTVLQRSKRMVLDSIGVGLVGSTTEVFDLALQHCQHMYASDDISFVYGRQGVKLSPTLAAFVNGVAAHSMDFDDTWHPATHPSGAVLPALLAISDMLHSNSKPSGLDFLTAFNVGIEIQGRLMRFSNEAHNIPKRFHPPSVVGTLGSAAACARLLSLDRNQASNALAIAASLAGAPMANAATQSKPLHIGNASRLGLEAALLASRGLEASPLVLDAVPGVAGFSAFYEDYAPRPIGSPEEDEHSFLIESQDIAFKRFPAHLGMHWIADAASVVHKTLVGLKGGSISPNLVQDILLRVPLSKYINRPFPESEHQARHSFQFNACTALLDGEVTVQSFHPEAIQRPELHALLSRVRLEHPSDNPANFNIMYGEVEVTLVTGDVLRGRCDTFYGHWRNPLSQESLHKKFRNNAGTVLSTEKVERLIEAVESLDRSDDCKQLLAQLQ
Protein: Bifunctional F420 biosynthesis protein FbiB [Includes: Coenzyme F420:L-glutamate ligase (EC 6.3.2.31) (EC 6.3.2.34) (Coenzyme F420-0:L-glutamate ligase) (Coenzyme F420-1:gamma-L-glutamate ligase); Dehydro-coenzyme F420-0 reductase (EC 1.3.8.17)] (P9WP79)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0.
Interaction partners:
- Phosphoenolpyruvate transferase
- Phosphoenolpyruvate guanylyltransferase
- F420-dependent glucose-6-phosphate dehydrogenase
- Deazaflavin-dependent nitroreductase
- FO synthase
- F420-dependent hydroxymycolic acid dehydrogenase
- Putative F420H
- F420H
- Probable cytoplasmic peptidase PepQ
- F420H
Sequence:
MTGPEHGSASTIEILPVIGLPEFRPGDDLSAAVAAAAPWLRDGDVVVVTSKVVSKCEGRLVPAPEDPEQRDRLRRKLIEDEAVRVLARKDRTLITENRLGLVQAAAGVDGSNVGRSELALLPVDPDASAATLRAGLRERLGVTVAVVITDTMGRAWRNGQTDAAVGAAGLAVLRNYAGVRDPYGNELVVTEVAVADEIAAAADLVKGKLTATPVAVVRGFGVSDDGSTARQLLRPGANDLFWLGTAEALELGRQQAQLLRRSVRRFSTDPVPGDLVEAAVAEALTAPAPHHTRPTRFVWLQTPAIRARLLDRMKDKWRSDLTSDGLPADAIERRVARGQILYDAPEVVIPMLVPDGAHSYPDAARTDAEHTMFTVAVGAAVQALLVALAVRGLGSCWIGSTIFAADLVRDELDLPVDWEPLGAIAIGYADEPSGLRDPVPAADLLILK
Protein: Myosin-1 (Myosin heavy chain 1) (Myosin heavy chain 2x) (MyHC-2x) (Myosin heavy chain, skeletal muscle, adult 1) (Q5SX40)
Organism: Mus musculus (Mouse)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin-2
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-4
- Troponin T, fast skeletal muscle
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Titin
- Myosin light chain 3
- Myosin regulatory light chain 11
- Alpha-actinin-3
Sequence:
MSSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVDAKESFVKATVQSREGGKVTAKTEGGTTVTVKDDQVYPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGYLARVEYQKMVERRESIFCIQYNVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE
Protein: D-lyxose ketol-isomerase (EC 5.3.1.15) (D-lyxose isomerase) (L-ribose isomerase) (A3E7Z6)
Organism: Cohnella laeviribosi
Function: Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose. Shows weak activity with D-mannose and L-ribose.
Interaction partners:
Sequence:
MRGTEWREARDRVAEMFRKAGIALTPSELEKVEVADFGLGNLAVQGLQLVTYINTDRYCAKELALFPHQTCPEHLHPPVGGDPGKMETFRCRWGKVFLYVEGEPAASVQAAVPPGSEAYYTVFHEIVLTPGEQYTIPPGTKHWFQGGPEGAIVSEFSSTSRDEFDIFTDPKVERMPVIEFDD
Protein: Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (P61626)
Organism: Homo sapiens (Human)
Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Subcellular location: Secreted.
Interaction partners:
- Myeloperoxidase
- Myeloblastin
- Lysozyme-like protein 1
- Lactotransferrin
- Fibrinogen alpha chain
- Apolipoprotein A-I
- Cathepsin G
- Chitotriosidase-1
- Beta-2-microglobulin
- Neutrophil elastase
Sequence:
MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
Protein: NACHT, LRR and PYD domains-containing protein 2 (Nucleotide-binding site protein 1) (PYRIN domain and NACHT domain-containing protein 1) (PYRIN-containing APAF1-like protein 2) (Q9NX02)
Organism: Homo sapiens (Human)
Function: Suppresses TNF- and CD40-induced NFKB1 activity at the level of the IKK complex, by inhibiting NFKBIA degradation induced by TNF. When associated with PYCARD, activates CASP1, leading to the secretion of mature pro-inflammatory cytokine IL1B. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and CASP1 and whose function would be the activation of pro-inflammatory caspases.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15030775, ECO:0000269|PubMed:15456791}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 1
- Caspase-1
- NLR family CARD domain-containing protein 4
- Interferon-inducible protein AIM2
- Pyrin
- NACHT, LRR and PYD domains-containing protein 12
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 6
- Caspase recruitment domain-containing protein 8
- Caspase-5
Sequence:
MVSSAQMGFNLQALLEQLSQDELSKFKYLITTFSLAHELQKIPHKEVDKADGKQLVEILTTHCDSYWVEMASLQVFEKMHRMDLSERAKDEVREAALKSFNKRKPLSLGITRKERPPLDVDEMLERFKTEAQAFTETKGNVICLGKEVFKGKKPDKDNRCRYILKTKFREMWKSWPGDSKEVQVMAERYKMLIPFSNPRVLPGPFSYTVVLYGPAGLGKTTLAQKLMLDWAEDNLIHKFKYAFYLSCRELSRLGPCSFAELVFRDWPELQDDIPHILAQARKILFVIDGFDELGAAPGALIEDICGDWEKKKPVPVLLGSLLNRVMLPKAALLVTTRPRALRDLRILAEEPIYIRVEGFLEEDRRAYFLRHFGDEDQAMRAFELMRSNAALFQLGSAPAVCWIVCTTLKLQMEKGEDPVPTCLTRTGLFLRFLCSRFPQGAQLRGALRTLSLLAAQGLWAQTSVLHREDLERLGVQESDLRLFLDGDILRQDRVSKGCYSFIHLSFQQFLTALFYTLEKEEEEDRDGHTWDIGDVQKLLSGVERLRNPDLIQAGYYSFGLANEKRAKELEATFGCRMSPDIKQELLRCDISCKGGHSTVTDLQELLGCLYESQEEELVKEVMAQFKEISLHLNAVDVVPSSFCVKHCRNLQKMSLQVIKENLPENVTASESDAEVERSQDDQHMLPFWTDLCSIFGSNKDLMGLAINDSFLSASLVRILCEQIASDTCHLQRVVFKNISPADAHRNLCLALRGHKTVTYLTLQGNDQDDMFPALCEVLRHPECNLRYLGLVSCSATTQQWADLSLALEVNQSLTCVNLSDNELLDEGAKLLYTTLRHPKCFLQRLSLENCHLTEANCKDLAAVLVVSRELTHLCLAKNPIGNTGVKFLCEGLRYPECKLQTLVLWNCDITSDGCCDLTKLLQEKSSLLCLDLGLNHIGVKGMKFLCEALRKPLCNLRCLWLWGCSIPPFSCEDLCSALSCNQSLVTLDLGQNPLGSSGVKMLFETLTCSSGTLRTLRLKIDDFNDELNKLLEEIEEKNPQLIIDTEKHHPWAERPSSHDFMI
Protein: FI18240p1 (Nyobe, isoform C) (Nyobe, isoform D) (Q9V9X0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE59626p
- RE37218p2
- trypsin
- FI18310p1
Sequence:
MFLRRCTLLLLICLIASDAASAARKTKRPVKPVKQTNPRTNVTPSPPAVASSGSSTPASTSSTTTTEGSGDQEVATVGSAALAGGGELPKPLVTPIEAQPEAKTDKAPALEEECDPDMIGFEIITGYVLSAPSKMLDTLPGTLMLTDCLEACQSNESCSAVNYETGLCVLFKTTADKLPGSLSRSQFPVFTIYAQKSCLGVRPCSKAWCIDRVQGYRLPEHVKSSQTVLSRRDCLELCLGETEFTCRSANYYRHSGLCELSDMDRITLSAGGSVEPYDGADYLENNCAEEPSKLCEFKRISGKILKTVDSVYQDINTIDECRDLCLNSPYRCHSYDYNDTGDMVCRLSHHSRATLTDVMDPYLDVPEAATYELSACYNVSIECRSGEMITKIRTSKLFDGKVYAKGAPKSCAVNVNNSLEFDFRMGYNDLECNVRQSAYGRYMNDIVIQHHDMIVTSSDLGLAVSCQYDLTNKTVLNDVDLGVTGEIESSLSEEITIDSPNVIMKITSRDGSDMKRMAEVGDPLALRFEIVEPNSPYEIFVRELVAMDGSDSAEITLIDANGCPTDQYIMGTIQKLAQNRKVLLSQFDAFKFPSSEVVQFRALVTPCIPRCEPVICDSEDGASGELKSLVSYGRKKRSVLNGTDGAEFLISTRHRRDVGPVDDNILLMQSIQITDKFGFQPEDGTTTHGNDSGPHEKAYAGVAQDKLTCLNGYGLIMAGALFLLAQLSIFGIWKTVQRRTSKERYLYQHEPTPTITYGAPTMLYGPPPNSSAGSSASGTSYGGSAKDTLSKLYDSGINGRYGQQF
Protein: Ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase subunit M1) (Ribonucleotide reductase large subunit) (P23921)
Organism: Homo sapiens (Human)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonucleoside-diphosphate reductase subunit M2 B
- Ribonucleoside-diphosphate reductase subunit M2
- Cancer-related nucleoside-triphosphatase
- Thymidylate synthase
- Glutaredoxin-1
- Thymidylate kinase
- DNA replication licensing factor MCM5
- UMP-CMP kinase 2, mitochondrial
- DNA replication licensing factor MCM6
- Guanylate kinase
Sequence:
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS
Protein: Voltage-dependent calcium channel gamma-6 subunit (Neuronal voltage-gated calcium channel gamma-6 subunit) (Q9BXT2)
Organism: Homo sapiens (Human)
Function: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21127204}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit beta-4
- Voltage-dependent calcium channel gamma-7 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent calcium channel gamma-4 subunit
- Voltage-dependent calcium channel gamma-8 subunit
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent calcium channel gamma-3 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Voltage-dependent L-type calcium channel subunit alpha-1C
Sequence:
MMWSNFFLQEENRRRGAAGRRRAHGQGRSGLTPEREGKVKLALLLAAVGATLAVLSVGTEFWVELNTYKANGSAVCEAAHLGLWKACTKRLWQADVPVDRDTCGPAELPGEANCTYFKFFTTGENARIFQRTTKKEVNLAAAVIAVLGLAVMALGCLCIIMVLSKGAEFLLRVGAVCFGLSGLLLLVSLEVFRHSVRALLQRVSPEPPPAPRLTYEYSWSLGCGVGAGLILLLGAGCFLLLTLPSWPWGSLCPKRGHRAT
Protein: Acetolactate synthase isozyme 3 large subunit (EC 2.2.1.6) (AHAS-III) (ALS-III) (Acetohydroxy-acid synthase III large subunit) (P00893)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Acetolactate synthase isozyme 3 small subunit
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydrogenase
- Acetolactate synthase isozyme 1 small subunit
- 2-isopropylmalate synthase
- Acetolactate synthase isozyme 2 small subunit
- L-threonine dehydratase biosynthetic IlvA
- D-malate dehydrogenase [decarboxylating]
- L-threonine dehydratase catabolic TdcB
- Dihydroxy-acid dehydratase
Sequence:
MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMDEMWLSKTERT
Protein: NAC domain containing protein 97 (Q9FGQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAC
- Subtilisin-like protease SBT3.18
- NAC domain containing protein 84
- Subtilisin-like protease SBT1.1
- Subtilisin-like protease SBT4.13
Sequence:
MDISAQRFAMNGRSMRLPPGFRFDPDDEDLVFEYLAKKVLHRPMDFDLPELRSCNVDPWDLLGEKNKEVYYFVKKEERERKGRETLSGYWEECEEEEVMEAGGRDCIHLEGRRKTFAFFIGKKPRGTITPWIMYEFRLLSSRATRWSSSPLPRGEVGKWRAVKVVVKEENDEEMVEDEHESDESDGEEVIQSR
Protein: Small ribosomal subunit protein eS10 (40S ribosomal protein S10) (P46783)
Organism: Homo sapiens (Human)
Function: Component of the 40S ribosomal subunit.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:20159986}. Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. {ECO:0000269|PubMed:20159986}.
Interaction partners:
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS5
Sequence:
MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGLEGERPARLTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFRGGFGRGRGQPPQ
Protein: Histone H1.2 (Histone H1c) (Histone H1d) (Histone H1s-1) (P16403)
Organism: Homo sapiens (Human)
Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
Subcellular location: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration.
Interaction partners:
- Histone H2A type 2-A
- Histone H2B type 2-E
- Histone H2B type 1-D
- Histone H2B type 1-C/E/F/G/I
- Histone H2B type 1-K
- Histone H2A type 1-C
- Histone H4
- Histone H1.3
- Histone H2A type 1-B/E
- Histone H1.4
Sequence:
MSETAPAAPAAAPPAEKAPVKKKAAKKAGGTPRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKVKKAGGTKPKKPVGAAKKPKKAAGGATPKKSAKKTPKKAKKPAAATVTKKVAKSPKKAKVAKPKKAAKSAAKAVKPKAAKPKVVKPKKAAPKKK
Protein: Paxillin, isoform B (Q9VIX3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MKIDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLKELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG
Protein: Uncharacterized protein (Q57WX1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLGLTISRFDELQSAVSNGDVVAVGRLLTSYNVNMADNERRMTLLMWAVCFQQHEVAEMLIRLGASLYPRDMFSYNVIHHAAWQGDVRMMKILLCSMSTSSSSEDETSESTSSRTDTFRFRPGVRSLVDLPHPYNGRTPLMFAALKGNVEMVNFLITQAGAAIGAKDLEGNSVMDIAARIGQKAVVTLLLSKCNDDEDMCFNKARRSAEDNCENASTLQQLNEFNDLKTTLCQDWLPQSLVSLS
Protein: Uncharacterized protein Rv2574 (P9WL87)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 2-dehydropantoate 2-reductase
Sequence:
MYPCERVGLSFTETAPYLFRNTVDLAITPEQLFEVLADPQAWPRWATVITKVTWTSPEPFGAGTTRIVEMRGGIVGDEEFISWEPFTRMAFRFNECSTRAVGAFAEDYRVQAIPGGCRLTWTMAQKLAGPARPALFVFRPLLNLALRRFLRNLRRYTDARFAAAQQS
Protein: FXYD domain-containing ion transport regulator (B0S4R3)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGQSSVLVMLAVLCAFFVEIEANPFVYNYERLRIGGLIIAGLLVAGGLFVLLNPKCTRKNKKSEDDTSEL
Protein: Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Q55BH9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75907}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- phosphatidate phosphatase
- PA-phosphatase related-family protein DDB_G0284367
- Lipase
- Diacylglycerol kinase A
- Uncharacterized protein
- Probable Delta
- Delta
- Acyl-lipid
- Fatty acyl-CoA synthetase A
Sequence:
MEPIPPSNGNKNNSMDKQPQQPQQPQQQQQQQQQQRRDQRNSKLNELNETERVRNRFISHEFHKLDRTKSRIDAPKISFSDSESESDSEFFLAKRNTNNNNQNNTSPTFSSANGKQSNLTQRKINTQIQSKQPTNNNVQPLTDDEGTINHSNHHHHHHNQNNNGNNNNNNNNNNNNNKISTPPKQEEKMTMNGLFTLRPSILSSESNGSSYRGFLNLLLILLITASFRLVILNHLLYGIRINLDLYKISEYHRWPGVMISLMINLFIIAAYLIEKAAAKQLLPDRICYLLRIINCAAVIIVPSGSIIAFSPNPASGIIVMILICTFSMKIISYAYENSKQRKLNPDNKKFVIDPTNTSIYPNNLSLRSTYWFMLVPTLVYQLSYPRSPKIRKGYLLRRIVEALSLSLLILWMVNQYMLPLVQNSIEPLEKIDIVLIVERIMKLSLPNLYVWLLGFYVFFHLYLNIVAEITRFGDREFYRDWWNSTGLDYFWRTWNMPVHHWMVVLIYTPMRRRGFSKNMGYFMCFFVSAIFHELVISIPFHSLKLWGFFGIMSQMVLIALTKNLMNGRNLGNVIFWISIVLGQPLVVLLYYRNFVLENPEWYRNVEPPTSPPVMPFY
Protein: Nonsense-mediated mRNA decay factor SMG7 (SMG-7 homolog) (hSMG-7) (Q92540)
Organism: Homo sapiens (Human)
Function: Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14636577}. Nucleus {ECO:0000269|PubMed:14636577}. Note=Predominantly cytoplasmic, and nuclear. Shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:14636577}.
Interaction partners:
- Serine/threonine-protein kinase SMG1
- Regulator of nonsense transcripts 1
- Nonsense-mediated mRNA decay factor SMG5
- RNA-binding protein 8A
- Telomerase-binding protein EST1A
- Regulator of nonsense transcripts 3A
- Regulator of nonsense transcripts 2
- Nonsense-mediated mRNA decay factor SMG9
- Polyadenylate-binding protein 1
- Regulator of nonsense transcripts 3B
Sequence:
MSLQSAQYLRQAEVLKADMTDSKLGPAEVWTSRQALQDLYQKMLVTDLEYALDKKVEQDLWNHAFKNQITTLQGQAKNRANPNRSEVQANLSLFLEAASGFYTQLLQELCTVFNVDLPCRVKSSQLGIISNKQTHTSAIVKPQSSSCSYICQHCLVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKALESRDEVKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQLVHVTVINLFQLHHLRDFSNETEQHTYSQDEQLCWTQLLALFMSFLGILCKCPLQNESQEESYNAYPLPAVKVSMDWLRLRPRVFQEAVVDERQYIWPWLISLLNSFHPHEEDLSSISATPLPEEFELQGFLALRPSFRNLDFSKGHQGITGDKEGQQRRIRQQRLISIGKWIADNQPRLIQCENEVGKLLFITEIPELILEDPSEAKENLILQETSVIESLAADGSPGLKSVLSTSRNLSNNCDTGEKPVVTFKENIKTREVNRDQGRSFPPKEVRRDYSKGITVTKNDGKKDNNKRKTETKKCTLEKLQETGKQNVAVQVKSQTELRKTPVSEARKTPVTQTPTQASNSQFIPIHHPGAFPPLPSRPGFPPPTYVIPPPVAFSMGSGYTFPAGVSVPGTFLQPTAHSPAGNQVQAGKQSHIPYSQQRPSGPGPMNQGPQQSQPPSQQPLTSLPAQPTAQSTSQLQVQALTQQQQSPTKAVPALGKSPPHHSGFQQYQQADASKQLWNPPQVQGPLGKIMPVKQPYYLQTQDPIKLFEPSLQPPVMQQQPLEKKMKPFPMEPYNHNPSEVKVPEFYWDSSYSMADNRSVMAQQANIDRRGKRSPGVFRPEQDPVPRMPFEKSLLEKPSELMSHSSSFLSLTGFSLNQERYPNNSMFNEVYGKNLTSSSKAELSPSMAPQETSLYSLFEGTPWSPSLPASSDHSTPASQSPHSSNPSSLPSSPPTHNHNSVPFSNFGPIGTPDNRDRRTADRWKTDKPAMGGFGIDYLSATSSSESSWHQASTPSGTWTGHGPSMEDSSAVLMESLKSIWSSSMMHPGPSALEQLLMQQKQKQQRGQGTMNPPH
Protein: Thyrotropin receptor (Thyroid-stimulating hormone receptor) (TSH-R) (P47750)
Organism: Mus musculus (Mouse)
Function: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}. Basolateral cell membrane {ECO:0000250|UniProtKB:P16473}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P16473}.
Interaction partners:
- Thyrotropin subunit beta
- Glycoprotein hormones alpha chain
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- Natriuretic peptides A
- Guanine nucleotide-binding protein G
- VIP peptides
- Thyroid peroxidase
Sequence:
MRPGSLLLLVLLLALSRSLRGKECASPPCECHQEDDFRVTCKELHRIPSLPPSTQTLKLIETHLKTIPSLAFSSLPNISRIYLSIDATLQRLEPHSFYNLSKMTHIEIRNTRSLTYIDPDALTELPLLKFLGIFNTGLRIFPDLTKIYSTDIFFILEITDNPYMTSVPENAFQGLCNETLTLKLYNNGFTSVQGHAFNGTKLDAVYLNKNKYLTAIDNDAFGGVYSGPTLLDVSSTSVTALPSKGLEHLKELIAKDTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSIRNLRQRKSVNILRGPIYQEYEEDPGDNSVGYKQNSKFQESPSNSHYYVFFEEQEDEVVGFGQELKNPQEETLQAFESHYDYTVCGDNEDMVCTPKSDEFNPCEDIMGYRFLRIVVWFVSLLALLGNIFVLLILLTSHYKLTVPRFLMCNLAFADFCMGVYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHAYTIMAGGWVSCFLLALLPMVGISSYAKVSICLPMDTDTPLALAYIVLVLLLNVVAFVVVCSCYVKIYITVRNPQYNPRDKDTKIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYQGQRVCPNNSTGIQIQKIPQDTRQSLPNMQDTYELLGNSQLAPKLQGQISEEYKQTAL
Protein: Uncharacterized protein C1778.05c (Q9Y7J2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C23D3.16
- Uncharacterized protein tam1
- GTP-binding protein gtr1
- Uncharacterized protein C29A10.17
- GTP-binding protein gtr2
- Target of rapamycin complex 1 subunit mip1
- Nitrogen permease regulator 3-like protein
- Nitrogen permease regulator 2 homolog
- Folliculin-like protein bhd1
- Serine/threonine-protein kinase tor2
Sequence:
MIKPKKLSSLMKQAVEETVPSIMVFTTTGSLLAYVSFEDPKDGLKRLDLAKRVRSIAALAGNMYSLYTATNPSPLVAESTDDVIAHQRDVLFETIIEFERGKLLIAAISIDGAEDKLYSKDPLLLGIVGTENAKEGMMQIKSELLKECITNELSTLGKPV