wanglab/gogpt-training-data huggingface dataset:
Protein: Fanconi anemia complementation group I (B0I564)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MAQRILQLAAEGSPERLQEALQGLTEGELGDMVTRQALRGRETAALLKGIFKGSPCSQQSGVLRRLQVYKHCVSLVESGDLHVGKVSEIIGLLMLEARQLPGHALAELATLFVEVIKRGSLSNGKSLELFSTVLTALSNSKESLAYGKGELNGEEFKKQLINTLCSSKWDPQCVIHLANMFRDIPLSGEELQFVVEKVLRMFSKLDLQEIPPLVYQLLLLSAKGSKKTVLEGIISFFNQLDKRQKEEQRVPQSADLEVATVPLDQLRHVEGTVILHIVSAINLDQDIGEELIKHLKTEQQKDPGKALCPFSVSLLLSTAVKHRLQEQIFDFLKTSITRSCKDLQILQASKFLQDLCPQQYDVTAVILEVVKNSAFGWDHVTQGLVDLGFSLMESYEPKKSFGGKAAETNLGLSKMPAQQACKLGASILLETFKVHEPIRSDILEQVLNRVLTKAASPVSHFIDLLSNIVVSAPLVLQNSSSRVTETFDNLSFLPIDTVQGLLRAVQPLLKVSMSVRDSLILVLQKAIFSRQLDARKAAVAGFLLLLRNFKILGSLTSSQCSQAIGATQVQADVHACYNSAANEAFCLEILGSLRRCLSQQADVRLMLYEGFYDVLRRNSQLASSIMETLLSQIKQYYLPQQDLLPPLKLEGCIMAQGDQIFLQEPLAHLLCCIQHCLAWYKSTVHLCKGAEDEEEEEDVGFEQNFEEMLESVTRRMIKSELEDFELDKSADFSPSSGVGVKNNIYAIQVMGICEVLIEYNFKIGNFSKNKFEDVLGLFTCYNKLSEILKEKAGKNKSTLGNRIARSFLSMGFVSTLLTALFRDNAQSHEESLAVLRSSTEFMRYAVSVALQKVQQLEEMGQTDGPDGQNPEKMFQNLCKITRVLLWRYTSIPTAVEESGKKKGKSISLLCLEGLLRIFNTMQQLYAARIPQFLQALDITDGDAEEADINVTEKAAFQIRQFQRSLVNQLSSAEDDFNSKETQLLITILSTLSKLLDPGSQQFLQFLTWTVKICKENALEDLSCCKGLLTLLFSLHVLYKSPVSLLRELAQDIHACLGDIDQDVEIESRSHFAIVNVKTAAPTVCLLVLGQADKVLEEVDWLIKRLTILGSDTSEDSTQASNQTQALEKGVILQLGTLLTVFHELVQTALPAGSCVDSLLRSLSKTYAILTSLIKHYIQACRSTSNTVPGRLEKLVKLSGSHLTPQCYSFITYVQNIHSESLSFAEEKKKKKKEDETAVVSTVMAKVLRDTKPIPNLIFAIEQYEKFLIHLSKKSKVNLMQYMKLSTSRDFRINASMLDSVLQEQNTEDAENEPDNNQSGTAEQPDENQEPQKKRRRKK
Protein: Type II secretion system protein J (T2SS protein J) (General secretion pathway protein J) (PilD-dependent protein PddD) (Q00517)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. Type II pseudopilus confers increased bacterial adhesive capabilities.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:8331069}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Type II secretion system protein K
- Type II secretion system protein I
- Type II secretion system protein H
- Type II secretion system core protein G
- Type II secretion system protein M
- Type II secretion system protein L
- Secretin XcpQ
- Type II secretion system protein E
- Probable type II secretion system protein
- HxcW putative pseudopilin
Sequence:
MRLQRGFTLLELLIAIAIFALLALATYRMFDSVMQTDQATRVQEQRMRELVRAMGALERDLTQAVERPVRDELGDNRGAFLSEGENDQIVEFTRGGWRNPLGQARSRLQRVRWSLSGETLERRYWLVLDRAQDSKPRVQQVLDGVTALSWRFLDKEHNWQGHWPTDEGSEEERLESLPLAVEMTLEHRHYGKLVRVWRLLDPPLKQDQPQGQPGGENGENGEGGVPQPPEGMPGAPE
Protein: Keratin-associated protein 5-9 (Keratin, cuticle, ultrahigh sulfur 1) (Keratin, ultra high-sulfur matrix protein A) (Keratin-associated protein 5.9) (UHS keratin A) (UHS KerA) (Ultrahigh sulfur keratin-associated protein 5.9) (P26371)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (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:
Sequence:
MGCCGCSGGCGSSCGGCDSSCGSCGSGCRGCGPSCCAPVYCCKPVCCCVPACSCSSCGKRGCGSCGGSKGGCGSCGCSQCSCCKPCCCSSGCGSSCCQCSCCKPYCSQCSCCKPCCSSSGRGSSCCQSSCCKPCCSSSGCGSSCCQSSCCKPCCSQSRCCVPVCYQCKI
Protein: MBF complex negative regulatory component yox1 (P40923)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Negative regulatory component of the MBF transcription factor complex involved in cell-cycle G1/S phase-specific gene expression and more particularly DNA replication checkpoint-dependent gene expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19714215}.
Interaction partners:
- Transcription factor nrm1
- Start control protein cdc10
- Cell division cycle-related protein res2/pct1
- Cell cycle transcriptional repressor whi5
- Cell division cycle-related protein res1/sct1
- Fork head protein homolog 2
- Transcriptional activator protein rep2
- Cell division control protein 18
- Ribonucleoside-diphosphate reductase large chain
Sequence:
MSLSDSPSKSGNTGKDLISNNEAKNHEDEETHQKKRRRRTTDAEATLLEQYFLKTPKPSLIERQELSKKLKSSMTPRELQIWFQNKRQSLRRSNCLSRNRLEGTGENSLLRRKSTLTLCETSTGQAELFFQSWPLHSQSVVGEMIHHEQDDYNKENKQQKVVDTTKDISRGSNGNEDSAAHQELEECARSLVELQQQCNDH
Protein: FI08437p (Sugar transporter 3) (Q7KJP2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MADGKQGWTCLLVLICVCITVGTVIPVGYAFGVMNAPSAFIRSWIMESVLERYSSRLGDSQMTIIMSTVVSIFLIGGMLGAPFAPIFSARLGRRGILTLSGLLLLVSCICQLFCRMANSIEMLLLGRLIGGLAAALIYATQPMYLVELAPAELSGSVGVFTCIGLTGGIVLGQVFSFDFLLGTEKLWPYALSGSAIFVLIGLAPIFWFPESPRFLMSQGRREKARVTLMRLRRDEGRVNAEMAEFEVSSTDEGQVTMKQVLCNSKLKLPLFIVCSFHFVQQMSGISAIWFYSIEIFTQSGFTAAVAMWLNFALGLLNFISALMGPWLMRSFNRRLMMTISCLCSAIFLVLLVVGLELMSTIHEFSFTCIAFLSLYIITFNMGLGPTPYFIGSEIFETASRPSAMALGSFFNWLANFVLNMIFPTLNSATGPFVFLLCVVFCAYGFLLTYRYLPETRNRDAKDVAQLMENGFKSKIK
Protein: Polarized growth protein RAX2 (A0A1D8PFE5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:23608319}; Single-pass type I membrane protein {ECO:0000255}. Cell tip {ECO:0000269|PubMed:23608319}.
Interaction partners:
- Rax1p
- Transcription activator TEC1
- Ubiquitin-ribosomal protein eS31 fusion protein
- 14-3-3 protein homolog
Sequence:
MLVQFQQLLLLLISIIKLCQADDNDNSFFQPVSQPSLNYKDTGNRIGLLGSFDALSFYSFVNSSQIVNDPDTSVSIFQKKRDVSNSSSSSTSFSNSLYLQDITNNYSLKFADINGQVNQLFKISNDSVVLNGNFTSFNNQSVISPIIFTISSREVTKIFSDDINGSVKTIFLDNDLIYLGGNFKFNNTYSAAVYNITAKKVHSTPFQGFGPNSSINSIAKVLNGDKEKEDNEEELGSILFGGQFDTLGLSDLLVHNITSNNTKKHNTSNTSIISAEQLISLRHGTFTSVNGESSEEDAAAIVCPSDNKEWAAQKNSGAEWKVELPDEMKGIHPTKARIYIPEGPNGIKLFRIYSYPNNGIMNLTYIDPATNELAYCDAWCPLLNYDDLNDHVDNNILNATELNENNSVFVDEQDGSYFQYYDPSTKTKNLGYASNFQEFAFVDNVGVDTVGVTIIDWYGDQGILAGFELYQNAITVYGNDSLNDPNCQSDASDDTNNNAVINSGSFKSVQSINPAITNTDYLVTSDTNAKITLYPNISYSGNYSIIMMTPGCAYDGSCARRAIVNVTVVGDDNDVLSTKTIYQNNENNKFDYLFYGHLNGSKTSTSSNRIEISYMGTVTEGVQDPYMVVDKVIANIVSLDNYYDKNSTNHTRNNTGYELAPIKLNGLFEYSLANFSQFDEQLVHYKRNNKTYISLNNTFVGNSSINLLSGELSNQSRIDQISLGPKQQDGNKQSLLLLGKFESDSKNITLSNNNLITLTIDSYNNTLNETNIELPSRLTKRDTQTILGGNFNNSITRLIELPGCFLAIGDFALSGKDGSSSIKDLSNNNQSVSSANNFALYSDDQWYSFGNDYTSNDFNQFTNLTLDSVEYYVFSGNGQFRTWDNDNFKWVTDPTKQLNLTQAAQINDHQQILGGTGFSTMQFQSVDQAYIADGNFSKFGIDVIANKSFMISNSYYVNSSLSVIGGKFETKDVKNVGLISNSDPNNTISALQGSIVWGDNTLIQSLYVDSSDEYLFMGVNGSVQINEQTNVTGIVIYDLVNNTFTSFQPAELSHSNGDPISVNSMVLFDKGNKLLVGGDFDLAGSLSCPSLCVYDITNTRWINPQNDATTTQSIGGVVTDMKFFQSNQVLITGNGLQLNGNSGIKFLIYNFNSNSFSVKDSLNKIDQTVEKFILNDENNKNLDGRMIAFGEKSISGFDGSNWQRIDSDIIYENFTKFNDMKLLTLDKPSDYNQTYFDKSQIFTIAGVFRLKDYGLVNMALFNGTSWIPYVFTSLQQQKSTGSGSGSGSGSRSSSLQIGQIQSILIDDSYRFQSSDDLKKTNKNLSRGKVVGISLACALGSTTLLGLLYIIPYFALFKNRKDGYFQPERIHEDEMMDAVNPEDLLHEIDLQREK
Protein: COP1, E3 ubiquitin ligase (A0A096UWG1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DET1 partner of COP1 E3 ubiquitin ligase
- DNA damage-binding protein 1
- DNA damage-binding protein 2
- Cullin-4A
- E3 ubiquitin-protein ligase RBX1
- ERCC excision repair 8, CSA ubiquitin ligase complex subunit
- Cellular tumor antigen p53
- Cullin-4B
- Tribbles homolog 3
- DET1- and DDB1-associated protein 1
Sequence:
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAASAATLVSGGVAPAAGSGGLGGPGRPVLVAAAVSGSASAGGAVSAGLSRLSCAARPSAGVGGSSSSLGSSSRKRPLIAPLCNGLLNSYEDKTAPACLITKAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDLLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGPSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYGTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNPASQTSDYEGTVILWDGFTGQRSKEHEKRCWSVDFNLMDPKLLASVLMMQRYCSFLFPLRRPHSFKLSLVHYSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALSDGVTQDAS
Protein: Annexin A7 (Q18043)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MYGRRTCSSSSSSSSSSDGSYRSPVGFGVTPIMPLPYGAPPPPVGAGVGYAPPPPRPYGATYAPPPPMGIGAGVNPSGYVQQAPPLPTQGYSAYNQQPPPLPQQPYQTNMYPSNPGYSSTPGYPQQQPYQIGTGATPAGMYPPPPTGQYPPPPPGQYPGYPRPY
Protein: Actin-related protein 2/3 complex subunit 4 (Actin-related protein C4) (Arp2/3 complex 20 kDa subunit) (p20-ARC) (F4JUL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity). Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2B
- Actin-related protein 2/3 complex subunit 5A
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 2A
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 5B
- Uncharacterized protein
Sequence:
MANSLRLYLACIKNTLEAAMCLQNFPCQEVERHNKPEVELKTSPELLLNPVLICRNEAEKCLIETSINSLRISLKVKQADELENILTKKFLRFLSMRAEAFQVLRRKPVQGYDISFLITNYHCEEMQKQKLIDFIIQFMEDIEKEIRDLKESVNTRGRLVATEFLKQFM
Protein: Troponin T, slow skeletal muscle (TnTs) (Slow skeletal muscle troponin T) (sTnT) (O88346)
Organism: Mus musculus (Mouse)
Function: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin I, slow skeletal muscle
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin I, cardiac muscle
- Troponin C, slow skeletal and cardiac muscles
- Tropomyosin beta chain
- Tropomyosin alpha-1 chain
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Tropomyosin alpha-3 chain
- Myosin light chain 3
Sequence:
MSDTEEQEYEEEQAEDEEAVEEEEAPEEPEPVAEREEERPKPSRPVVPPLIPPKIPEGERVDFDDIHRKRMEKDLLELQTLIDVHFEQRKKEEEELIALKDRIERRRAERAEQQRFRTEKERERQAKLAEEKMRKEEEEAKKRAEDDAKKKKVLSNMGAHFGGYLVKAEQKRGKRQTGREMKLRILSERKKPLNIDYMGEDQLREKAQELSEWIHQLESEKFDLMEKLKQQKYEINVLYNRISHAQKFRKGAGKGRVGGRWK
Protein: Glyoxalase domain-containing protein 4 (Q9CPV4)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MATRRALHFVFKVKNRFQTVHFFRDVLGMQVLRHEEFEEGCKAACNGPYDGKWSKTMVGFGPEDDHFVAELTYNYGIGDYKLGNDFMGITLASSQAVSNARKLEWPLSKVAEGIFETEAPGGYKFYLQDRSPSQSDPVLKVTLAVSDLQKSLNYWSNLLGMKIYEQDEEKQRALLGYADNQCKLELQGIQGAVDHAAAFGRIAFSCPQKELPDLEDLMKRESHSILTPLVSLDTPGKATVQVVILADPDGHEICFVGDEAFRELSKMDPKGSKLLDDAMEADKSDEWFATRNKPKASG
Protein: Aldehyde-alcohol dehydrogenase (Q6Q3I1)
Organism: Listeria innocua
Interaction partners:
Sequence:
MAIKENAAQEVLEVQKVIDRLADNGQKALKAFESYNQEQVDNIVHAMALAGLDQHMPLAKLAVEETGRGLYEDKCIKNIFATEYIWNNIKNNKTVGVINEDTQTGVIEIAEPVGVVAGVTPVTNPTSTTLFKAIIAIKTRNPIIFAFHPSAQRCSSEAAKVVYDAAVAAGAPEHCIQWVEKPSLEATKQLMNHDKVALVLATGGAGMVKSAYSTGKPALGVGPGNVPAYIDKTAKIKRSVNDIILSKSFDQGMICASEQAVIVDKEVAKEVKAEMEANKCYFVKGAEFKKLESYVINPEKGTLNPDVVGKSPAWIANQAGFKVPEDTKILVAEIKGVGDKYPLSHEKLSPVLAFIEAATQAEAFDRCEEMLVYGGLGHSAVIHSTDKEVQKAFGIRMKACRIIVNAPSAQGGIGDIYNGFIPSLTLGCGSYGKNSVSQNVSATNLLNVKRIADRRNNMQWFKLPPKIFFEKYSTQYLQKMEGVERVFIVTDPGMVQFKYVDVVIEHLKKRGNDVAYQVFADVEPDPSDVTVYKGAELMKDFKPDTIIALGGGSAMDAAKGMWLFYEHPEASFFGLKQKFLDIRKRTFKYPKLGGKAKFVAIPTTSGTGSEVTPFAVITDKENNIKYPLADYELTPDVAIVDAQYVTTVPAHITADTGMDVLTHAIESYVSVMASDYTRGLSIRAIELVFENLRESVLTGDPDAREKMHNASALAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVIRYNALKPKKHALFPRYESFRADEDYARISRIIGFPAATTEEGVKSLVDEIIKLGKDVGIDMSLKGQNVAKKDLDAVVDTLADRAFMDQCTTANPKQPLVSELKEIYLEAYKGV
Protein: Cathepsin H (A0A087X0D5)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIQLSASCRRGYEHVLDTACVKLRRYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV
Protein: Sucrose synthase 3 (AtSUS3) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 3) (Q9M111)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Modulates metabolic homeostasis and direct carbon towards starch synthesis in developing seeds.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- alpha-D-xyloside xylohydrolase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Probable alpha-amylase 2
Sequence:
MANPKLTRVLSTRDRVQDTLSAHRNELVALLSRYVDQGKGILQPHNLIDELESVIGDDETKKSLSDGPFGEILKSAMEAIVVPPFVALAVRPRPGVWEYVRVNVFELSVEQLTVSEYLRFKEELVDGPNSDPFCLELDFEPFNANVPRPSRSSSIGNGVQFLNRHLSSVMFRNKDCLEPLLDFLRVHKYKGHPLMLNDRIQSISRLQIQLSKAEDHISKLSQETPFSEFEYALQGMGFEKGWGDTAGRVLEMMHLLSDILQAPDPSSLEKFLGMVPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALETEMLLRIKRQGLDISPSILIVTRLIPDAKGTTCNQRLERVSGTEHTHILRVPFRSEKGILRKWISRFDVWPYLENYAQDAASEIVGELQGVPDFIIGNYSDGNLVASLMAHRMGVTQCTIAHALEKTKYPDSDIYWKDFDNKYHFSCQFTADLIAMNNADFIITSTYQEIAGTKNTVGQYESHGAFTLPGLYRVVHGIDVFDPKFNIVSPGADMTIYFPYSEETRRLTALHGSIEEMLYSPDQTDEHVGTLSDRSKPILFSMARLDKVKNISGLVEMYSKNTKLRELVNLVVIAGNIDVNKSKDREEIVEIEKMHNLMKNYKLDGQFRWITAQTNRARNGELYRYIADTRGAFAQPAFYEAFGLTVVEAMTCGLPTFATCHGGPAEIIEHGLSGFHIDPYHPEQAGNIMADFFERCKEDPNHWKKVSDAGLQRIYERYTWKIYSERLMTLAGVYGFWKYVSKLERRETRRYLEMFYILKFRDLVKTVPSTADD
Protein: Uncharacterized protein YGR266W (P53326)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YGR269W
Sequence:
MHATNWFDDWNPEALYRDDVTGCDDCSETSPIPKSGIICGPILRLINMDFKEKTYEGSIMVVVRGEENFPKITYQLGPSLPSEDEDIEVNEAFFEGKLFHKDILKDDNIWFYRYEIKLPMSNYEQMVKYAVDGTMEPHYRFFVPSFTQNSNVISYSCNGFSLSVDTSKFKGSLWYDVLKKHRYVHYHAILGGGDQIYSDNIKLHAPNLKAWLETKDPIKKYNTQTTEETKEQIRQFYLEHYLNWYGYGHWYGSTPKSKTTQKCFVKSLACIPAINVWDDHDIIDGYGSYNDSFMKTENFLTVGRMAYRYYMLFQQHVSASKQDGDEYAYLKSKQWILGNEKGSSYIGERSHSIFSWLGPKMAMLGLDCRTERKLHEIFSERSYSLIWERVEREIKNLKGGHLLLMLGIPIAYPRLVWLEWLFTSKLLAPIKYLSKKGIFASGFVNEFNGDVELLDDLNDHWCARHHKKERNYLIMKLQDIGAKYGVRITILSGDVHLASVGRFRAKIHRHHLIMSEEKEKENTRIIEEPTKDVRLIFNIIASAIVNTPPPDAMATLLQKRCRLHHFDLETDEDAVPIFAKEVDGVHKRKESCFMNKRNWSDIIPIENLLNNPQLSKELGVKVGDIVIPGIITEQQKLQKLENDDQINSYPVTSGGLFTTIHVERDANQTNSQTVSYCLPIPELTVTCERLSHKGIKHLNIT
Protein: Galectin-9 (Gal-9) (O08573)
Organism: Mus musculus (Mouse)
Function: Binds galactosides (By similarity). Has high affinity for the Forssman pentasaccharide (By similarity). Ligand for HAVCR2/TIM3 (By similarity). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (By similarity). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth. Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function. Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (By similarity). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (By similarity). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (By similarity). Inhibits degranulation and induces apoptosis of mast cells (By similarity). Induces maturation and migration of dendritic cells (By similarity). Inhibits natural killer (NK) cell function. Can transform NK cell phenotype from peripheral to decidual during pregnancy (By similarity). Astrocyte derived galectin-9 enhances microglial TNF production. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000250|UniProtKB:O00182}. Note=May also be secreted by a non-classical secretory pathway (PubMed:9038233). Secreted by mesenchymal stromal cells upon IFNG stimulation (By similarity). {ECO:0000250|UniProtKB:O00182, ECO:0000269|PubMed:9038233}.
Interaction partners:
- Hepatitis A virus cellular receptor 2 homolog
- Cytotoxic T-lymphocyte protein 4
- Lymphocyte activation gene 3 protein
- Programmed cell death protein 1
- CD44 antigen
- T-cell immunoreceptor with Ig and ITIM domains
- Tumor necrosis factor receptor superfamily member 9
- Receptor-type tyrosine-protein phosphatase C
- Programmed cell death 1 ligand 1
- B- and T-lymphocyte attenuator
Sequence:
MALFSAQSPYINPIIPFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFNGNDIAFHFNPRFEEGGYVVCNTKQNGQWGPEERKMQMPFQKGMPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFITFQNSAAPVQHVFSTLQFSQPVQFPRTPKGRKQKTQNFRPAHQAPMAQTTIHMVHSTPGQMFSTPGIPPVVYPTPAYTIPFYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCGGDIAFHLNPRFNENAVVRNTQINNSWGQEERSLLGRMPFSRGQSFSVWIICEGHCFKVAVNGQHMCEYYHRLKNLQDINTLEVAGDIQLTHVQT
Protein: F-actin-capping protein subunit beta (CapZ-beta) (Q9M9G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A9XFX6}.
Interaction partners:
- F-actin-capping protein subunit alpha
- DNA binding protein
- Actin-interacting protein 1-1
- Actin-interacting protein 1-2
- Uncharacterized protein At4g04980
- Vacuolar protein sorting-associated protein 45 homolog
- Actin-related protein 2/3 complex subunit 2A
- Actin-related protein 3
- Uncharacterized protein
- Profilin-3
Sequence:
MEAALGLLRRMPPKQSETALSALLSLIPQHSSDLLSQVDLPLQVLRDIESGKDFILCEYNRDADSYRSPWSNKYLPPLEDALYPSSELRKLEVEANDIFAIYRDQYYEGGISSVYMWEDDNEGFVACFLIKKDGSKSGHGRRGCLEEGAWDAIHVIQVGSEEEEMAQYCLTSTIMLSLTTDDESSGKFGLSGSIRRQMKMELAVADGHLCNMGRMIEELEGKLRNSLDQVYFGKTREMVCTLRPPAEIVQMRLPDT
Protein: Two-component system protein A (EC 2.7.13.3) (Q9P896)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: May be part of a two-component regulatory system required for formation of conidia on certain growth media.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Histidine-containing phosphotransfer protein
Sequence:
MLLNGQISALSLDDNDNGQQHQDEVQAKHQDQGHTCPSRPSVPSLSRIYRCTPVPTIVLDASMVIIEVSNSHVALFGKPRDSLLHTSISDVSPECIPVPNIPILYGALRAACSTREIQVVEHVVVGEKIAHNLRVTPVYEDETLLFVVLEVENLRAEVINNQHAYMNETYKILVDTVKDYAIFMLDPTGHIATWNAGAGVLKGYKAEEIIGKHFSILYSPADRDNGKPARALDVCLREGRIEDEGWRYRRDGSRFWANVLITPIYQFGQHVGFVKVTRDLTERKEAEACMIAAFEESSRLKTDFLANISHEIRTPMNGMQIALTMLTDTGLSEEQREHANIVQDSMSLLLQIVNDVLDYSKLSSGSFSLHADMLDIREIVGAVVRNCRSSLQEGVELDTEISPKLPTRMRGDPLRYRQVLQNLVGNAVKFTEKGSIHVKITSSTDEEDSDSSVVRTEVTDTGIGVPDSAINTLFTPFSRFANSAARKYQGTGLGLSICKSLAELMDGSVGYSPNPNASGSVFWFTAKMGGRSVTPPSKSPSVSGSPVPTEVASEMRSIAPRKHVLLVEDNIVNHTVMLKLLHTIGFQRIDGAWNGAEAVRMVRQKPLSYDIILMDVSMPVLDGLAATEQIRDMGLTMPIIAITGNAMKGDAETYIAQGMDDCICKPVHRDQLLRVLWKWFGT
Protein: glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (Q96AW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAISFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
Protein: Fowlicidin-1 (C4PFJ7)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLSCWVLLLALLGGACALPAPLGYSQALAQAVDSYNQRPEVQNAFRLLSADPEPGPNVQLSSLHNLNFTIMETRCQARSGAQLDSCEFKEDGLVKDCAAPVVLQGGRAVLDVTCVDSMADPVRVKRVWPLVIRTVIAGYNLYRAIKKK
Protein: Small ribosomal subunit protein eS1 (40S ribosomal protein S3a) (v-fos transformation effector protein) (Fte-1) (P61247)
Organism: Homo sapiens (Human)
Function: May play a role during erythropoiesis through regulation of transcription factor DDIT3.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23636399}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03122}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Interaction partners:
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL18
Sequence:
MAVGKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATGDETGAKVERADGYEPPVQESV