wanglab/gogpt-training-data huggingface dataset:
Protein: Stress-induced-phosphoprotein 1 (STI1) (mSTI1) (Hsc70/Hsp90-organizing protein) (Hop) (Q60864)
Organism: Mus musculus (Mouse)
Function: Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8999875}. Nucleus {ECO:0000269|PubMed:8999875}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q7ZWU1}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 1B
- Major prion protein
- Activator of 90 kDa heat shock protein ATPase homolog 1
- DnaJ homolog subfamily B member 1
- Heat shock cognate 71 kDa protein
- Prostaglandin E synthase 3
- Hsp90 co-chaperone Cdc37
- Heat shock protein 105 kDa
Sequence:
MEQVNELKEKGNKALSAGNIDDALQCYSEAIKLDPQNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNLQLKEGLQNMEARLAERKFMNPFNLPNLYQKLENDPRTRSLLSDPTYRELIEQLQNKPSDLGTKLQDPRVMTTLSVLLGVDLGSMDEEEEAATPPPPPPPKKEPKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDKALKHYDRAKELDPTNMTYITNQAAVHFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPRDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
Protein: Pectin lyase 2 (PL2) (EC 4.2.2.10) (Pectin lyase D) (PLD) (Q2TXS4)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable rhamnogalacturonase A
- Probable rhamnogalacturonase B
Sequence:
MKYAAVLTTVAALASRALGAGVSGTAEGFASSATGGGSATAVYPTTTDELVSYLGDDEARVIVLSQTFDFTNTEGTTTETGCAPWGTGSACQVAINKDDWCTNYESSAPSTSVTYDNAGSLGITVNSNKSLIGEGTKGVIKGKGLRIVNGVENVIIQNIAVTDINPKYVWGGDAITINQADLVWIDHVTTARIGRQHYVLGTEADNRVTLSNNYIDGESDYSATCDGHHYWNVYLDGSSDKVTMKGNYFYKTSGRAPKVQGNTYLHAVNNYWNDNSNHAFEIGSGGYVLAEGNTFADVTAAVEDSSFEGELFSSSSDADTCSSYIGRACKANSFTNSGDLSGTTVDVLSKFKGETVATADTASTAPASNAGQGNL
Protein: Basic leucine zipper transcription factor (Basic-leucine zipper (BZIP) transcription factor family protein) (Similarity to G-box binding factor) (Q9FNB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- BZIP transcription factor, putative
- Basic leucine zipper 8
- RING-H2 finger protein ATL52
- At3g63040
- Basic leucine zipper 24
- Transcription factor HY5
Sequence:
MTSFQVMRSSNSRNSDLSRRISSASTSSSSIRPQQQFRRDLTSVGYGGRNDGLYSSNSMTVEGILHDTFASDPPAPTESSLLDASINLMDASPAPMEITTTTASDVVDHGGGTETTRGGKSVDEIWREMVSGEGKGMKEETSEEIMTLEDFLAKAAVEDETAVTASAEDLDVKIPVTNYGFDHSAPPHNPFQMIDKVEGSIVAFGNGLDVYGGGARGKRARVMVEPLDKAAAQRQRRMIKNRESAARSRERKQAYQVELEALAAKLEEENELLSKEIEDKRKERYQKLMEFVIPVVEKPKQQPPRFLRRIRSLEW
Protein: Adenylate cyclase, aggregation specific (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q03100)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Coordinates cell aggregation by synthesizing the cAMP that influences differentiation and morphogenesis of cells within a developing multicellular structure.
Subcellular location: Membrane {ECO:0000269|PubMed:12600317}; Multi-pass membrane protein {ECO:0000269|PubMed:12600317}. Cell projection, uropodium {ECO:0000269|PubMed:12600317}. Note=In non-polarized cells ACA is uniformly distributed at the membrane but upon polarization it becomes highly enriched at the uropodium.
Interaction partners:
- 3',5'-cyclic-nucleotide phosphodiesterase regA
- cAMP-dependent protein kinase catalytic subunit
- Cyclic AMP receptor 1
- cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A
- Uncharacterized protein
- Contact site A protein
- Ankyrin repeat-containing protein
- F-box domain-containing protein
- Guanine nucleotide-binding protein alpha-2 subunit
- Cyclic AMP receptor 3
Sequence:
MASSSPMFNDHAIARSKYALNSVLQQTNELHDGNGGGGYTPSSPHLGGVSLNKSQNQPYTQYNNGGGGGGGGGGHINPMHLNLNSITNNHNNHHNHHPNTLSTPHNNNHNNNNHSTSHHPHSNSVANGGHLSQSITQQRGGLADLANAVINRKNRSDSVQTKMKPTDSASNIESWAKVEKFSSSIFDSEKSKKSNIFQKYTLRLKNSYEKGYLHQHYNSQIMLLRITNLIGIVAVSYGFTKEAIFMLIAIRILCFNLFAFSIFLSFLRNRELYKKLFHPLFLFSFTTFFITILLEYKTTTTTLILFLYVVIFCCLYALGCLLFIWMVMCNLMNAICFIIFIFLESTLDRNNLISFVIYILTMFLVGASHLYVLEKFRKESFIAEKKLIKESNILKNEKEKSSKLLNNILPDFIIENIVYDFEKRDIVIPEPEEYKSCSILCFDIVQFTNMSAKLDSPSRLVDLLTQVFREFDTVVLRNGCQKIKTDGDAYICACGLKSKKKAKKQMPNSKSTPLLQSTSSTSVNNIDLDKDNKDNNNNNNNNKNSNNNFKNKNNIINNNNNSNSNNNNNNNSNNNNINNSGNDDDDEEIEDSELEHFEKLIDVAIEIMNLDVLKETGNTEGIQVQFRCGIAAGSVYGGVIGSQKYQFDIWGDTIARSHTLEQLGQPGKVHVGETIMTHKNWLKKWQYNYNIVSNSECKDQEHDYEFHKAHGECITSYFVDWKDDYREKKKKDLSCDFSINKVLNAETIESKSNNNNYNNNNYNNNNYNNNYNNNNLNNNSNNNNNEYGSSSSSSSVLGEAVTEQIDCNNTNPPLQHKKSQSILTNNENDIVSPSLTSNSPILDTTVNNNNNNNNTNNNNKNQNNIYGNNNNNEEDFKIKSKSNSSFEIEMSNIKKPKSRFIDRVMGILHHVKISNDKIDKEIIQIDEDFVKVTKLRKYFLFFENLTTEKFFHKYVIINNVVETKFFLVIGLILHLMFYLDDHIMDSAPYFNSNVIYLVMGIAFLVYIGLSFTRIFRTPLVYQIAFFILLCAFGVCTVLELIRFQNPLARSSLTRVCATLFYLNVFHSLNFLSVLFLNLFIFSFFIICSILISPTLTNHLYETDYIGFVIVLLIQICSSYGMKLAMRKAWVVNCKINFKTISVNKEKDKFNFLLKSIFPQSALTKLRDMIDTPNIETKGIVYVQPHQDVSIMFIQIAGFQEYDEPKDLIKKLNDIFSFFDGLLNQKYGGTVEKIKTIGNTYMAVSGLDGSPSFLEKMSDFALDVKAYTNSVAISRVVRIGISHGPLVAGCIGISRAKFDVWGDTANTASRMQSNAQDNEIMVTHSVYERLNKLFYFDDEKEILVKGKGKMVTHVLKGKKDLEQTNKWFTKPPEVWEVNATPAGIASPLSGTLLGEIGSFTTPRFHLSS
Protein: UPAR/Ly6 domain-containing protein cold (Protein coiled) (Q9VPR7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome membrane {ECO:0000269|PubMed:20570942}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21613501}; Lumenal side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21423573}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21613501}; Lumenal side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:21423573, ECO:0000269|PubMed:21613501}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21613501}; Extracellular side {ECO:0000269|PubMed:21613501}. Cell junction, septate junction {ECO:0000269|PubMed:21423573}.
Interaction partners:
- UPAR/Ly6 domain-containing protein bou
- LD42595p
- UPAR/Ly6 domain-containing protein crim
- Pasiflora 1, isoform A
- FI02817p
Sequence:
MKSWEIAVVLVAAVYLCSQVNFVAGLECYVCSNQTGNTEKCLNTIKTCEPFENVCGTEIRWGSQPYFSEGALKQYYVSKRCMTKEQCQSKRKRYMQLYCTHIWYEDWACNECCKGDRCNYFVISGAPSRQGYGVCLTLLTALLGLGSWLIPRS
Protein: Glutathione S-transferase (PfGST) (EC 2.5.1.18) (Q8ILQ7)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).
Interaction partners:
- Glutathione synthetase
- Glutathione peroxidase
- Glutathione reductase
- 1-cys peroxiredoxin
Sequence:
MGDNIVLYYFDARGKAELIRLIFAYLGIEYTDKRFGVNGDAFVEFKNFKKEKDTPFEQVPILQIGDLILAQSQAIVRYLSKKYNICGESELNEFYADMIFCGVQDIHYKFNNTNLFKQNETTFLNEDLPKWSGYFEKLLKKNHTNNNNDKYYFVGNNLTYADLAVFNLYDDIETKYPSSLKNFPLLKAHNEFISNLPNIKNYITNRKESVY
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y761)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKSEQRTDRKDNQLGLC
Protein: Uncharacterized protein (Q57VY7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTASRYHLHIVDGGDRSSTVTASMIFAHLALRCGQLRNYLLVSASSTDVKKNRDAANPNRLASSLGGSSAGGTRPTYVGTSDAGTDDQLLLAGEALLRGEGLSHNGISDESSWGEVLSSLKDRIIPYESFSRSFAESEVSLAMSEGPYFDFIATADVASFDYLLDYYLGPCLRSAKKGQLGVGRYGGLPEKRDRRIGLIHILCGEPVRAGYLLQRFMELLLEIDTKSAAGESGKAGEEAWINRVDHVVLQMYQLLSVDVLFTVV
Protein: Protein REDUCED WALL ACETYLATION 1 (EC 2.3.1.-) (Q8L7C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable O-acetyltransferase involved in the acetylation of xylan during secondary wall biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21673009}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Xyloglucan O-acetyltransferase 1
- Anthocyanin acyltransferase-like protein
- xyloglucan O-acetyltransferase 2
- Xylan O-acetyltransferase 1
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- UDP-glucuronic acid decarboxylase 3
- Xyloglucan endotransglucosylase/hydrolase protein 19
Sequence:
MVDPGPITPGQVSFLLGVIPIFVGWIYSELLEYRKSWVPLKPHSDNNLVELGDVAEKDDDKADLLEGGLARSPSVKFHNSSIRTNIIRFLSMEDSFLLEHRATLRAMSEFGAILIYFYICDRTELLGDSTKNYNRDLFLFLYVLLIIVSAMTSLRKHNDKSPISGKSILYLNRHQTEEWKGWMQVLFLMYHYFAAAEIYNAIRIFIAAYVWMTGFGNFSYYYVRKDFSVARFAQMMWRLNFFVAFCCIVLNNDYMLYYICPMHTLFTLMVYGALGIFSKYNEIGSVMALKIFSCFLVVFLLWEIPGAFEIFWGPLTFLLGYNDPAKPDLHRLHEWHFRSGLDRYIWIIGMIYAYYHPTVERWMEKLEDCETKKRLSIKAAIVTITVLVGYVWYECIYKLDRTSYNMYHPYTSWIPITVYICLRNFTHQLRSVSLTLFAWLGKITLETYISQFHIWLRSNMPDGQPKWLLSIIPGYPMLNFMLTTAIYVLVSHRLFELTNTLKTVFVPTKDNKRLFSNFIAGIAIALPLYCFSFVLLQIHR
Protein: EF-hand domain-containing protein (Q38F14)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIYSDNNNPREDSVFLRVKRAVRCGGRGPVTGPIQMVDFLRDFRCLEEEQRASGRKGVTHKQFVKLMEQYGTKLREGDAAYLCKAFDDDNDGYINPERFVRHFTGLNQRRHNAVLRAWASLPKDAKGRVRRNHLNERFSETVTHGDVWGTFSSTVPREAQANNADDDSDDPTLCFEEFLAFYAAVSVEIPLDEKFELFLLREWCADSSRAPVMNSTLREWGQGGDPLAIGKPLYVQDVLDRPLGLSTKSYNYEHMKRVHPYIPPLPPLQLPYLSTMRKDYREFSTQERALSNTLHGR
Protein: Transcription factor Y1 (Myb-related protein Y1) (R2R3 MYB transcription factor Y1) (Yellow seed1) (Q4G2I2)
Organism: Sorghum bicolor (Sorghum) (Sorghum vulgare)
Function: Transcription factor involved in regulating the biosynthetic pathway of flavan-4-ol-derived red phlobaphene and red-brown 3-deoxyanthocyanidin (3-DA) pigments. Regulates transcription of chalcone synthase, chalcone isomerase, dihydroflavonol reductase and flavonoid 3'-hydroxylase genes required for the phlobaphene and 3-DA biosynthesis. Transcription of these genes is activated in mesocotyls in response to ingress of non-pathogenic fungus C.heterostrophus. Regulates the production of 3-DA phytoalexins (luteolinidin, 5-methoxyluteolinidin, apigeninidin and 7-methoxyapigeninidin) in mesocotyls in response to C.heterostrophus and corn leaf aphid (CLA) R.maidis. Involved in resistance against anthracnose leaf blight (ALB) caused by the pathogenic C.sublineolum fungus by inducing the production of 3-DA phytoalexins. Confers resistance, also by inducing the production of 3-DA phytoalexins, against CLA R.maidis, which is an insect and a pest.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000305}.
Interaction partners:
Sequence:
MGRAPCCDKVGLKRGRWTAEEDQILANYIAEHGEGSWRSLPKNAGLLRCGKSCRLRWINYLRADVKRGNISKEEEDIIIKLHATLGNRWSLIASHFPGRTDNEIKNYWNSHLSRQIHTYRRKYTAAPDTTVIIDMSKLHSAEKRRGGRTPGWSPKSSSANTTTNTTSSKTNKSKETDPGPGLKSACDAKGASSPPTAATTTSAASSPRHSDGARSAVVDPDPNQPNSSSGSTAEGPCSGEDATGPWELDPIDLGDLWEAESEIDALMSMDAPLEGFDAVVGEAQAQVDDLFDMDMDWDGFAAHLWGGPEQNDHIAELQQAAEPQATAAACTPNEHEPQVAAAAAACTPDEHEPQAAAAAAAATCTPDEHGLEAFETWLLSDSF
Protein: Transcription initiation factor IIA subunit 2 (General transcription factor IIA subunit 2) (TFIIA 13.5 kDa subunit) (Transcription initiation factor IIA small chain) (Transcription initiation factor IIA small subunit) (P32774)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10525531}. Nucleus {ECO:0000269|PubMed:10525531}. Note=Imported to nucleus via interaction with KAP122.
Interaction partners:
- TATA-box-binding protein
- Transcription initiation factor IIA large subunit
- Transcription initiation factor IIB
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIF subunit beta
- DNA-directed RNA polymerase II subunit RPB1
- Transcription initiation factor IIF subunit alpha
- Transcription initiation factor IIE subunit alpha
- General transcription and DNA repair factor IIH subunit SSL1
- General transcription and DNA repair factor IIH helicase subunit XPD/RAD3
Sequence:
MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE
Protein: Uncharacterized protein (Q38CH7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYKYSSREYCSPVCMRCVKSNGVRGSVDTVGGDTGRCECHTSIGHRHKYSVERKNNAGRQTTSILSPAPCSARGTATDAPADRQNVDGQRRSSFAKPSPNDIVWIPTSQLLPRFHGTDTGGSNEEEEYCPVTKWPKPQDIPLPSMIPLPSSVLRSLPPEKSQPPSQWSSIPVNEQTIKKKRGCDGQGYEVAERPVAPSVRVEGHVCPCEKRMLHTYPSNRETAETHEEAEQQKCDVKESEEEPANINNNNNTPGQYINECCDSDETQKYDSVQMWCQSLRQPTRRCEQPPPRSRKSSASPTAEGFAACGTSQHRCTATHPDGSCERRRDSELRGGSGARENSLHPPRKSVDSKVSRGTNNIHARKSETRKLREVVNVRTTSSNSDTASVRSEPEEVSRDREERFRVHLTNMDELYRHLLSRYDEFQKDHADFLEKNGSSRRVVDEQTAHPQKLSIKKDTVDLVDDIPPLPERGYSGKLYPLSEDSQKLQEQLISLETRWKQTGRPKKGGAEERMWGLAETAVNAERDRKQTRPLARRTKTLSADRKFSSGRTYVVKKAESKESRGRTQSVKRVPTDSKIVGTTRHMSPQGGARRRDVSPQLVYNFLAAQKDKNSEENDGNGECVSDSRGRHLDFTREQVLHLVRERKMLFSREEKK
Protein: NADH-quinone oxidoreductase subunit H (EC 7.1.1.-) (NADH dehydrogenase I subunit H) (NDH-1 subunit H) (NUO8) (P0AFD4)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit K
Sequence:
MSWISPELIEILLTILKAVVILLVVVTCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWIPKFSDRVIFTLAPMIAFTSLLLAFAIVPVSPGWVVADLNIGILFFLMMAGLAVYAVLFAGWSSNNKYSLLGAMRASAQTLSYEVFLGLSLMGVVAQAGSFNMTDIVNSQAHVWNVIPQFFGFITFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTISALMVTLFFGGWQGPLLPPFIWFALKTAFFMMMFILIRASLPRPRYDQVMSFGWKICLPLTLINLLVTAAVILWQAQ
Protein: T-cell surface protein tactile (Cell surface antigen CD96) (T cell-activated increased late expression protein) (CD antigen CD96) (P40200)
Organism: Homo sapiens (Human)
Function: May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Nectin-2
- Poliovirus receptor
- Nectin-1
- T-cell immunoreceptor with Ig and ITIM domains
- Natural cytotoxicity triggering receptor 3
- NKG2-A/NKG2-B type II integral membrane protein
- Transmembrane protein PVRIG
- Natural cytotoxicity triggering receptor 1
- Lymphocyte activation gene 3 protein
- Cytotoxic T-lymphocyte protein 4
Sequence:
MEKKWKYCAVYYIIQIHFVKGVWEKTVNTEENVYATLGSDVNLTCQTQTVGFFVQMQWSKVTNKIDLIAVYHPQYGFYCAYGRPCESLVTFTETPENGSKWTLHLRNMSCSVSGRYECMLVLYPEGIQTKIYNLLIQTHVTADEWNSNHTIEIEINQTLEIPCFQNSSSKISSEFTYAWSVENSSTDSWVLLSKGIKEDNGTQETLISQNHLISNSTLLKDRVKLGTDYRLHLSPVQIFDDGRKFSCHIRVGPNKILRSSTTVKVFAKPEIPVIVENNSTDVLVERRFTCLLKNVFPKANITWFIDGSFLHDEKEGIYITNEERKGKDGFLELKSVLTRVHSNKPAQSDNLTIWCMALSPVPGNKVWNISSEKITFLLGSEISSTDPPLSVTESTLDTQPSPASSVSPARYPATSSVTLVDVSALRPNTTPQPSNSSMTTRGFNYPWTSSGTDTKKSVSRIPSETYSSSPSGAGSTLHDNVFTSTARAFSEVPTTANGSTKTNHVHITGIVVNKPKDGMSWPVIVAALLFCCMILFGLGVRKWCQYQKEIMERPPPFKPPPPPIKYTCIQEPNESDLPYHEMETL
Protein: N-terminal acetyltransferase A complex subunit nat1 (NatA complex subunit nat1) (O74985)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. nat1 anchors ard1 and nat5 to the ribosome and may present the N termini of nascent polypeptides for acetylation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-terminal acetyltransferase A complex catalytic subunit ard1
- Uncharacterized N-acetyltransferase C663.13c
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase B complex subunit arm1
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Pre-mRNA-splicing factor cwf24
- N-terminal acetyltransferase A complex subunit-like protein C418.02
Sequence:
MAKVQLSPKEITLFRTALKCYETKQYKKGLKAIEPLLERHPEHGESLAIKGILLHSLGNTKEGYDNVRLGLRNDVGSGVCWHIFGLISRADKDYVQAAKCYINAHKLEKNNSSLLRDLALLQSQLRQYKALADTRNALLQDNPGVRANWSALAVAQFLRGEYASAYKIVDAFESTINQGVPVDTQEESEAMLFMNLVILKKDGVEDAYKHLLSIEKKVLDRVAFLETRAEYELYLSKMEEAKSTIYLLLDRNPDNHQYYYNLQRAYGYEDASGKVLDSAEWLNLYSQLAKRYPKSECPTRLPLEKLEGDEFLTHVDLYLRKKLKRGIPSVFVDVKSLYKDTKKCKVVEDLVSKYASSLSTTNKFSEDDDNSQIEIPTTLLWTYYFLAQHFDHVGELEKAEKYVDLAIDHTPTLVELFMTKARISKHKGELQTAMEIMDHARKLDLQDRFINGKCAKYMLRNDENELAAKTVSLFTRNEAVGGAVGDLADMQCLWYMLEDGKSFARQKKFALALKRFSTVFKIFDTWADDQFDFHFFAFRKGSLRTYLDLMSWEDSVYDDPSFREAAQGSIEIYFALFDLPFAKYSPKLPDFEKLSSGEINEEEEKKIYKKLKKDLSKRLERAEKLKEADKSRAKSEDGMPVKYDEDPLGENLVATSEPLKEAQKCLEKLLPYGDKNPSAYILAAQLYTRLKNFDTASKYLEQAKVILGQNDPTVISTEKFYNSIKTQSN
Protein: Protein Vago (Q9VZ35)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably involved in the antiviral immune response. May have a role in controlling viral load in the adult fat body, after infection with viruses such as the Drosophila C virus.
Subcellular location: Secreted {ECO:0000269|PubMed:32878003}. Note=Expressed in hemolymph. {ECO:0000269|PubMed:32878003}.
Interaction partners:
- FI07211p
- Cytokine receptor
Sequence:
MESISSMIYLVAMMSLIIGGSQAIPYRPSAYLYNQQYCMDTLTGRQLYIGEVFTREDQCVRIQCLETLQLWEDSCQVPKLTQGNCTPVPSTNPHAEYPRCCPLYECKSYESNSGGTLEQTNIYDHYGTLRSSHLTEMIVIDGRTPPRGEIHTASARKYQV
Protein: Alphabet, isoform A (Alphabet, isoform C (EC 3.1.3.16)) (Alphabet, isoform D) (Q9VAK1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
Sequence:
MGGFLDKPKTAKHNDEGEGNKLLFGVSSMQGWRSEMEDAYYARAGLGDALPDWSFFAVFDGHAGCKVSEHCAKHLLESIISTEEFIGGDHVKGIRTGFLRIDEVMRELPEFTRESEKCGGTTAVCAFVGLTQVYIANCGDSRAVLCRQGVPVFATQDHKPILPEEKERIYNAGGSVMIKRVNGTLAVSRALGDYDFKNVKEKGQCEQLVSPEPEIFCQSRQDSDEFLVLACDGIWDVMSNEDVCSFIHSRMRVTSNLVSIANQVVDTCLHKGSRDNMSIIIIAFPGAPKPTEEAIEAEHRLEKQIEKITRDEIESSKITDYVDLLKCLQNRDDIEGLPPGGGLQSKYHVIERTFKQEFPDRPCESPTH
Protein: Netrin-G1 (Laminet-1) (Q8R4G0)
Organism: Mus musculus (Mouse)
Function: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10964959}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10964959}; Extracellular side {ECO:0000269|PubMed:10964959}.
Interaction partners:
- Leucine-rich repeat-containing protein 4C
- Leucine-rich repeat-containing protein 4B
- Leucine-rich repeat-containing protein 4
Sequence:
MYLSRFLSIHALWVTVSSVMQPYLFVWGHYDVCKSLIYTEEGKVWDYTACQPESTDMTKYLKVKLDPPDITCGDPPESFCAMGNPYMCNNECDASTPELAHPPELMFDFEGRHPSTFWQSATWKEYPKPLQVNITLSWSKTIELTDNIVITFESGRPDQMILEKSLDYGRTWQPYQYYATDCLHAFHMDPKSVKDLSQHTVLEIICTEEYSTGYSTNSKIIHFEIKDRFAFFAGPRLRNMASLYGQLDTTKKLRDFFTVTDLRIRLLRPAVGEIFVDELHLARYFYAISDIKVRGRCKCNLHATSCLYDNSKLTCECEHNTTGPDCGKCKKNYQGRPWSPGSYLPIPKGTANTCIPSISSIGNCECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGYFRNASAQLDDENVCIECYCNPLGSIHDRCNGSGFCECKTGTTGPKCDECLPGNSWYYGCQPNVCDNELLHCQNGGTCQNNVRCACPDAYTGILCEKLRCEEAGSCGSESGQGAPPRGSPALLLLTMLLGTAGPLVF
Protein: P2X purinoceptor (Q7SZM2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Membrane {ECO:0000256|RuleBase:RU000681}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000681}.
Interaction partners:
Sequence:
MPCVLLNLCEYDTQKLVKIKSVKLGSLKWTLNGVILMFICIMMLWNKEYQEYDFVVSSVTTKVKGVAKITLPEVGDVVWDVVDYSGPSQGKNSFFVATNAIVTKNQKQGNCAEILPNGKLCRTDKDCEKGFSDQHSHGVQTGACVKLEILKKTCEVTAWCPIENKKNPRPALLAAAENFTVMIKNNIRFPAFNYIRRNILSEMKDTDFKGCIYHRYKNPYCPIFRLGDIVAEAKEKFSEMAVEGGVIGIQINWDCDLNRFFHSCLPKYSNRRLDEKESNRTLYPGLNFRFARYSTVNGVEQRTLFKMYGIRFDVMVFGKAGKFSIIQLIIYIGSTLSYYAITTIFLDWLIGTGYYSKEAKQNYTERKFEAVQDREECFLCVSFVDEDNLRVVKKSRKKILQETKPLSIHQRKNELASMKTLLSVLQCGQSRSEPVQNGQSGGLIVDENLSSRHNGRQNPDTPLLETTQSSSPTWCQCGSCRPAETLQEQLCCRLKKGRCITSSPIFSSLIVSRSVLENALFFVDPLAELHEESQLRHGAYAQFIRWRFGDSTPRDALPVIPSCCIWRIRAEYPSPDGTYRGLRSFQVITSQTEVNR
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSV7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- GDP-mannose transporter
Sequence:
MSLKPRSLTAKKRRPSQNHGELMALGIGNPLDVVRKYLGLGVSDMDLNDGRYVSKKKRNRYTVMPMLVFFVVVMYLLVSTFMPNGMRAPVTYPPEHGAYQNEVISSSPLIFPHVEHAPVLKEIGIRGLFILRMEMDGTKRFVIKPEDKPFSDEEKKKTTDQVLLVKKSFLDHGKLIFPKKNESPEFVVVTLVDFDNFDRDTIVKIVQNRVDYAQRHKYGIYVRWAQEFVTEMSIQEVAPSYQLMKASIMRAAIHAFPYAKYFLFLDQTSLIMNSEIPLQKLILHQPTVEANKQVLPILQHYNGRNVPAKLAQQPDLVFPQHDNGVLDLSAFIVANSLHGKMFLDYLNDPLVRDYHWDDIYTQYGHVLNWHPELLDRTLLVKRKTLASPVEDPTNLNIKDNKIDGGDSGYSTGDFIASLAKCKERISCTSDLDVMYKFSHMG
Protein: Chemokine (C-X-C motif) ligand 8b, duplicate 1 (Interleukin-8, like 1) (Interleukin-8b.1 precursor) (N0GW19)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Chemokine
- Chemokine
- Stromal cell-derived factor 1
- C-C motif chemokine 19a.2 precursor
- Chemokine
- C-C motif chemokine
- C-C motif chemokine
- C-X-C chemokine receptor type 2
- NACHT, LRR and PYD domains-containing protein 16
- Chemokine
Sequence:
MMKLSVSAFMLLICTTALLCANEGEALPPPQRCQCIKTHSKPPIPKRQVLGLKVTPAGSHCRNEEIIATLKKGQICLNPTETWVISLKEKFAASATKLAATAAPAQTTTTFSTIMTTN
Protein: Cyclin-dependent kinase-like 2 (EC 2.7.11.22) (Protein kinase p56 KKIAMRE) (Serine/threonine-protein kinase KKIAMRE) (Q92772)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9000130}. Nucleus {ECO:0000269|PubMed:9000130}.
Interaction partners:
Sequence:
MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAERFSQELQLKVQKDARNVSLSKKSQNRKKEKEKDDSLVEERKTLVVQDTNADPKIKDYKLFKIKGSKIDGEKAEKGNRASNASCLHDSRTSHNKIVPSTSLKDCSNVSVDHTRNPSVAIPPLTHNLSAVAPSINSGMGTETIPIQGYRVDEKTKKCSIPFVKPNRHSPSGIYNINVTTLVSGPPLSDDSGADLPQMEHQH