wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase epsilon catalytic subunit A (EC 2.7.7.7) (DNA polymerase II subunit A) (P87154)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA polymerase II participates in chromosomal DNA replication.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA polymerase epsilon subunit D
- DNA polymerase epsilon subunit B
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm5
- Cell division control protein 45 homolog
- DNA polymerase delta catalytic subunit
- DNA replication licensing factor mcm4
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm6
- DNA polymerase alpha catalytic subunit
Sequence:
MPLKTARGASKYQFRKFNGNYNGKSKSNGRTFAKSTEEVGFNDPMKIVYKKNEIDRMMGFDSYEGGQPREAWLLNVHPTVIESTKGNSTLSAVDFYFIQDDGDTFRCTIPYSPYFYIAAREGKEALVDDYLKKKFVGLIKSTTRIFKEDLQLKNHIVGYQKLYIKLVFDNLNDLQAVRKSLMSAVKANSSQQDAVDAYTNLSSENLNGIIENAFEDPLNHVLDIREYDVPYHSRTLIDLNIRVGQWYTVSYHEGHVQISLLASRIERAEPTIMAFDIETTKLPLKFPDSSFDKIMMISYMIDGQGFLITNREIISQNIEDFHYTPREEFEGPFIIFNEPDEVGLLHRFFKHIRSAKPSVIVTYNGDFFDWPFVDARAAFHGLNLTEETGFFRDAEDEYKSSYCSHMDAFRWVKRDSYLPQGSQGLKAVTVSKLGYNPIELDPELMTPYASEKPQVLAQYSVSDAVATYFLYMKYVHPFIFSLCNIIPLNPDEVLRKGTGTLCETLLTVEACTKNIILPNKHVDASQKFFDGHLLASETYVGGHVESLESGVFRSDLPTNFNMDPKVYEELILQLDKALDFSLTVENNVNVDEIENYEEVRDSILKKLSDLRDRPKRSEKPRIYHLDVASMYPNIMITNRLQPDSVKDESFCATCDLNVPNKTCDRRMVWAWRGEYYPAKKGEYHMIYSALQSERFPGPTPFSPFRSFQELSPSEQAAMVQKRIADYSRKVYHRLYDNTVIERETIICQKENSFYIDTVKSFRDRRYDFKGLQKKWVKQLAAIKEKGGLAEIEEAKKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSIEMAGITCLTGATIIQMARQIVERAGRPLELDTDGIWCILPESFPENFEFKKKSGGKVFISYPCVMLNHLVHEKFTNHQYSALKDPEKLVYETTSENSIFFEVDGPYRAMILPASTEEGKNLKKRYAVFNFDGSLAELKGFEVKRRGELKLIKDFQSQIFKVFLKGDSLEECYQEVAYVADTWLEILFTKGSNLTDDELIELISENRSMSKALSEYGSQKSTSITTARRLADFLGDQMTKDKGLACRFIISASPKGRPVAERAVPVAIFFAEESVKRHFLRLWLKDNGLYDVDIRDIIDWDYYLKRLGSVVQKLISIPAALQRISNPVTRFPLPDWLQKRVAVLNSKYQQKKIDSIFSLAPTNPSTINNTKVTDIEDLGSVTHKDKRIVARVTKRKLLQQSGNSEAPVSFEVKPVSFMDGYSNWLKYAKKKWKYQKQVKLRRRHLIGFQSRQFTNVLQSSAEVMFENLWHILQIRETDVPGILHAWVIIRNRLTSIRFIVNRKFFVCFKDETLPNVEIEGCLIEKSNAILPHGSTSDKLFLLEIPEKSYLTEKVSISMIFAHPSVSGIYETRIEPIERLILEMGSRKRFNNSVPGALGKGFEFGFESKMFTDPSDNDVSYLDGVEMNYLYAFHFSISNRFVFSLFMPHLKKVEAIIYDKLPGSDMSFPSISKIYEELRSKFDNLIKESSIEYPDTLSCNVIFSGNERKAYKLIDEKLLQYFSTKTKNSLLIIESSLPHILKANVKQIEELPYIMIPRLESNIQSLSWKQHIATKMIQHFLAIGSWLFHRIQLSRFSDIPLCNFESDDIQYSIDVVYSRKLKEHNIILWWNKGPTPDLGGIEKDSILQIASPKDPLEVNNPGAYSNACVDISLSNLALCSILNSALINDIEGIGDMAALNDNYMTAINDDLEEKLGIHDNIGLTHSLPVLKALVKTWWNEAASGNNLADLIIQHLARWISSSKSYLYSPLLSSHVEVIMRKTFLQLLSEIKRLGAHIIHASANKILIKTSKLIVQNAVTYSNYLLKSIKTLPLFHFLDLNVTEYWDYLLWMDSVNYGGKMVAANFSATNEEPQTVVSWHIKSHLPPIIQPEFQSWIVEFIEEVYKQKLEKSNTKVGFVRVKNNNADEDSEIVGSGILKSKLIHPLKRKVAQVRRCFQELQLDENTREDLKFPKLPGSFLNYTDGALELVKSICAVFELSHDLNLEVRFLKKSLLSLLQIQEFSTQAVFRYPSRRLSLDQIPCKQCGVHQDFDLCLHEHLWPTRDDMGTLVFSDGWSCSSCNLVYDRWVFEETLVDNLYHQLTLYQLQDLICSKCKTVKQWSLKERCSCSGEWVLQLSPTKFREMLNVYQSVADFYEFSILQNSVQSILSVLN
Protein: Histone H3.3 type c (Histone 3, variant 3 type c) (Q55BP0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome. Note=Associated with pericentromeric heterochromatin.
Interaction partners:
- Histone H4
- Histone-lysine N-methyltransferase set1
- Histone H2B.v3
- Histone H2A.z
- VWFA domain-containing protein
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- PHD zinc finger-containing protein
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase roco8
Sequence:
MARTKQTARKSTGAKVPRKHLSSKSSFPSKPVNEVLKKTHRFRPGTVALREIRRYQKSSDLLIKKLPFQRLVREIAQEFKTDLRFQAAAIEALQEATEAYLVGLFEDTNLCAIHAKRVTIMVKDIQLARRIRGERA
Protein: Trypsin inhibitor CMe (Alpha-amylase/trypsin inhibitor) (BTI-CMe1) (BTI-CMe2.1) (BTI-CMe3.1) (Chloroform/methanol-soluble protein CMe) (P01086)
Organism: Hordeum vulgare (Barley)
Function: Inhibits trypsin in vitro. Probably plays a protective role through inhibition of insect midgut proteases.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MAFKYQLLLSAAVMLAILVATATSFGDSCAPGDALPHNPLRACRTYVVSQICHQGPRLLTSDMKRRCCDELSAIPAYCRCEALRIIMQGVVTWQGAFEGAYFKDSPNCPRERQTSYAANLVTPQECNLGTIHGSAYCPELQPGYGVVL
Protein: Nervana 3, isoform E (M9PDX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha
- Sodium/potassium-transporting ATPase subunit alpha
- Uncharacterized protein, isoform A
- LP13633p
- GEO05126p1
Sequence:
MADKKIGEYYAPPVKMGKWEGFKKFLWNSETSQCLGRTGSSWAKILLFYIIFYAALTGFFAAIFTVFYQTLDNEKPKWMLDNGLIGSNPGLGFRPMPPEANVESTLVWYESSKKDNYKYWVDETSRFLKYHTYQDLEKQNQVNCSFEHPPQDDKVCGIDFSSFSPCTADNNFGYHVARPCIFLKLNKIYNWIPEIYNDSKTLPDHMPEELKQHIKEKQSLRPNETNVVWVSCEGENPADVENIKARDYYPRMGFPRYYFPFKNIQGYIPPIVAVQFTVETGVLINIECKAWARNINHDRSDRRGSVHFELMVD
Protein: Mitochondrial inner membrane protein SHH4 (SDH4 homolog) (Q06236)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Homolog of SDH4, but seems not to be a stoichiometric subunit of either the succinate dehydrogenase (SDH) complex or the mitochondrial inner membrane translocase TIM22 complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:22152483}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial inner membrane protein SHH3
- Succinate dehydrogenase cytochrome b subunit
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MSSTKFLKPLCRIRAFHTSIARSFTIPFLPKIPQKPGGVSGTANDSSYMPPESRAQGSYHWIVERGLSLAVLPLIAVPLVTTGPISTFTDTFLSLVLLGHCHIGFQSCIIDYISERVYGKVHHYAMYLLSLGSFLSFVGIYKLESQEAGLIASLKSLWDNKPVEKKRQ
Protein: Mediator of RNA polymerase II transcription subunit 11 (Q6ID77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 32
- Mediator of RNA polymerase II transcription subunit 4
- ATP-dependent DNA helicase Q-like 2
Sequence:
MDPQTQNTSLQRLQNVENRVVKVLELAGGVMEELASPSGPKKEFVNSHCREFMQSMKDIQVTLREEIKSACEYRPFEKCDYNARIANEICFQKLEYVLTQLEDLKQTADRYPSSD
Protein: Myozenin-3 (Calsarcin-3) (FATZ-related protein 3) (Q8TDC0)
Organism: Homo sapiens (Human)
Function: Myozenins may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localized at the Z-line of skeletal muscle. {ECO:0000250}.
Interaction partners:
- LIM domain-binding protein 3
- Telethonin
- Filamin-C
- Alpha-actinin-2
- Alpha-actinin-1
Sequence:
MIPKEQKGPVMAAMGDLTEPVPTLDLGKKLSVPQDLMMEELSLRNNRGSLLFQKRQRRVQKFTFELAASQRAMLAGSARRKVTGTAESGTVANANGPEGPNYRSELHIFPASPGASLGGPEGAHPAAAPAGCVPSPSALAPGYAEPLKGVPPEKFNHTAISKGYRCPWQEFVSYRDYQSDGRSHTPSPNDYRNFNKTPVPFGGPLVGGTFPRPGTPFIPEPLSGLELLRLRPSFNRVAQGWVRNLPESEEL
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102) (O35142)
Organism: Rattus norvegicus (Rat)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Shows only a slight preference for the cis-Golgi apparatus (<55%), compared with the trans-Golgi (>45%). {ECO:0000250}.
Interaction partners:
- Coatomer subunit gamma-1
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit epsilon
- Coatomer subunit alpha
- Coatomer subunit zeta
- Coatomer subunit gamma
- Bifunctional glutamate/proline--tRNA ligase
- Coatomer subunit zeta
- ADP-ribosylation factor GTPase-activating protein 2
Sequence:
MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKRFQPSRATAQQEPDGKPASSPVIMASQTTHKEEKSFQELEDDLDTMELEDIDTTDINLDEDILDD
Protein: Interferon alpha/beta receptor 1 (IFN-R-1) (IFN-alpha/beta receptor 1) (Type I interferon receptor 1) (P33896)
Organism: Mus musculus (Mouse)
Function: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves (By similarity). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (By similarity). Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:24075985}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000305|PubMed:14532120}. Lysosome {ECO:0000305|PubMed:14532120}. Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes. {ECO:0000305|PubMed:14532120, ECO:0000305|PubMed:24075985}.
Interaction partners:
- Tyrosine-protein kinase JAK1
- Non-receptor tyrosine-protein kinase TYK2
- Interferon alpha/beta receptor 2
- Interferon beta
- Signal transducer and activator of transcription 2
- Signal transducer and activator of transcription 1
- Interferon epsilon
- Interferon kappa
- Interferon alpha-2
- Interferon alpha-1
Sequence:
MLAVVGAAALVLVAGAPWVLPSAAGGENLKPPENIDVYIIDDNYTLKWSSHGESMGSVTFSAEYRTKDEAKWLKVPECQHTTTTKCEFSLLDTNVYIKTQFRVRAEEGNSTSSWNEVDPFIPFYTAHMSPPEVRLEAEDKAILVHISPPGQDGNMWALEKPSFSYTIRIWQKSSSDKKTINSTYYVEKIPELLPETTYCLEVKAIHPSLKKHSNYSTVQCISTTVANKMPVPGNLQVDAQGKSYVLKWDYIASADVLFRAQWLPGYSKSSSGSRSDKWKPIPTCANVQTTHCVFSQDTVYTGTFFLHVQASEGNHTSFWSEEKFIDSQKHILPPPPVITVTAMSDTLLVYVNCQDSTCDGLNYEIIFWENTSNTKISMEKDGPEFTLKNLQPLTVYCVQARVLFRALLNKTSNFSEKLCEKTRPGSFSTIWIITGLGVVFFSVMVLYALRSVWKYLCHVCFPPLKPPRSIDEFFSEPPSKNLVLLTAEEHTERCFIIENTDTVAVEVKHAPEEDLRKYSSQTSQDSGNYSNEEEESVGTESGQAVLSKAPCGGPCSVPSPPGTLEDGTCFLGNEKYLQSPALRTEPALLC
Protein: Monooxygenase, putative (Q582J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
Sequence:
MNGRTRVLFTAGVPTPPNCAHNVVISGGGIVGAAAMAALQKLRARFLAESVGAEGSVSHNVHSRCLSRLLLADPMARPHYDAANIMHNLRTVSLTPVSSKLLDNLGSWKRLQTKHAYYRIALRHERTNGPVAPDQSSQEKSRNFFVNGPLGNGTSTAEPLLEFTNLDSPLGFICYNSDINTTLLDVVEEQMKQYQQPLGSDGCGVQEQPTDCIEFGSSLGSYSLPHRNIVDGPAGRAILRKSVGDQPVEFSLLLGCEGRGGHLRESLGSALVQHDYAQTAFVCTVQLKRPADGNVCCFQNFFTNGDIIALLPTSEDTSNIVFSTTAEHARELAAAKQSELVEELNRCLHAFAPRDIPLIISVPEVELGGKTVRAQGMFPVRLSVALQPFGPRCLLLGDAAHGIHPFAGQGLNLGLYDVCALVEVLERAVRSGQDIGSVIAVGQPFAAAMMSHTGIMITAMESVFGLLATMPGLSCTGMSVLQKLPLVSSLGKQSIIHVASGGFFASHHRESFLLA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9PVT8)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
LPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQQNTETRKRKLTIRRYKVVPLSQRSGVLEWCSGTTPIGEFLVNADQGAHKRYRPHDYSGFLCQKIMMDAQKKHSEEKYNIFMKVCDNFQPVFRYFCMEKFRDPAVWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILIDEQTAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKMAVMRNSQEALLTIVEVLLYDPLFDWTMTPLKALYLQQGPEDEADMSSTLGADPQACKRKASDDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAMDPKNLSRLFPGWKPWV
Protein: Zinc finger protein 6 (Q39265)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor required for the initiation of inflorescence trichomes in response to gibberellin and cytokinin. Acts upstream of GIS, GIS2, ZFP8, ZFP5 and the trichome initiation regulators GL1 and GL3. Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q39261}.
Interaction partners:
- Transcription factor GLABRA 3
- Zinc finger protein 11
- Transcription factor MYB23
- Zinc finger protein 10
- C2H2 and C2HC zinc fingers superfamily protein
- Transcription factor EGL1
- Homeobox-leucine zipper protein GLABRA 2
Sequence:
MATETSSLKLFGINLLETTSVQNQSSEPRPGSGSGSESRKYECQYCCREFANSQALGGHQNAHKKERQLLKRAQMLATRGLPRHHNFHPHTNPLLSAFAPLPHLLSQPHPPPHMMLSPSSSSSKWLYGEHMSSQNAVGYFHGGRGLYGGGMESMAGEVKTHGGSLPEMRRFAGDSDRSSGIKLENGIGLDLHLSLGP
Protein: Reiske iron-sulfur protein, mitochondrial (EC 1.10.2.2) (Q38D40)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Mitochondrial processing peptidase alpha subunit, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Electron transfer protein, putative
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Cytochrome c
- Acyl carrier protein
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Mitochondrial processing peptidase alpha subunit, putative
- Mitochondrial processing peptide beta subunit, putative
Sequence:
MFRRSCISAFQPTAFLRVSLVFKQLEGSNPLTVKDRPVNSWSDEFLKPPVSKEMADKYGRYAKYSDPTLCSVDTSSEVVLNTYPEGSREGRIEATAGVALKDYDASMWDEEFFRKYILKPKLPNELEDRARVTDYALNSALLGFVILMVRYAVLPLWYVGQPAMSMVGQMNIEAEVGELEDRECKTVVWRGKPVFVYRRSERQMNDVLGTPLSALKHPETDEARFPDHREMAVVIAICTHLGCIPIPNEGLFGGFFCPCHGSHYDASGRIRQGPAPLNLEVPPYRWVDDKTIYLGKL
Protein: Sulfate transporter CysZ (P0A6J3)
Organism: Escherichia coli (strain K12)
Function: High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway. Does not transport thiosulfate.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00468, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00468}.
Interaction partners:
Sequence:
MVSSFTSAPRSGFYYFAQGWKLVSQPGIRRFVILPLLVNILLMGGAFWWLFTQLDVWIPTLMSYVPDWLQWLSYLLWPLAVISVLLVFGYFFSTIANWIAAPFNGLLAEQLEARLTGATPPDTGIFGIMKDVPRIMKREWQKFAWYLPRAIVLLILYFIPGIGQTVAPVLWFLFSAWMLAIQYCDYPFDNHKVPFKEMRTALRTRKITNMQFGALTSLFTMIPLLNLFIMPVAVCGATAMWVDCYRDKHAMWR
Protein: Oligopeptidase A (EC 3.4.24.70) (P27298)
Organism: Escherichia coli (strain K12)
Function: May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4).
Interaction partners:
- Ribosomal RNA small subunit methyltransferase J
- Chaperone protein ClpB
Sequence:
MTNPLLTPFELPPFSKILPEHVVPAVTKALNDCRENVERVVAQGAPYTWENLCQPLAEVDDVLGRIFSPVSHLNSVKNSPELREAYEQTLPLLSEYSTWVGQHEGLYKAYRDLRDGDHYATLNTAQKKAVDNALRDFELSGIGLPKEKQQRYGEIATRLSELGNQYSNNVLDATMGWTKLVTDEAELAGMPESALAAAKAQAEAKELEGYLLTLDIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAGKWDNSKVMEEILALRHELAQLLGFENYAFKSLATKMAENPQQVLDFLTDLAKRARPQGEKELAQLRAFAKAEFGVDELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKRIYGITAKERKDVDVWHPDVRFFELYDENNELRGSFYLDLYARENKRGGAWMDDCVGQMRKADGSLQKPVAYLTCNFNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISGVPWDAVELPSQFMENWCWEPEALAFISGHYETGEPLPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHAEFRPDQGAKILETLAEIKKLVAVVPSPSWGRFPHAFSHIFAGGYAAGYYSYLWADVLAADAFSRFEEEGIFNRETGQSFLDNILSRGGSEEPMDLFKRFRGREPQLDAMLEHYGIKG
Protein: DNAJB1 protein (DnaJ (Hsp40) homolog, subfamily B, member 1, isoform CRA_a) (cDNA, FLJ93008, Homo sapiens DnaJ (Hsp40) homolog, subfamily B, member 1 (DNAJB1),mRNA) (Q6FHS4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (Membrane-associated guanylate kinase inverted 3) (MAGI-3) (Q9EQJ9)
Organism: Mus musculus (Mouse)
Function: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15195140}; Peripheral membrane protein {ECO:0000269|PubMed:15195140}. Cell junction, tight junction {ECO:0000269|PubMed:15195140}. Nucleus {ECO:0000250}. Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity). {ECO:0000250}.
Interaction partners:
- Catenin beta-1
- Rap guanine nucleotide exchange factor 2
- Lysophosphatidic acid receptor 2
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Rap guanine nucleotide exchange factor
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Frizzled-4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Vang-like protein 2
- Dendrin
Sequence:
MSKTLKKKKHWLSKVQECAVSWAGPPGDLGAEIRGGAERGEFPYLGRLRDEAGGGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYLSLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDTESQRKRTTSVSKMERMDSSLPEEEEDEDKEAVNGSGSMETREMHSETSDCWMKTVPSYNQTNSSMDFRNYMMRDENLEPLPKNWEMAYTDTGMIYFIDHNTKTTTWLDPRLCKKAKAPEDCEDGELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVEEAKRKKQLGQAEIHSAKTDVERAHFTRDPSQLKGVLVRASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYPLPDDSEDPVVDIVAATPVINGQSLTKGETCMNTQDFKLGAMVLDQNGKSGQILASDRLNGPSESSEQRASLASSGSSQPELVTIPLIKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILRGGPCSPTKTAKTKTDTKENSGSLETINEPIPQPMPFPPSIIRSGSPKLDPSEVYLKSKTLYEDKPPNTKDLDVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRRKIFYGEKQPEDESHQAFSQNGSPRLNRAELPTRSAPQEAYDVTLQRKENEGFGFVILTSKSKPPPGVIPHKIGRVIDGSPADRCGGLKVGDHISAVNGQSIVDLSHDNIVQLIKDAGVTVTLTVVAEEEHHGPPSGTNSARQSPALQHRPMGQAQANHIPGDRIALEGEIGRDVCSSYRHSWSDHKHLAQPDTAVISVVGSRHNQSLGCYPVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGTGLIPDHGDWDTNSPSSSNVIYDEQPPPLPSSHSASTFEESHVPATEDSLTRVQICEKAEELKDTVQEKKSTLNGSQPEMKYQSVHKTMSKKDPPRGSGHGEKSRLKGENGVTRRGRSASPKKSVNRHSEEHLEKIPRPLKSDPKEKSRDRSLSPRKGESKGRLTIKAGSGQDPYRKDRGRSSSPKKQQKIGGNSLSNTEGKLSEAGSRRAAGHPRDSTEQLPDGREKSGVSRKDLKQSQPGKTRTKSPEKKSSKVDETSLPSKKTSSTAGRVVSEKEKGKKPTAGETSRETVEHTQISAKQLKQEAQEKTALGNADDHKGRESEVTDRCRERAGCTPQSSSLVKKAPITPGPWRVPRANKVTGTTGMADKQL
Protein: Oocyte maturation, beta (D3YX29)
Organism: Mus musculus (Mouse)
Interaction partners:
- Oocyte maturation, alpha
- Oogenesin-3
- Protein TCL1B3
- Protein TCL1B1
- Protein TCL1B5
Sequence:
MMSQLHICYGPVCEMQHHLPSFLDPLEFVIVYLETWVYKGLFDLRPELLLYFLNMHVLITSDGDLSETVLYIYGSKGIRIFAMFVIVSLACNLRTKRNRARAWARGLQSPVWWNRRYFI
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (Plasmin receptor) (Plasminogen-binding protein) (P0C0G7)
Organism: Streptococcus pyogenes serotype M1
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MVVKVGINGFGRIGRLAFRRIQNIEGVEVTRINDLTDPNMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGNFIKVSAERDPENIDWATDGVEIVLEATGFFAKKEAAEKHLHANGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASCTTNCLAPMAKALHDAFGIQKGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVVTLDKNVSVDEINAAMKAASNDSFGYTEDPIVSSDIVGVSYGSLFDATQTKVMEVDGSQLVKVVSWYDNEMSYTAQLVRTLEYFAKIAK