wanglab/gogpt-training-data huggingface dataset:
Protein: Spectrin repeat containing nuclear envelope protein 1 (H0Y325)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
EKIEQNGLALIQNKKEDVSSIVMSTLRELGQTWANLDHMVGQLKILLKSVLDQWSSHKVAFDKINSYLMEARYSLSRFRLLTGSLEAVQVQVDNLQNLQDDLEKQERSLQKFGSITNQLLKECHPPVTETLTNTLKEVNMRWNNLLEEIAEQLQSSKALLQLWQRYKDYSKQCASTVQQQEDRTNELLKAATNKDIADDEVATWIQDCNDLLKGLGTVKDSLFFLHELGEQLKQQVDASAASAIQSDQLSLSQHLCALEQALCKQQTSLQAGVLDYETFAKSLEALEAWIVEAEEILQGQDPSHSSDLSTIQERMEELKGQMLKFSSMAPDLDRLNELGYRLPLNDKEIKRMQNLNRHWSLISSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEQKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIIDGQRLLEQGQVDDRDEFNLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLVEVSYLPMSGLGSVPIPLQQARTLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELAEIQEKWKSASMRLEEQKKKLAFLLKDWEKCEKGIADSLEKLRTFKKKLSQSLPDHHEELHAEQMRCKELENAVGSWTDDLTQLSLLKDTLSAYISADDISILNERVELLQRQWEELCHQLSLRRQQIGERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAIAQENKIQLQQMGERLAKASHESKASEIEYKLGKVNDRWQHLLDLIAARVKKLKETLVAVQQLDKNMSSLRTWLAHIESELAKPIVYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLKSSERTAAFPSSSGVIYTVAKEELKKFEAFQRQVHECLTQLELINKQYRRLARENRTDSACSLKQMVHEGNQRWDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHWHDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSDVMIPESPEAYVKLTENAIKNTSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTVHKRWLRFLPF
Protein: Ceramide kinase-like isoform 32 (G0XYI0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MHIILGHIRSVDVCTFSSAGKLLCFGFSAMFGFGGRTLALAEKYRWMSPSQRRDFAIIKALAKLKPEDCKISFLLAGCSQNKQERKSQRSAESDCGGHWQTIQGQFLNISIMAMPCPCSMAPRGFTPDTRLHNGSMALRVVRNTTRSEFVKHLKRHSSVKNQGLYRYN
Protein: Mitogen-activated protein kinase kinase kinase 3 (EC 2.7.11.25) (MAPK/ERK kinase kinase 3) (MEK kinase 3) (MEKK 3) (Q99759)
Organism: Homo sapiens (Human)
Function: Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators.
Interaction partners:
- Cerebral cavernous malformations 2 protein
- Dual specificity mitogen-activated protein kinase kinase 5
- Sequestosome-1
- Dual specificity mitogen-activated protein kinase kinase 3
- TNF receptor-associated factor 6
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Mitogen-activated protein kinase kinase kinase 2
- NF-kappa-B essential modulator
- Dual specificity mitogen-activated protein kinase kinase 6
Sequence:
MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY
Protein: UBA domain-containing protein (Q388X6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMISVRKTVNVPTSNHAQGNAQRKKPKKKAEPSATSSVSHESRGGDGERIDQRIPASIQAMLSRSKCSLSESEIKAMVNSTAEDRCTALRMVFEGQSADEAIAFLLGAYNGKDSPKRSKTKSASSLLPIIITGLDNSSVEAARSNEWDAGSTAVFCGSSNSKESLSSAEVAPPLLSMQQTIWNSALLTDCESTAAHSRSVSPSIRMPSPKSHGHQIAKQPLTEVAVNTMSNTHVTSKAMGDHYTQLNATGSPLTMSVTTVPTVTAQGPSKQFNQSTCSAWDERLQTYIVHPNQLRCVGELEKMRTSPDAVRRGGGAALRRLTREGRTHSPVGGIAAARQCAQKPISTRNGELVAPLQMGHDEQHNRGFGNDEKQPQQRQRESKKTAKGVSESGHQEQQAITRDAATAAPKSPSGKENVFARLFSASKYQPQSYAATERSRASTSNIWGGLSPLNSPCMRLCDSVHEESASERHPVERVTSETRFSHYGSALRLQRTQSAIDSRYRTQRQRYFQSFYTQMRKPRSELHTGQVVRPSI
Protein: Probable nuclear hormone receptor HR38 (dHR38) (Nuclear receptor subfamily 4 group A member 4) (P49869)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to NGFI-B response elements. Plays an important role in late stages of epidermal metamorphosis.
Subcellular location: Nucleus.
Interaction partners:
- Protein ultraspiracle
- RAC serine/threonine-protein kinase
- Steroid receptor seven-up, isoform A
- Ecdysone receptor
Sequence:
MMRDRLASLIVVKQEGGSNTSISHHQATAIKCEASLYTESSLFQEINNNSCYRQNLNAPTHQQSHTSHLQHAQQHQTHQQHPLLPPPLPTLPLIYPCRNLFPDGCDINHLACCSSSNSNSNCNSDSNSTSSSPGNSHFFANGNTCAAALTPAPPATEPRKIKPLGAGKLKVGKTDSNSDSNSNCDSRAAAAASTSATSATSATTLAATAAATAAAAEAGGAASAAAAAKISQVRLTNQATTSMLLLQPNSSFSSLSPFDNFSTQTASTTTTTSASAAGHHQHHNHLLHQQHHNQQQQQQQQQQQQQQQQQQQEHLQQQHQQQLVSPQQHLLKSETLLSHEEDQLISNLTDSSVVSHSELFSDLFFPSDSNNSLLSPTTSGYPDNPAEDLTSSIENLTKLTCLRDKRLSSIPEQQLSSEQEQQLCLLSLRSSSDPAIALHAQQQQQQQQQQQQQQQQHQQQQQHLQLQLISPIGGPLSCGSSLPSFQETYSLKYNSSSGSSPQQASSSSTAAPTPTDQVLTLKMDEDCFPPLSGGWSASPPAPSQLQQLHTLQSQAQMSHPNSSNNSSNNAGNSHNNSGGYNYHGHFNAINASANLSPSSSASSLYEYNGVSAADNFYGQQQQQQQQSYQQHNYNSHNGERYSLPTFPTISELAAATAAVEAAAAATVGGPPPVRRASLPVQRTVSPAGSTAQSPKLAKITLNQRHSHAHAHALQLNSAPNSAASSPASADLQAGRLLQAPSQLCAVCGDTAACQHYGVRTCEGCKGFFKRTVQKGSKYVCLADKNCPVDKRRRNRCQFCRFQKCLVVGMVKEVVRTDSLKGRRGRLPSKPKSPQESPPSPPISLITALVRSHVDTTPDPSCLDYSHYEEQSMSEADKVQQFYQLLTSSVDVIKQFAEKIPGYFDLLPEDQELLFQSASLELFVLRLAYRARIDDTKLIFCNGTVLHRTQCLRSFGEWLNDIMEFSRSLHNLEIDISAFACLCALTLITERHGLREPKKVEQLQMKIIGSLRDHVTYNAEAQKKQHYFSRLLGKLPELRSLSVQGLQRIFYLKLEDLVPAPALIENMFVTTLPF
Protein: Flagellin (Q729A8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362073}. Bacterial flagellum {ECO:0000256|RuleBase:RU362073}.
Interaction partners:
- Flagellar protein FliS
- Flagellar assembly factor FliW
- Uncharacterized protein
- Flagellar hook-associated protein 2
- Flagellar hook-associated protein 1
- Flagellar motor switch protein FliG
- histidine kinase
- Flagellar hook protein FlgE
- Flagellar motor switch protein FliN
- Flagellum-specific ATP synthase FliI
Sequence:
MSLVINHNMMAMNAAGNLSNSYGKLSTSVRRLSSGLRVGTAADDAAGLAIRELMRSDISALNQGVRNANDAISLIQTADGALGVIDEKLIRMKELAEQAATGTYTSDQRLIIDSEYQAMASEITRIANATDFNGLHLLNGNLSSDTHDGSGLQSTGKMKIHFGTANDSAEDYYYVQIGTSTASALGVGNQATAGSAGYTISTQSAAQQALVAIQNAIISKDNIRASLGALQNRLENTISNLRTQAENLQSAESRISDVDVSSEMTEFVRQQILTQSAVAMLSQANSLPRMAMQLLGG
Protein: Effector protein OEC45 (A0A088QTX9)
Organism: Golovinomyces orontii
Interaction partners:
Sequence:
MQPNPNAAQPHPNAADCPYEGRICDKKDIEPYRSVKYLRATCKKCGKITNNNVVGKKNYKLRYCLYCDMKYIHDLSLRKTKMLYKCPDCETELR
Protein: Rho-related protein racC (P34149)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Serine/threonine-protein kinase pakB
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- Darlin
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Protein pirA
- Nck-associated protein 1 homolog
- Protein BRICK1
Sequence:
MSAAEVIKLVVIGDGAVGKTCLLISYANNRFPEDYIPTVFDNYVVNLTAGDRNIELGLWDTAGQEEYDKLRPLSYANANVFLICFSITNPVSFENVYTKWYPEVMHFCPEVPQILVGTKLDTRDDRGVLDKLQQTGHKPITTEQGNDLARRIKAIKYMECSAKTSQNLKQVFDEAIKSVLFIKKKKSKCIVM
Protein: Uncharacterized protein (Q38A75)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPIKGSRKSPTKGPKEVCKNGSPHVGPDSVRRKENPSESLISRLQFILSGAVGGRPGGCADRVGVTGPPKGGGELVRLATILHGCFLITMAGKAQLGVGKIDHCVIATVDERWLEAITRYCGFTVVPRDIIECGAAFPEWLSAFESVVEHGVSNGGTNCAHSTPVVKVKLVRNLVPSVAEAEQFLRERWGGENSWRHGRVEEVLNSSSTAAVSSNSAGEVLRFNEGAGAAATSVVGSVSDEELLRQLSAELRATLTGERLKGVLAQMRREALGLEAREEELINRRQRQERLLSTYDLARVLLGEKRSACNVAELVEQMVRQNRFGDGKEGIIEQLVCLTKVKESGMTIIRVDEGKGTNESKRKRRAKATSDTASLTSRRVELSASSTLKELEISVLRLDRTLASRAGLHQVLQREQPQ
Protein: L(3)mbt interactor in ovarian somatic cells, isoform A (L(3)mbt interactor in ovarian somatic cells, isoform B) (RE68603p) (Q9W4W7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD20362p
- GEO11824p1
- DNA methyltransferase 1-associated protein 1
- Enhancer of polycomb-like protein
- Chromatin modification-related protein MEAF6
Sequence:
MKQSKDEDKEESPVQPTTHNSSAGSNGHDAKSPVVTTAPAATCSVSVSDASGAGASVRTTGRVKKPKQVYDPSDNYVSRASSNRNSLSSVPATSNVQSPPVKEATDSQDSTTSPVSEQQQQQLQQAAQLRNFDTCQKCGKSEPKRGSGHKSNFLTCKGCMQKWHFPCLPITFHNQSTARKKFKCDKCRYCRLCNVRGPGLSICSLCVDAYHPDCNDPTLKQSKAVEANPNWRCFRCEACNIGGSTSASSEEQTGARKSTASREDQAQPVVPRKSNAGRKKRVQSEPTGQEKAAKIEKLAKRRQPLKTEKKKEYKKEEDEEPAQIKVKVEKVEPVDMETEQIENNDLPGPEQESLSLRLTPITAVERRSHPVSTWSVEQVVQFVAKRYPKEANVFRYQDIDGASLLLLNRHDVMNGFGLKLGPALRVFELVMSLQTQSNDVGLAWLD
Protein: Piwi-like protein 1 (EC 3.1.26.-) (Q9JMB7)
Organism: Mus musculus (Mouse)
Function: Endoribonuclease that plays a central role in postnatal germ cells by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle. Acts as an endoribonuclease that cleaves transposon messenger RNAs. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Probable component of some RISC complex, which mediates RNA cleavage and translational silencing. Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability. Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11578866, ECO:0000269|PubMed:12062093, ECO:0000269|PubMed:16787948, ECO:0000269|PubMed:16938833, ECO:0000269|PubMed:19020299, ECO:0000269|PubMed:19584108}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also present in chromatoid body.
Interaction partners:
- Tudor domain-containing protein 6
- Tudor and KH domain-containing protein
- ATP-dependent RNA helicase TDRD9
- Tudor domain-containing protein 1
- ATP-dependent RNA helicase DDX4
- Tudor domain-containing protein 5
- Protein maelstrom homolog
- RNA helicase Mov10l1
- RING finger protein 17
- Deleted in azoospermia-like
Sequence:
MTGRARARARGRARGQETVQHVGAAASQQPGYIPPRPQQSPTEGDLVGRGRQRGMVVGATSKSQELQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVKLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGRCHAFDGTILFLPKRLQHKVTEVFSQTRNGEHVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPSDPIDIPNHRLVIWPGFTTSILQYENNIMLCTDVSHKVLRSETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKDDNVQRELRDWGLSFDSNLLSFSGRILQSEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGIQMKKAIMIEVDDRTEAYLRALQQKVTSDTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDMPLKLAMIVGIDCYHDTTAGRRSIAGFVASINEGMTRWFSRCVFQDRGQELVDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL
Protein: Aminopeptidase (EC 3.4.11.1) (Leucine aminopeptidase) (PaAP) [Cleaved into: Aminopeptidase AP58; Aminopeptidase AP56; Aminopeptidase AP28] (Q9HZQ8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: A secreted aminopeptidase. Acts on free N-terminal amino groups with a very strong preference for Leu- followed by Met- and Ala-, and no activity on Glu- or Gly- peptides (an exhaustive analysis was not performed). Both the AP56 and AP28 forms have activity.
Subcellular location: Secreted {ECO:0000269|PubMed:11533066}.
Interaction partners:
- Elastase
- Lysyl endopeptidase
- Protease LasA
- Chitin-binding protein CbpD
- Serralysin
- Immunomodulating metalloprotease
- Type IVb pilin, Flp
- Secretion protein XqhA
Sequence:
MSNKNNLRYALGALALSVSAASLAAPSEAQQFTEFWTPGKPNPSICKSPLLVSTPLGLPRCLQASNVVKRLQKLEDIASLNDGNRAAATPGYQASVDYVKQTLQKAGYKVSVQPFPFTAYYPKGPGSLSATVPQPVTYEWEKDFTYLSQTEAGDVTAKVVPVDLSLGAGNTSTSGCEAEDFANFPAGSIALIQRGTCNFEQKAENAAAAGAAGVIIFNQGNTDDRKGLENVTVGESYEGGIPVIFATYDNGVAWSQTPDLQLHLVVDVVRKKTETYNVVAETRRGNPNNVVMVGAHLDSVFEGPGINDNGSGSAAQLEMAVLLAKALPVNKVRFAWWGAEEAGLVGSTHYVQNLAPEEKKKIKAYLNFDMIGSPNFGNFIYDGDGSDFGLQGPPGSAAIERLFEAYFRLRGQQSEGTEIDFRSDYAEFFNSGIAFGGLFTGAEGLKTEEQAQKYGGTAGKAYDECYHSKCDGIANINQDALEIHSDAMAFVTSWLSLSTKVVDDEIAAAGQKAQSRSLQMQKSASQIERWGHDFIK
Protein: Uncharacterized protein (Q57WW0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein mS41
- Enoyl-CoA hydratase/isomerase domain-containing protein
- Ribosomal protein S9
- Uncharacterized protein
- Pentacotripeptide-repeat region of PRORP domain-containing protein
- Uncharacterized protein
- Opioid growth factor receptor
- LysM domain-containing protein
Sequence:
MVLRRWFPLLGVHRVGYTHPSTLPVPCAQRWDLRLARARIFQEYIEEKAPGAWQLEDERSMSPEFKTFTGYPMRDMRPGYGQNLPDYIMKKRLPNNTHYELFARRDIPNEDNAMYGKYLYDMTVHGTSLPSTYRMHKDINKAQRNDRKLSGNRFKVLCSSGAKNPPSGWEPIPDATEEEED
Protein: Uncharacterized protein (Q8C463)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
APVCDTTLRQVRQVLERAPVCDTTLRQVRQVLERAPVCDTTLRQVRQVLERAPVCDTTLRQVRQVLERAPVCDTTLRQVRQVLERAPVCDTTLRHGTAGIREGTCV
Protein: Uncharacterized oxidoreductase YhhX (EC 1.-.-.-) (P46853)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YnfO
- Putative oxidoreductase YceM
- Putative transposase InsK for insertion sequence element IS150
- Uncharacterized protein YgaC
Sequence:
MVINCAFIGFGKSTTRYHLPYVLNRKDSWHVAHIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAQAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRPVAETKPGLPQDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFEAQLFYGDLKAIVKTSHLVKIDYPKFIVHGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYVNDEGVTVREEMKPEMGDYGRVYDALYQTITHGAPNYVKESEVLTNLEILERGFEQASPSTVTLAK
Protein: Monocarboxylate transporter 4 (MCT 4) (Solute carrier family 16 member 3) (P57787)
Organism: Mus musculus (Mouse)
Function: Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (By similarity). Plays a predominant role in the L-lactate efflux from highly glycolytic cells (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:O15427}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is dependent upon the BSG/MCT4 interaction. Basolateral sorting signals (BLSS) in C-terminal cytoplasmic tail ensure its basolateral expression in polarised epithelial cells. {ECO:0000250|UniProtKB:O15427}.
Interaction partners:
- Basigin
- Carbonic anhydrase 9
- L-lactate dehydrogenase A chain
- Integrin beta-1
- Pyruvate kinase PKM
- Embigin
- Solute carrier family 2, facilitated glucose transporter member 3
- Hexokinase-2
Sequence:
MGGAVVDEGPTGIKAPDGGWGWAVLFGCFIITGFSYAFPKAVSVFFKELMHEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQIYLTTGVITGLGLALNFQPSLIMLNRYFNKRRPIANGLAAAGSPVFLCALSPLGQLLQDHYGWRGGFLILGGLLLNCCVCAALMRPLVAPQVGGGTEPRGPQRPPQRLLDLSVFRDRGFLIYAVAASIMVLGLFVPPVFVVSYAKDMGVPDTKAAFLLTILGFIDIFARPTAGFITGLKKVRPYSVYLFSFAMFFNGFTDLTGSTATDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTQKFSSAIGLVLLLEAVAVLIGPPSGGKLLDATKVYKYVFILAGAEVLTSSLVLLLGNFFCIGKRKRPEVTEPEEVASEEKLHKPPVDVGVDSREVEHFLKAEPEKNGEVVHTPETSV
Protein: 3-isopropylmalate dehydratase large subunit, chloroplastic (EC 4.2.1.33) (2-(omega-methylthio)alkylmalate dehydratase large subunit) (EC 4.2.1.170) (AtLEUC) (Isopropylmalate isomerase large subunit 1) (AtIIL1) (IPMI LSU1) (Methylthioalkylmalate isomerase large subunit) (MAM-IL) (Q94AR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. Functions in both the biosynthesis of leucine and in the methionine chain elongation pathway of aliphatic glucosinolate formation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20663849}.
Interaction partners:
- 3-isopropylmalate dehydrogenase 1, chloroplastic
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase small subunit 1
- 2-isopropylmalate synthase 1, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
Sequence:
MASVISSSPFLCKSSSKSDLGISSFPKSSQISIHRCQKKSISRKIVSVMAPQKDRSPGTTGSVKTGMTMTEKILARASEKSLVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKAKVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKYFYDITDLGNFKANPDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTFLVPATQKVWMDVYALPVPGAGGKTCAQIFEEAGCDTPASPSCGACLGGPADTYARLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREFLQ
Protein: Cadherin 13 (A0A8I5XWM0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTSPVPRQKRSIVVSPILIPENQRQPFPRDVGKVVDSDRPEGSKFRLTGKGVDQDPKGTFRINENTGSVSVTRTLDRETIATYQLFVETTDASGRTLEGPVPLEVIVIDQNDNRPIFREGPYIGHVMEGSPTGTTVMRMTAFDADDPATDNALLRYNIRQQTPDKPSPNMFYIDPEKGDIVTVVSPALLDRETLENPKYELIIEAQDMAGLDVGLTGTATATIVIDDKNDHSPKFTKKEFQATVEEGAVGVIVNLTVEDKDDPATGAWRAAYTIINGNPGQSFEIHTNPQTNEGMLSVVKPLDYEISAFHTLLIKVENEDPLVPDVSYGPSSTATVHITVLDVNEGPVFYPDPMMVTKQENISVGSVLLTVNATDPDSLQHQTIRYSVYKDPAGWLSINPINGTVDTTAVLDRESPFVHNSVYTALFLAIDSGNPPATGTGTLMITLEDVNDNAPVIYPTVAEVCDDARNLSVVILGASDKDLHPNTDPFKFEIHKQTVPDKVWKISKINNTHALVSLLQNLNKANYNLPIMVTDSGKPPMTNITDLRVQVCSCKNSKVDCNAAGTLHLSLSLLLLFSLLSLLSGKLA
Protein: E3 ubiquitin-protein ligase IpaH1.4 (EC 2.3.2.27) (Invasion plasmid antigen 1.4) (A0A0H2USG1)
Organism: Shigella flexneri
Function: E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP. Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. By promoting degradation of host RNF31/HOIP, IpaH1.4 prevents formation of the bacterial ubiquitin coat and activation of host cell innate immunity.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}.
Interaction partners:
Sequence:
MIKSTNIQAIGSGIMHQINNVYSLTPLSLPMELTPSCNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLSENGSNHIA
Protein: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2Aa) (Medium tumor antigen-associated 61 kDa protein) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha) (Q32PI5)
Organism: Bos taurus (Bovine)
Function: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12912990}. Nucleus {ECO:0000250|UniProtKB:P30153}. Chromosome {ECO:0000250|UniProtKB:P30153}. Chromosome, centromere {ECO:0000250|UniProtKB:P30153}. Lateral cell membrane {ECO:0000250|UniProtKB:P30153}. Cell projection, dendrite {ECO:0000250|UniProtKB:P30153}. Note=Centromeric localization requires the presence of BUB1. Recruited to chromatin and transcription pause-release checkpoint via its association with the Integrator complex. {ECO:0000250|UniProtKB:P30153}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Shugoshin 1
Sequence:
MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELHKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDSTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPVLEKLTQDQDVDVKYFAQEALTVLSLA
Protein: Stromal membrane-associated protein 1 (Q91VZ6)
Organism: Mus musculus (Mouse)
Function: GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis.
Subcellular location: Cell membrane {ECO:0000305|PubMed:9644265}; Peripheral membrane protein {ECO:0000305|PubMed:9644265}; Cytoplasmic side {ECO:0000305|PubMed:9644265}.
Interaction partners:
Sequence:
MATRSCREKAQKLNEQHQLILSKLLREEDNKYCADCEAKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTPEQIQCMQDMGNTKARLLYEANLPENFRRPQTDQAVEFFIRDKYEKKKYYDKNAIAITNKEKEKKKDEKKREKEPEKPAKPLTTEKLPKKEEQQLEPKKSTSPKNAAEPTIDLLGLDGPAEAPVTNGNPATAPALSDDLDIFGPMISNPLPAAVMPPAQGTASVPAPATLSTVTSGDLDLFTEQTTKSEEVAKKQLSKDSILSLYGTGAQQSTPGVFMGPTNIPFTSQAPTAFQGFPSMGVPVPAAPGLIGNMMGQNTGMMVGMPMHNGFMGNAQTGVMPLPQNVVGPQGGMVGQMGAPQSKFGLPQAQQPQWNLSQMNQQMAAMNLSSANASAGFGQPPSTTAGWSGSSSGQTLSTQLWK