wanglab/gogpt-training-data huggingface dataset:
Protein: Bridging integrator 2 (Breast cancer-associated protein 1) (Q9UBW5)
Organism: Homo sapiens (Human)
Function: Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23285027}. Cell projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23285027}. Cell projection, phagocytic cup {ECO:0000269|PubMed:23285027}. Note=Associates with membranes enriched in phosphoinositides. Detected in the actin-rich cell cortex at the leading edge of migrating cells. Detected at podosomes, at an actin-rich ring-like structure. {ECO:0000269|PubMed:23285027}.
Interaction partners:
- Bridging integrator 3
- Myc box-dependent-interacting protein 1
- Amphiphysin
- Tyrosine-protein kinase BTK
Sequence:
MAEGKAGGAAGLFAKQVQKKFSRAQEKVLQKLGKAVETKDERFEQSASNFYQQQAEGHKLYKDLKNFLSAVKVMHESSKRVSETLQEIYSSEWDGHEELKAIVWNNDLLWEDYEEKLADQAVRTMEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIGCYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEKQHSNKVFVVKGLSSSSRRSLVISPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNGPAQAQPSPTTERAKSQEEVLPSSTTPSPGGALSPSGQPSSSATEVVLRTRTASEGSEQPKKRASIQRTSAPPSRPPPPRATASPRPSSGNIPSSPTASGGGSPTSPRASLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKENENIHNQNPEELCTSPTLMTSQVASEPGEAKKMEDKEKDNKLISANSSEGQDQLQVSMVPENNNLTAPEPQEEVSTSENPQL
Protein: L-amino-acid oxidase (DRS-LAAO) (LAO) (EC 1.4.3.2) (Q4F867)
Organism: Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active on L-Leu followed by L-Phe and L-Ile, moderately active on L-Asp, L-Glu, and L-Lys, and not active on L-Pro, L-Asn, L-Gly, L-Ser and L-Cys. Exhibits diverse biological activities such as antibacterial activity (Minimal inhibitory concentrations (MIC) are 9.0 ug/ml against S.aureus, 144.0 ug/ml against P.aeruginosa and 288.0 ug/ml against E.coli) and inhibition of ADP- and TMVA-induced platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also induce hemolysis, edema, apoptosis and have antiparasitic activities.
Subcellular location: Secreted {ECO:0000269|PubMed:19523971}.
Interaction partners:
Sequence:
ADDKNPLEECFREDDHRIVREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVRFKARVIKIQQNAEKVTVTYQTTQKNLLLETVDYVIVCTTSRAARRITFKPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIQGGKSTTDLPSRFIYYPNHNFTTGVGVIIAYGIGDDANFFQALNLNECADIVFNDLSSIHQLPKKDLQTFCYPSIIQKWSLDKYAMGAITTFTPYQFQHFSEALTAPVGRIFFAGEYTANAHGWIDSTIKSGLTAARDVNRASEL
Protein: Proliferation-associated protein A (Q1ZXG4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Large ribosomal subunit protein uL18
- 60S ribosomal export protein NMD3
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL4
- Ribosome biogenesis protein NOP53
- Nucleolar GTP-binding protein 2
Sequence:
MSNKDQEIKEEAPVAIEDLSNPVVVDSYNAAGIIANNAIKHVISKCVVGALVVDICQYGDDFIEAEAAKTFTKRKNLEKGIAFPTCVSVNNCVGHFSPLKGNTRTLKQGDVVKIDLGCHIDGYIAVGAHTIIIGNTSAESMTGKVADAICAAHYALEAALRMIRPGKTSNEVTQVIEKISDMYGVTSVSGILSHELKRFIIDGEKVIFSKNEPSQKIQTYEFQENEVYCIDIVMSTGEGKAREEADRPTIYRRNLDSTYKLKSKASRDFKDQIVKRYSALPFPLRNFDEKVSKLGLVELVEHQVLAAYPVLFDRSGCEVVQFKTTVLVLPNGNHKLIGTEFPLPFVRSEFSVTDDAIKALIASPLKINKKAAKKASATTIDVKMQ
Protein: Reduced folate transporter (Methotrexate carrier 1) (MTX-1) (MTX1) (Plasma membrane folate antiporter SLC19A1) (Reduced folate carrier 1) (RFC-1) (RFC1) (Solute carrier family 19 member 1) (Q62866)
Organism: Rattus norvegicus (Rat)
Function: Antiporter that mediates the import of reduced folates. Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates (By similarity). Has high affinity for N5-methyltetrahydrofolate, the predominant circulating form of folate (By similarity). Also able to mediate the import of antifolate drug methotrexate. 5-amino-4-imidazolecarboxamide riboside (AICAR), when phosphorylated to AICAR monophosphate, can serve as an organic anion for antiporter activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19243012}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}. Apical cell membrane {ECO:0000250|UniProtKB:P41440}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}. Basolateral cell membrane {ECO:0000269|PubMed:19243012}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}.
Interaction partners:
- Proton-coupled folate transporter
- Gamma-glutamyl hydrolase
Sequence:
MVPTGQVAEKQACEEPRQDRELKSWRWLVFYLCFFGFMAQLRPGESFITPYLLERNFTKEQVTNEIIPMLPYSHLAVLVPIFLLTDYLRYKPVLVLQCLSFVCVWLLLLLGTSVVHMQLMEVFYSITMAARIAYSSYIFSLVQPSRYQRMASYSRAAVLLGVFISSVLGQVLVTLGGISTYMLNCISLGFILFSLSLSLFLKRPKRSLFFNRSALVQGALPCELDQMHPGPGRPEPRKLERMLGTCRDSFLVRMLSELVKNVRQPQLRLWCLWWVFNSAGYYLITYYVHVLWKITDSRLNYNGAVDAASTLLSAITAFTAGFVNIRWALWSKLVIASVIAIQAGLVFCMFQIPDIWVCYVTFVLFRGAYQFLVPIATFQIASSLSKELCALVFGINTFLATALKTSITLVVSDKRGLGLQVHQQFRIYFMYFLTLSIICLAWAGLDGLRYYRRGRHQPLAQAQALSPLEDSVQAISLQDGDLRRPQPSAPQLLPEDGSVEDGRADLRVEAKA
Protein: All-trans-retinol dehydrogenase [NAD(+)] ADH4 (EC 1.1.1.105) (ADH2) (Alcohol dehydrogenase 2) (Alcohol dehydrogenase 4) (Alcohol dehydrogenase class II) (Alcohol dehydrogenase II) (Q9QYY9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (By similarity). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Also catalyzes the reduction of benzoquinones (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase 1A1
- Cytochrome P450 2E1
- Retinal dehydrogenase 2
- Aldehyde dehydrogenase, cytosolic 1
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase family 3 member B1
- Cytochrome P450 26A1
- Aldehyde dehydrogenase family 3 member B3
- Aldehyde oxidase 3
Sequence:
MGTQGKVIKCKAAIAWKTGSPLCIEEIEVSPPKACEVRIQVIATCVCPTDINATDPKKKALFPVVLGHECAGIVESVGPGVTNFKPGDKVIPFFAPQCKRCKLCLSPLTNLCGKLRNFKYPTIDQELMEDRTSRFTCKGRSIYHFMGVSSFSQYTVVSEANLARVDDEANLERVCLIGCGFSSGYGAAINTAKVTPSSTCAVFGLGCVGLSAIIGCKIAGASRIIAIDINGEKFPKAKALGATDCLNPRELDKPVQDVITELTAGGVDYSLDCAGTAQTLKAAVDCTVLGWGSCTVVGAKVDKMTIPTVDVILGRSINGTFFGGWKSVDSVPNLVSDYKNKKFDLDLLVTHALPFESINDAIDLMKEGKSIRTILTF
Protein: Zinc finger CCCH domain-containing protein 18 (Nuclear protein NHN1) (Q86VM9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Serrate RNA effector molecule homolog
- THO complex subunit 2
- Nuclear cap-binding protein subunit 1
- Bromodomain-containing protein 4
- Zinc finger CCHC domain-containing protein 8
- Splicing factor 3A subunit 2
- Serine/arginine repetitive matrix protein 2
- RNA-binding protein 7
- Splicing factor 3A subunit 1
Sequence:
MDVAESPERDPHSPEDEEQPQGLSDDDILRDSGSDQDLDGAGVRASDLEDEESAARGPSQEEEDNHSDEEDRASEPKSQDQDSEVNELSRGPTSSPCEEEGDEGEEDRTSDLRDEASSVTRELDEHELDYDEEVPEEPAPAVQEDEAEKAGAEDDEEKGEGTPREEGKAGVQSVGEKESLEAAKEKKKEDDDGEIDDGEIDDDDLEEGEVKDPSDRKVRPRPTCRFFMKGNCTWGMNCRFIHPGVNDKGNYSLITKADPFPPNGAPPLGPHPLMPANPWGGPVVDEILPPPPPEPPTESAWERGLRHAKEVLKKATIRKEQEPDFEEKRFTVTIGEDEREFDKENEVFRDWNSRIPRDVRDTVLEPYADPYYDYEIERFWRGGQYENFRVQYTETEPYHNYRERERERERENRQRERERERERDRERERRQRERERERERERDKERQRRKEEWERERAKRDEKDRQHRDRDREKEREKEKGKPKPRSPQPPSRQAEPPKKEAATTGPQVKRADEWKDPWRRSKSPKKKLGVSVSPSRARRRRKTSASSASASNSSRSSSRSSSYSGSGSSRSRSRSSSYSSYSSRSSRHSSFSGSRSRSRSFSSSPSPSPTPSPHRPSIRTKGEPAPPPGKAGEKSVKKPAPPPAPPQATKTTAPVPEPTKPGDPREARRKERPARTPPRRRTLSGSGSGSGSSYSGSSSRSRSLSVSSVSSVSSATSSSSSAHSVDSEDMYADLASPVSSASSRSPAPAQTRKEKGKSKKEDGVKEEKRKRDSSTQPPKSAKPPAGGKSSQQPSTPQQAPPGQPQQGTFVAHKEIKLTLLNKAADKGSRKRYEPSDKDRQSPPPAKRPNTSPDRGSRDRKSGGRLGSPKPERQRGQNSKAPAAPADRKRQLSPQSKSSSKVTSVPGKASDPGAASTKSGKASTLSRREELLKQLKAVEDAIARKRAKIPGKA
Protein: MYB31 transcription factor31 (ZmMYB31) (Myb-related protein Hv1) (B4FNX4)
Organism: Zea mays (Maize)
Function: Transcription factor that regulates negatively the expression of caffeic acid O-methyl-transferase genes (COMTs) and of other genes involved in the biosynthesis of lignin, thus preventing lignification.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MGRSPCCEKAHTNKGAWTKEEDERLVAHIRAHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIVKLHSVLGNKWSLIAGRLPGRTDNEIKNYWNTHIRRKLLSRGIDPVTHRPVTEHHASNITISFETEVAAAARDDKKGAVFRLEEEEERNKATMVVGRDRQSQSQSHSHPAGEWGQGKRPLKCPDLNLDLCISPPCQEEEEMEEAAMRVRPAVKREAGLCFGCSLGLPRTADCKCSSSSFLGLRTAMLDFRSLEMK
Protein: m7GpppN-mRNA hydrolase dcap-2 (EC 3.6.1.62) (Nudix hydrolase 5) (mRNA-decapping enzyme 2) (O62255)
Organism: Caenorhabditis elegans
Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. RNA-decapping enzyme although it does not bind the RNA cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia. Required for the developmental axon guidance and regrowth of PLM touch receptor neurons. Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons. Promotes survival at high temperatures.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:18439994}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18439994}. Note=Localizes to perinuclear puncta in pachytene-stage germ cells (PubMed:18439994). Diffusely localized to cytoplasmic puncta in maturing oocytes (PubMed:18439994). {ECO:0000269|PubMed:18439994}.
Interaction partners:
- mRNA-decapping enzyme 1
- ATP-dependent RNA helicase cgh-1
- 5'-3' exoribonuclease 1
- Protein PAT1 homolog 1
- FHA domain-containing protein
- CCR4-NOT transcription complex subunit 7
- Protein LSM14 homolog car-1
- U6 snRNA-associated Sm-like protein LSm1
- Regulator of nonsense transcripts 1
- NAD
Sequence:
MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP
Protein: Transcriptional regulator, LysR family (Q9KT56)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Interaction partners:
- Transcriptional regulator, LysR family
- Transcriptional regulator, LysR family
- Transcriptional regulator, LysR family
Sequence:
MQHNVSETMKLDDLNLFRLVVENGSYTSTSKKTMIPVATITRRIQALEDSLNLRLLNRHARKLTLTEAGERFYKDCSPLLERLASMTEEITDECRGASGRIRISAPSNLTKRMMMPMFNAFMEKYPDIHIELMMSNQADDLDPTEWDVIFRVGPQRDSSLIARKIGEVKDILVASPQYLSSHPQPTHAEELHQHQLLKGYPLLKWQLTNSQGETVVNSDRGRFQASALNVVRSACSEGLGITLMPDVMLREFLEDGSLVQVLSDWSSNPRDIYMLYNHKDHQPEKVRLFIDFVIGYHLQ
Protein: Meis homeobox 2 (A0A0G2JT27)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MLLSYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLVRLTVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGPMSGMGMNMGMDGQWHYM
Protein: CUGBP Elav-like family member 4 (K7EJW4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGGSTPPGITAPAVPSIPSPIGVNGFTGLPPQANGQPAAEAVFANGIHPYPAQSPTAADPLQQAYAGVQQYAGRFVSFDNPASAQTAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: Interleukin-24 (IL-24) (Melanoma differentiation-associated gene 7 protein) (MDA-7) (Suppression of tumorigenicity 16 protein) (Q13007)
Organism: Homo sapiens (Human)
Function: Multifunctional cytokine mainly produced by T-cells that plays a regulatory role in immune response, tissue homeostasis, host defense, and oncogenesis. Possesses antiviral functions and induces the type I intereferon response during influenza infection. Signals through two receptor complexes IL20RA/IL20RB or IL20RB/IL22RA1. In turn, stimulates the JAK1-STAT3 and MAPK pathways and promotes the secretion of pro-inflammatory mediators including IL8 and MMP1. Intracellularly, maintains endoplasmic reticulum homeostasis by restricting the eIF2alpha-CHOP pathway-mediated stress signal (By similarity). In addition, acts as a quality control mechanism for the ubiquitin proteasome system by alerting the cell to proteasome dysfunction through activation of PKR/EIF2AK2 (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:11706020}.
Interaction partners:
- Interleukin-20 receptor subunit beta
- Interleukin-22 receptor subunit alpha-1
- Interleukin-20 receptor subunit alpha
- Interleukin-19
- Interleukin-20
- Interleukin-10 receptor subunit beta
- Interleukin-10 receptor subunit alpha
- Interleukin-22 receptor subunit alpha-2
- Interleukin-10
- Interleukin-22
Sequence:
MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL
Protein: Pescadillo homolog (B5MCF9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03028}. Chromosome {ECO:0000256|HAMAP-Rule:MF_03028}. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. {ECO:0000256|HAMAP-Rule:MF_03028}.
Interaction partners:
Sequence:
MGGLEKKKYERGSATNYITRNKARKKLQLSLADFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIRFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNTVERLKDNKPNYKLDHIIKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFMHYIIAARALRKVFLSIKGIYYQAEHPTDVDYRVMATFTEFYTTLLGFVNFRLYQLLNLHYPPKLEGQAQAEAKAGEGTYALDSESCMEKLAALSASLARVVVPATEEEAEVDEFPTDGEMSAQEEDRRKELEAQEKHKKLFEGLKFFLNREVPREALAFIIRSFGGEVSWDKSLCIGATYDVTDSRITHQIVDRPGQQTSVIGRCYVQPQWVFDSVNARLLLPVAEYFSGVQLPPHLSPFVTEKEGDYVPPEKLKLLALQRGEDPGNLNESEEEEEEDDNNEGDGDEEGENEEEEEDAEAGSEKEEEARLAALEEQRMEGKKPRVMAGTLKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDEAVRSEKKAKKARPE
Protein: Acetolactate synthase large subunit IlvB1 (ALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase large subunit) (AHAS) (P9WG41)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate.
Interaction partners:
- Putative acetolactate synthase small subunit
- Ketol-acid reductoisomerase
- 2-isopropylmalate synthase
- 3-isopropylmalate dehydrogenase
- L-threonine dehydratase biosynthetic IlvA
- Dihydroxy-acid dehydratase
- Putative acetolactate synthase large subunit IlvB2
- Acetolactate synthase large subunit IlvG
- Putative acetolactate synthase large subunit IlvX
- 2-oxoglutarate oxidoreductase subunit KorA
Sequence:
MSAPTKPHSPTFKPEPHSAANEPKHPAARPKHVALQQLTGAQAVIRSLEELGVDVIFGIPGGAVLPVYDPLFDSKKLRHVLVRHEQGAGHAASGYAHVTGRVGVCMATSGPGATNLVTPLADAQMDSIPVVAITGQVGRGLIGTDAFQEADISGITMPITKHNFLVRSGDDIPRVLAEAFHIAASGRPGAVLVDIPKDVLQGQCTFSWPPRMELPGYKPNTKPHSRQVREAAKLIAAARKPVLYVGGGVIRGEATEQLRELAELTGIPVVTTLMARGAFPDSHRQNLGMPGMHGTVAAVAALQRSDLLIALGTRFDDRVTGKLDSFAPEAKVIHADIDPAEIGKNRHADVPIVGDVKAVITELIAMLRHHHIPGTIEMADWWAYLNGVRKTYPLSYGPQSDGSLSPEYVIEKLGEIAGPDAVFVAGVGQHQMWAAQFIRYEKPRSWLNSGGLGTMGFAIPAAMGAKIALPGTEVWAIDGDGCFQMTNQELATCAVEGIPVKVALINNGNLGMVRQWQSLFYAERYSQTDLATHSHRIPDFVKLAEALGCVGLRCEREEDVVDVINQARAINDCPVVIDFIVGADAQVWPMVAAGTSNDEIQAARGIRPLFDDITEGHA
Protein: Berberine bridge enzyme-like 27 (AtBBE-like 27) (EC 1.1.1.-) (Q9FI25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:18796151}.
Interaction partners:
- rhamnogalacturonan endolyase
- Cytochrome P450, family 705, subfamily A, polypeptide 32
- Acetyltransferase At1g77540
- BTB/POZ domain-containing protein At4g08455
- At1g12570
- Glycoside hydrolase family 28 protein / polygalacturonase
- Pectin lyase-like superfamily protein
- Monothiol glutaredoxin-S12, chloroplastic
- Peroxidase 43
- Peroxidase 36
Sequence:
MEILRFLLSLFIYFLLLNLSLSHFPSISAQRTNHENFLKCLSHRINEDDSRIIHTSKDPSYFSILNSSIQNPRFFVLETPKPVSIITPVQATDVQSTIKCARLHGIHIRTRSGGHDYEGLSYMAKSRPFVVIDLRNLRSITLDVDNRTGWVQSGATIGELYYEIGKLSKSLAFPAGLYPTVGIGGQFGGGGYGTLMRKYGLSADNVIDAHIVDANGSFLDRQGMGEDFFWAIRGGGGSSFSVVLSWKIRLLDVPSVVTVFKVVKTSEKEAVSIINKWQYIADKVPNDLFIRAMLQKETEVYASFPGLYLGPVSDLLALMKDKFPELGLEIGNCREMSWIESVLWFIKGESMEILAKRKRTSRSFKGKDDFIEEPIPKTAIQYLWRRFEAPEARLAKIILTPFGGKMSEIADNEIPFPHREGNLYEIQYLAYWSEEEDKNKTNTEKYLRWVESVYEFMTPYVSKSPRRAYVNFRDIDLGMYLGLNMKTKYEEAKVWGVKYFKNNFDRLVRVKTNVDPMDFFCDEQSIPIMKYVNDI
Protein: Serine protease (O01953)
Organism: Bombyx mori (Silk moth)
Interaction partners:
Sequence:
MKVFAAVLMALAAVVVAEEPIELDYHIKIGIPRAESLRRAEEAADFDGTRIVGGSAANAGAHPHLAGLVIALTNGRTSICGASLLTNTRSVTAAHCWRTRRAQARQFTLALGTANIFSGGTRVTTSNVQMHGSYNMDTLHNDVAIINHNHVGFTNNIQRINLASGSNNFAGTWAWAAGFGRTSDAASGANNQQKRQVSLQVITNAVCARTFGNNVIIASTLCVDGSNGRSTCSGDSGGPLTIGSGGSRQLIGITSFGSAQGCQRGHPAGFARVTSFNSWIRARI
Protein: Protocadherin-1 (Cadherin-like protein 1) (Protocadherin-42) (PC42) (Q08174)
Organism: Homo sapiens (Human)
Function: May be involved in cell-cell interaction processes and in cell adhesion.
Subcellular location: Cell junction. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries.
Interaction partners:
Sequence:
MDSGAGGRRCPEAALLILGPPRMEHLRHSPGPGGQRLLLPSMLLALLLLLAPSPGHATRVVYKVPEEQPPNTLIGSLAADYGFPDVGHLYKLEVGAPYLRVDGKTGDIFTTETSIDREGLRECQNQLPGDPCILEFEVSITDLVQNGSPRLLEGQIEVQDINDNTPNFASPVITLAIPENTNIGSLFPIPLASDRDAGPNGVASYELQAGPEAQELFGLQVAEDQEEKQPQLIVMGNLDRERWDSYDLTIKVQDGGSPPRASSALLRVTVLDTNDNAPKFERPSYEAELSENSPIGHSVIQVKANDSDQGANAEIEYTFHQAPEVVRRLLRLDRNTGLITVQGPVDREDLSTLRFSVLAKDRGTNPKSARAQVVVTVKDMNDNAPTIEIRGIGLVTHQDGMANISEDVAEETAVALVQVSDRDEGENAAVTCVVAGDVPFQLRQASETGSDSKKKYFLQTTTPLDYEKVKDYTIEIVAVDSGNPPLSSTNSLKVQVVDVNDNAPVFTQSVTEVAFPENNKPGEVIAEITASDADSGSNAELVYSLEPEPAAKGLFTISPETGEIQVKTSLDREQRESYELKVVAADRGSPSLQGTATVLVNVLDCNDNDPKFMLSGYNFSVMENMPALSPVGMVTVIDGDKGENAQVQLSVEQDNGDFVIQNGTGTILSSLSFDREQQSTYTFQLKAVDGGVPPRSAYVGVTINVLDENDNAPYITAPSNTSHKLLTPQTRLGETVSQVAAEDFDSGVNAELIYSIAGGNPYGLFQIGSHSGAITLEKEIERRHHGLHRLVVKVSDRGKPPRYGTALVHLYVNETLANRTLLETLLGHSLDTPLDIDIAGDPEYERSKQRGNILFGVVAGVVAVALLIALAVLVRYCRQREAKSGYQAGKKETKDLYAPKPSGKASKGNKSKGKKSKSPKPVKPVEDEDEAGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQVGQPFQLSTPQPLPHPYHGAIWTEVWE
Protein: Minor capsid protein VP1 (EC 3.1.1.4) (Coat protein VP1) (Q9PZT0)
Organism: Human parvovirus B19 (strain HV) (HPV B19)
Function: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.
Subcellular location: [Isoform Minor capsid protein VP1]: Virion {ECO:0000269|PubMed:1376332, ECO:0000269|PubMed:7544049}. Host nucleus {ECO:0000269|PubMed:12620794}. Host cytoplasm.; SUBCELLULAR LOCATION: [Isoform Major capsid protein VP2]: Virion {ECO:0000269|PubMed:15289612}. Host nucleus {ECO:0000269|PubMed:12620794}. Host cytoplasm.
Interaction partners:
Sequence:
MSKESGKWWESDDKFAKAVYQQFVEFYEKVTGTDLELIQILKDHYNISLDNPLENPSSLFDLVARIKNNLKNSPDLYSHHFQSHGQLSDHPHALSSSSSHAEPRGENAVLSSEDLHKPGQVSVQLPGTNYVGPGNELQAGPPQSAVDSAARIHDFRYSQLAKLGINPYTHWTVADEELLKNIKNETGFQAQVVKDYFTLKGAAAPVAHFQGSLPEVPAYNASEKYPSMTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLSMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVPGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL
Protein: Uncharacterized aminotransferase C6B12.04c (EC 2.6.1.-) (O14209)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein arg11
- Ornithine decarboxylase
- Homoserine dehydrogenase
- Aspartokinase
- Threonine synthase
- S-adenosylmethionine synthase
- Arginine biosynthesis bifunctional protein ArgJ
- Acireductone dioxygenase-requiring))
- Probable prephenate dehydrogenase [NADP
- Cell wall integrity and stress response component 1
Sequence:
MAFRGIRPSNKVAASRPDVWTLVNQATAECKVPPVSLSQGFFNYNPPKFVLDAAKKSIDEVACNQYSHTRGRPSLRKALSEAYSPYFKRTLNPDTEIVVTAGANEGFFSVFAAFLNPGDEVIVMEPFFDQYISNITMNGGVPVYVPIIPPEEGSVKPVSAGAWKLDMNKLRNAITEKTKMIVINTPHNPLGKIFSEEELNEIADLVLKHNLLVVSDEVYDRLSFVPFVRLATLRPELFKHVVTVGSGGKTFGCTGWRVGWLIGDESLIKYSAAAHTRICFAVNSPCQEALAIAFGEAEKHNYYEEYKSSYKKRFEILAKAFDQLEIPYTIPDGSYYTMANFSKLKLPKDYPFPEEIANRPRDFKLCYWILKEIGVATIPPTEFYTDEDAPVAENYLRFAFCKTFETLEEAARRLQKLKDYF