wanglab/gogpt-training-data huggingface dataset:
Protein: Origin recognition complex subunit 1 (Q80Z32)
Organism: Rattus norvegicus (Rat)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Origin recognition complex subunit 2
- DNA replication factor Cdt1
- Cell division control protein
- Origin recognition complex subunit 3
- Origin recognition complex subunit 4
- DNA replication licensing factor MCM4
- Origin recognition complex subunit 5
- DNA replication licensing factor MCM2
- Origin recognition complex subunit 6
- DNA replication licensing factor MCM3
Sequence:
MPSYVTRQKTRQTFSWVGRPLPNRKQFYQMYKEICMKINGCSEIHIKVGQFVLIQGEDNQKPYVAKLIELFENGSEVPPKKYARVQWFVRFCEIPIPKRHLLGRRPSAQEIFWYDCSDCDNDIHVETIIGPVQVVALAPEDEIPVNQKSEETLFVKLSWNKKNFAPLPPEELAALRRLECQKPLEAKTKSVKSPSWSTAEQEVKRIESSHSTSRSYQDPAHTVTPNAMKSLECGGFTRKPNMRLSRKILCDSLDSQKTCKRRAAFSETTSPPKKPQPGEIKTSSALETLGKNGHTQPFFAKSSMVLRTRGTAVKTTKLTVESALSPVRSRSRYSVAPSVGLTPQYIGRKAKEQETHKEPIHTSLRARRRSSLLTLKRIKQQLWLLDDDKSDQEEEESISSVEVSDSSSEEEDESVPSPPTGKPVGQSRTRRTASKPSSQTPSKSPKKTFRPRPPLHATPQIRDRNLAVQEPASVLEEARLRLHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVPPFEYVEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLAKQFCSRGSQKETTVLLVDELDLLWTHKQDVLYNLFDWPTHKGARLVVLTIANTMDLPERIMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHLKAFEDDAVQLVARKVAALSGDARRCLDICRRATEICEVSHQRGDSQCLVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPSRNDLLLRVRLNVSQNDVLYALKEE
Protein: Bicyclomycin resistance protein (Sulfonamide resistance protein) (P28246)
Organism: Escherichia coli (strain K12)
Function: Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance. Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth. Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Ribosomal small subunit pseudouridine synthase A
Sequence:
MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFALGQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVINALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAMIFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVYIEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISALLGLGFWSLVVGVAAFVGCVSMVSSNAMAVILDEFPHMAGTASSLAGTFRFGIGAIVGALLSLATFNSAWPMIWSIAFCATSSILFCLYASRPKKR
Protein: Insulin [Cleaved into: Insulin B chain; Insulin A chain] (P01315)
Organism: Sus scrofa (Pig)
Function: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular location: Secreted.
Interaction partners:
- Tyrosine-protein kinase receptor
- Tyrosine-protein kinase receptor
- Insulin-like growth factor 1
- Pro-epidermal growth factor
- Insulin receptor substrate 1
- Albumin
- Insulin-degrading enzyme
- Insulin receptor substrate 2
- Tyrosine-protein kinase receptor
- Receptor protein-tyrosine kinase
Sequence:
MALWTRLLPLLALLALWAPAPAQAFVNQHLCGSHLVEALYLVCGERGFFYTPKARREAENPQAGAVELGGGLGGLQALALEGPPQKRGIVEQCCTSICSLYQLENYCN
Protein: KATNB1-like protein 1 (Katanin p80 subunit B-like 1) (Q9H079)
Organism: Homo sapiens (Human)
Function: Regulates microtubule-severing activity of KATNAL1 in a concentration-dependent manner in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26929214}. Note=Localizes to the spindle poles only during mitosis. Sequestered to the nucleus during interphase. {ECO:0000269|PubMed:26929214}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A1
- Katanin p80 WD40 repeat-containing subunit B1
- Katanin p60 ATPase-containing subunit A-like 1
Sequence:
MASETHNVKKRNFCNKIEDHFIDLPRKKISNFTNKNMKEVKKSPKQLAAYINRTVGQTVKSPDKLRKVIYRRKKVHHPFPNPCYRKKQSPGSGGCDMANKENELACAGHLPEKLHHDSRTYLVNSSDSGSSQTESPSSKYSGFFSEVSQDHETMAQVLFSRNMRLNVALTFWRKRSISELVAYLLRIEDLGVVVDCLPVLTNCLQEEKQYISLGCCVDLLPLVKSLLKSKFEEYVIVGLNWLQAVIKRWWSELSSKTEIINDGNIQILKQQLSGLWEQENHLTLVPGYTGNIAKDVDAYLLQLH
Protein: Elongation factor 1-alpha-A (EF-1-alpha-A) (P0CT53)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Elongation factor 1-gamma
- Elongation factor 1-beta
- GTP-binding nuclear protein spi1
- Elongation factor 1-alpha-B
- Elongation factor 3
- Adenylyl-sulfate kinase
- Elongation factor 1-alpha-B/C
- Eukaryotic peptide chain release factor subunit 1
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
Sequence:
MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAVLIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK
Protein: BIIDXI-like protein At5g11420 (Q9LYE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:Q94F20}.
Interaction partners:
- Proline-tRNA ligase
- Nucleotide binding protein
- 11-beta-hydroxysteroid dehydrogenase-like 2
- Protein RALF-like 22
- rRNA biogenesis protein RRP36
- Large ribosomal subunit protein P3z
- Classical AGP protein
- Protein BRI1-5 ENHANCED 1
- At1g19540
- Putative beta-glucosidase 41
Sequence:
MKGGSLSFLFVLLIATITSVICFSDGMLPNGDFELGPKPSDMKGTQVINKKAIPSWELSGFVEYIKSGQKQGDMLLVVPAGKFAIRLGNEASIKQRLNVTKGMYYSLTFSAARTCAQDERLNISVAPDSGVIPIQTVYSSSGWDLYAWAFQAESNVAEIVIHNPGEEEDPACGPLIDGVAIKALYPPRPTNKNILKNGGFEEGPYVLPNATTGVLVPPFIEDDHSPLPAWMVESLKAIKYVDVEHFSVPQGRRAVELVAGKESAIAQVARTVVGKTYVLSFAVGDANNACQGSMVVEAFAGKDTLKVPYESRGKGGFKRASLRFVAVSTRTRVMFYSTFYSMRSDDFSSLCGPVIDDVKLLSARKP
Protein: Small ribosomal subunit protein RACK1 (D6RFX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDI
Protein: F-box only protein 22 (F-box protein FBX22p44) (Q8NEZ5)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933}. Nucleus {ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Amino acid depletion lead to a time-dependent increase of FBXO22 in the cytoplasm. {ECO:0000269|PubMed:37979583}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- NF-kappa-B inhibitor alpha
- E3 ubiquitin-protein ligase RBX1
- Transcription regulator protein BACH1
- Lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
Sequence:
MEPVGCCGECRGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVLRTHRSVTWISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGHKRARKRTSMETALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQPFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVVSTFSDMNIILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEKTAEAAMQRLKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRIVTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK
Protein: WD repeat-containing protein 55 (Protein WD repeat domain 55) (Protein WDR55 homolog) (O80775)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for male and female gametogenesis, seed development, and embryo and endosperm development at early stages. Involved in the establishment of bilateral symmetry in the transition from the globular to the heart embryo stage. May act in the frame of a CRL4 complex. Required for proper vegetative growth and organization of the adult plant body. May play a role in hormonal control of plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:22447688}. Cytoplasm {ECO:0000269|PubMed:22447688}.
Interaction partners:
- Ribosome biogenesis protein WDR12 homolog
- DNA damage-binding protein 1a
- tRNA
- THO complex subunit 6
- Suppressor of mec-8 and unc-52 protein homolog 2
- Protein ROOT INITIATION DEFECTIVE 3
- Protein ALTERED SEED GERMINATION 2
- BRISC and BRCA1-A complex member 1
- Uncharacterized protein At1g27050
- RNA-binding
Sequence:
MEIDLGANAFGIDFHPSTNLVAAGLIDGHLHLYRYDSDSSLVRERKVRAHKESCRAVRFIDDGQRIVTASADCSILATDVETGAQVAHLENAHEDAVNTLINVTETTIASGDDKGCVKIWDTRQRSCSHEFNAHEDYISGMTFASDSMKLVVTSGDGTLSVCNLRTSKVQSQSEFSEDELLSVVIMKNGRKVICGTQNGTLLLYSWGFFKDCSDRFVDLAPNSVDALLKLDEDRLITGCDNGIISLVGILPNRIIQPIGSHDYPIEDLALSHDKKFLGSTAHDSMLKLWNLEEILEGSNVNSGNASGAAEDSDSDNDGMDLDNDPSKSSKGSKRKTKSKANTLNATNNFFADL
Protein: A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 149 kDa) (AKAP 149) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84) (Q92667)
Organism: Homo sapiens (Human)
Function: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity. Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O08715}. Mitochondrion {ECO:0000250|UniProtKB:O08715}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase type II-beta regulatory subunit
- 3',5'-cyclic-AMP phosphodiesterase 4A
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Rap guanine nucleotide exchange factor 3
- c-Myc-binding protein
- A-kinase anchor protein 5
- A-kinase anchor protein 6
Sequence:
MAIQFRSLFPLALPGMLALLGWWWFFSRKKGHVSSHDEQQVEAGAVQLRADPAIKEPLPVEDVCPKVVSTPPSVTEPPEKELSTVSKLPAEPPALLQTHPPCRRSESSGILPNTTDMRLRPGTRRDDSTKLELALTGGEAKSIPLECPLSSPKGVLFSSKSAEVCKQDSPFSRVPRKVQPGYPVVPAEKRSSGERARETGGAEGTGDAVLGEKVLEEALLSREHVLELENSKGPSLASLEGEEDKGKSSSSQVVGPVQEEEYVAEKLPSRFIESAHTELAKDDAAPAPPVADAKAQDRGVEGELGNEESLDRNEEGLDRNEEGLDRNEESLDRNEEGLDRNEEIKRAAFQIISQVISEATEQVLATTVGKVAGRVCQASQLQGQKEESCVPVHQKTVLGPDTAEPATAEAAVAPPDAGLPLPGLPAEGSPPPKTYVSCLKSLLSSPTKDSKPNISAHHISLASCLALTTPSEELPDRAGILVEDATCVTCMSDSSQSVPLVASPGHCSDSFSTSGLEDSCTETSSSPRDKAITPPLPESTVPFSNGVLKGELSDLGAEDGWTMDAEADHSGGSDRNSMDSVDSCCSLKKTESFQNAQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDDQFSPEADAAMSEMTGNTALLAQVTSYSPTGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYTSL
Protein: vacuole-related protein 17 (Vacuole-specific MYO2 receptor VAC17) (P25591)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuole-specific MYO2 receptor required for vacuole inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar membrane protein, forming a transport complex which moves the attached vacuole membrane along actin cables into the bud. Once the vacuole arrives in the bud, VAC17 is degraded, depositing the vacuole in its correct location.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12594460}; Peripheral membrane protein {ECO:0000269|PubMed:12594460}; Cytoplasmic side {ECO:0000269|PubMed:12594460}.
Interaction partners:
- Vacuolar protein 8
- Myosin-2
- Inheritance of peroxisomes protein 2
- GTP-binding protein YPT11
- GTP-binding protein YPT32/YPT11
- Protein BIM1
- Mitochondrial MYO2 receptor-related protein 1
- Autophagy-related protein 18
- Karyogamy protein KAR9
- Rab guanine nucleotide exchange factor SEC2
Sequence:
MATQALEDITERLLIRSQEAILQLDLWIQRQQRSSICQTTDQESLDKLSQQYNQYMSQLNSLYVRSESVRDKLSKEQQRRLITEDNEHQRIEDLVREFQDITLRLNELATVPNEAPNDSPQSQSTRSSLGSFQPRPLKIIERQRLCMVTPSKPPKKSVGFNPINEVDCPSKTNSLPCSPKKQPARNRTLRAAKSHDTGLNKSKKPSSSDTYESFFKNRQRLSLTFFDEMDDEDFDSDQDTIILPNISTPPHVGVTAKGAEFEPLRRYNSHESILSNKPAPSKSLNLGSFSASFFRPSNPTFGTSISNVQVNCHPTVAATMAPSRNGPRISSSKALLSSFIARSDTHTVKENNTNLKHASFMDKFNSSLSTISESFQSKRGRKNKGMNEERISNHNVAQEQKNNMDISVSIEELQDALNTELLF
Protein: PDGF- and VEGF-receptor related, isoform H (EC 2.7.10.1) (E1JHB8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIGNGHIDKDGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSLPSEQEKYQFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAVYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRIEELPDDYMEMSRDSDPDACTAIFSPTRLEGESSDFPDFSSETTFNFPGARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: GMP phosphodiesterase delta subunit domain-containing protein (G5EGP9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTGGNEQRAGTAKGRRGAQDSTTAYMKAEQQQQSIAPGSATFPSQMPRPPPVTEQAITTEAELLAKNQITPNDVLALPGITQGFLCSPSANVYNIEFTKFQIRDLDTEHVLFEIAKPENETEENLQAQAESARYVRYRFAPNFLKLKTVGATVEFKVGDVPITHFRMIERHFFKDRLLKCFDFEFGFCMPNSRNNCEHIYEFPQLSQQLMDDMINNPNETRSDSFYFVENKLVMHNKADYSYDA
Protein: Dye-decolorizing peroxidase (EglDyP) (EC 1.11.1.19) (EC 1.11.1.7) (I2DBY2)
Organism: Exidia glandulosa (Black witch's butter)
Function: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.
Subcellular location: Secreted {ECO:0000305|PubMed:23111597}.
Interaction partners:
Sequence:
MRLSPSFLSLALVIFVGEVVARNVVARASNPASVTGTRKVSLLKNVAGLPAVPTAQQVAVSSLNTDDIQGDILVGMHKQQQRFYFFTINDAATFKTHLAADIAPVVASVTQLSSVSTQPLVALNIAFSQTGLNALGVTDNVGDALFTAGQASNTVGNLKETTDNWVAQFKTPGIHGVILLASDDKSLIDQQEASIQSTFGAAISKVYSLDGAIRPGAEAGHEMFGFLDGIAQPAISGLGTPLPGQLVVDEGVIIVGGTNDPIARPADGWMTGGSFLAFRQLEQLVPEFNKYLLDNAPAVDGKSLQDRADLLGARMVGRWKSGAPIDLTPLADDPALGADPQRNNNFDFTHANFSITTDQTHCPFSAHIRKTRPRADLVAPANSIIRSGIPYGSEVSAAEAAANATTNERGLAFVSYQSQLNKGFQFLQNTWANNPGFIFGKNVQPGQDPIIGQNSGAIRSVVGLDPANPTGALSMGQFVVSRGGEYFFSPPISALTGKLAA
Protein: Opioid-binding protein/cell adhesion molecule precursor (Zgc:92901) (Q642G9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MGITGYFELQWKCLVVVALRLLFLVPAGVPARSGDSYLKDNITVRQGDSAVLKCSMDNKVSRVAWLNRTTILFTGNEKWSLDPRVVLLNTAVNEYSIKILNVNLYDEGPYVCSILTNKKPESTKVHLIVQVPARIVNVSTDVSVNEGSNVSLMCLAIGRPEPSILWKFRSSKGNRIVTEGEYVEMTGITKDMSGSYDCITSNDISPPDVRTVQVTVNYPPVISRARSTGTAVGQKGVLWCEASAVPLADFQWFKGERRILNGFNGVKIENKGKQSMLTFFNVSEEDYGNYTCVAINTLGITNASIILYGPGAIHDVNNAALSPTCSLLLLTLLLTLSLLSKF
Protein: Gamma-aminobutyric acid receptor subunit gamma-1 (GABA(A) receptor subunit gamma-1) (GABAAR subunit gamma-1) (P23574)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit beta-1
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor-associated protein-like 1
- Gamma-aminobutyric acid receptor subunit alpha-2
- Gamma-aminobutyric acid receptor subunit beta-3
Sequence:
MGSGKVFLFSPSLLWSQTRGVRLIFLLLTLHLGNCIDKADDEDDEDLTMNKTWVLAPKIHEGDITQILNSLLQGYDNKLRPDIGVRPTVIETDVYVNSIGPVDPINMEYTIDIIFAQTWFDSRLKFNSTMKVLMLNSNMVGKIWIPDTFFRNSRKSDAHWITTPNRLLRIWSDGRVLYTLRLTINAECYLQLHNFPMDEHSCPLEFSSYGYPKNEIEYKWKKPSVEVADPKYWRLYQFAFVGLRNSTEISHTISGDYIIMTIFFDLSRRMGYFTIQTYIPCILTVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFAALMEYGTLHYFTSNNKGKTTRDRKLKSKTSVSPGLHAGSTLIPMNNISMPQGEDDYGYQCLEGKDCATFFCCFEDCRTGSWREGRIHIRIAKIDSYSRIFFPTAFALFNLVYWVGYLYL
Protein: Platelet glycoprotein VI (GPVI) (Glycoprotein 6) (Q9HCN6)
Organism: Homo sapiens (Human)
Function: Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane protein.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein kinase Lyn
- von Willebrand factor
- Tyrosine-protein kinase Fyn
- Integrin alpha-2
- Galectin-3
- Platelet glycoprotein V
- Protein S100-A10
- Collagen alpha-2
- Platelet glycoprotein Ib alpha chain
Sequence:
MSPSPTALFCLGLCLGRVPAQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPPLPPLPLTRKSNGGQDGGRQDVHSRGLCS
Protein: Uncharacterized protein (G5EB42)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPLSLCSALHTVTPFYHFGLQSQSLDHPSHRSASSARVYYL
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (Q27597)
Organism: Drosophila melanogaster (Fruit fly)
Function: This enzyme is required for electron transfer from NADP to cytochrome p450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome b5 (By similarity). May function to clear the olfactory organ (antennae) from accumulating chemicals.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Cytochrome P450 6a2
- Cytochrome P450 6a8
- Probable cytochrome P450 4d14
- Cytochrome P450 4d2
- Probable cytochrome P450 9f2
- Probable cytochrome P450 4s3
- Cytochrome P450 4c3
- Probable cytochrome P450 6a18
- Probable cytochrome P450 4d20
- PAPS synthetase, isoform D
Sequence:
MASEQTIDGAAAIPSGGGDEPFLGLLDVALLAVLIGGAAFYFLRSRKKEEEPTRSYSIQPTTVCTTSASDNSFIKKLKASGRSLVVFYGSQTGTGEEFAGRLAKEGIRYRLKGMVADPEECDMEELLQLKDIDNSLAVFCLATYGEGDPTDNAMEFYEWITSGDVDLSGLNYAVFGLGNKTYEHYNKVAIYVDKRLEELGANRVFELGLGDDDANIEDDFITWKDRFWPAVCDHFGIEGGGEEVLIRQYRLLEQPDVQPDRIYTGEIARLHSIQNQRPPFDAKNPFLAPIKVNRELHKGGGRSCMHIELSIEGSKMRYDAGDHVAMFPVNDKSLVEKLGQLCNADLDTVFSLINTDTDSSKKHPFPCPTTYRTALTHYLEITAIPRTHILKELAEYCTDEKEKELLRSMASISPEGKEKYQSWIQDACRNIVHILEDIKSCRPPIDHVCELLPRLQPRYYSISSSAKLHPTDVHVTAVLVEYKTPTGRINKGVATTYLKNKQPQGSEEVKVPVFIRKSQFRLPTKPETPIIMVGPGTGLAPFRGFIQERQFLRDEGKTVGESILYFGCRKRSEDYIYESELEEWVKKGTLNLKAAFSRDQGKKVYVQHLLEQDADLIWNVIGENKGHFYICGDAKNMAVDVRNILVKILSTKGNMSEADAVQYIKKMEAQKRYSADVWS
Protein: Paternally-expressed gene 3 protein (ASF-1) (Q3URU2)
Organism: Mus musculus (Mouse)
Function: Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B. Plays a role in regulating maternal behavior and offspring growth.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
Sequence:
MYHHEDDTNSDMNSDDDMSRSGRETPPPRPSHAFGSERDLERRGRSRDVEPRDRWPYTRNPRSRLPQRDLSLPVMSRPHFGLDRDDDRRSMDYESRSQDAESYQNVVELKEDKKPQNPIQDNLENYRKLLSLGVQLAEDDRHSHMTQGHSSRSKRTAYPSTSRGLKPMPEAKKPSHRRGICEDESSHGVIMEKFIKDVARNPKSGRARELNERPPPRFPRPNDNWKDSSSSRRESVIQERGYEGSAFRGGFRFNADLASRSRALERKRRYHFDSDERGSGHEHKSCVRKKPFECGAEMRQAMSMGNLNSPSFSESQSIDFGANPYVCDECGRQFSVISEFVEHQIMHTRENLYEYGESFIHSVAVNEVQKGQGGGKRFECKECGETFSRSAALAEHRQIHAREYLAECRDQEDEETIMPSPTFSELQKMYGKDKFYECKVCKETFLHSSALIEHQKIHGRGNSDDRDNERERERDRLRARAREQRERERERERERELGEPFLTCPNFNEFRKMYRKDKIYECKVCGESFLHLSSLREHQKIHTRGNPFENKSRMCEETFVPSQSLRRRQKTYREKLFDFNNARDALMGNSDSSEHQKNRSRRNFFEGRGFEKPFVESQKSHTITRPPENKDDDKPFTISVNPNDKLKFPIMENGSQGKSYERSVIHSLGSAEAQKSHGGLGFSKPRPVAESSTQSSSSIYYPRAHSGGNTYEGKEYKDSIIHSLPAPRPLKRHRANDHIQCDEGGESSIYIPDIINKGRKIPAREDAYEGSSSSNYHTPNVSRAEPPSLSGESHDSKQDVTFSVPSSSVREHQKARAKKKYIEPRNNETSVIHSLPFGELLAGHRRAKFFECQECGEAFARRSELIEHQKIHDRERPSGSRHYERSVIRSLAPSDPQTSYAQERFIQEQVRKFRAFGQRSTTSNNLSVQKIYAQETFNAEEPHDKETHGQKIHDKEPYGKEPSGKEPHGDEPQDKEPLDQEMRSEEPHDDKPHGQEPHDDKPHGQEPHDDKPHGQEPHGDEPHGQEPHGDEPHDKEPIDQEMRSEEPHSEESHGDEPHGEESHGQEKVEDATIQASVSEEHQKDDAGDAIYECQDCGLGFTDLNDLTSHQDTHSRKALVDSREYAHSEVHAHSVSEFEKKCSGEKLYECPKCGESFIHSSLLFEHQRVHEQDQLYSVKACDDAFIALLPVRPRRNCTVERNPAVSGSAIRCRQCGQGFIHSSALNEHMRQHRDNEIMEQSELSDEIFIQGLALTEYQGSETEEKLFECTICGECFFTAKQLGDHHTKVHKDEPYEYGPSYTHASFLTEPLRKHIPLYECKDCGQSFLDDTVIAERMVFHPEREGGSEIVAATAQEVEANVLIPQEVLRIQGSNAEAAEPEVEAAEPEVEAAEPEVEAAEPNGEAEGPDGEAAEPDGEAEQPNGEAEQPNGDADEPDGAGIEDPEERADEPEEDVEEPEGDADEPDGADIEDPEEEGEDQEIEVEEPYYNCHECAETFASSSAFGEHLKSHASVIIFEPANAPGECSGYIERASTSAGGAEQADDKYFKCDVCGQLFNDRLSLARHQNSHTG