wanglab/gogpt-training-data huggingface dataset:
Protein: Collagen alpha-4(VI) chain (A2AX52)
Organism: Mus musculus (Mouse)
Function: Collagen VI acts as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Platelet glycoprotein VI
- CD44 antigen
- Integrin beta-4
- Integrin alpha-9
Sequence:
MGTWKTFWLIISLAAGLGFVKSQRIVCREASVGDIVFLVHNSINPQHAHSVRNFLYILANSLQVGRDNIRVGLAQYSDTPTSEFLLSVYHRKGDVLKHIRGLQFKPGGNRMGQALQFILEHHFREGAGSRASQGVPQVAVVVSSGLTEDHIREPAEALRRAGILVYAIGVKDASQAELREISSSPKDNFTFFVPNFPGLPGLAQKLRPELCSTLGKAAQYTERESPACSEASPADIVFLVDSSTSIGLQNFQKVKHFLHSVVSGLDVRSDQVQVGLVQYSDNIYPAFPLKQSSLKSAVLDRIRNLPYSMGGTSTGSALEFIRANSLTEMSGSRAKDGVPQIVVLVTDGESSDEVQDVADQLKRDGVFVFVVGINIQDVQELQKIANEPFEEFLFTTENFSILQALSGTLLQALCSTVERQMKKSTKTYADVVFLIDTSQGTSQASFQWMQNFISRIIGILEVGQDKYQIGLAQYSDQGHTEFLFNTHKTRNEMVAHIHELLVFQGGSRKTGQGLRFLHRTFFQEAAGSRLLQGVPQYVVVITSGKSEDEVGEVAQILRKRGVDIVSVGLQDFDRAELEGIGPVVLVSDLQGEDRIRQLMLDVNMFIQGSPKPPRVMTDVAKDAVEECLVPVPADLVFLVEDFSSARQPNFQRVVHFLTTTVHSLNIHPDTTRVSLVFYSEKPRLEFSLDMYQSAAQVLRHLDRLTFRARRGRAKAGAALDFLRKEVFLPEKGSRPHRGVQQIAVVIIESPSLDNVSTPASYLRRAGVTIYAAGTQPASESKDLEKIVTYPPWKHAIRLESFLQLSVVGNKLKKKLCPEMLSGMPPLMSFIPESTRQSTQEGCESVEKADIYFLIDGSGSIKPNDFIEMKDFMKEVIKMFHIGPDRVRFGVVQYSDKIISQFFLTQYASMAGLSAAIDNIQQVGGGTTTGKALSKMVPVFQNTARIDVARYLIVITDGQSTDPVAEAAQGLRDIGVNIYAIGVRDANTTELEEIASKKMFFIYEFDSLKSIHQEVIRDICSSENCKSQKADIIFLIDGSESIAPKDFEKMKDFMERMVNQSNIGADEIQIGLLQFSSNPQEEFRLNRYSSKVDMCRAILSVQQMSDGTHTGKALNFTLPFFDSSRGGRPRVHQYLIVITDGVSQDNVAPPAKALRDRNIIIFAIGVGNVQRAQLLEITNDQDKVFQEENFESLQSLEKEILSEVCSSQGCNIDLSVGVDTSTSSERAQQELRRLLPELMQQLAFLSNISCEAPGQMEPRFRYVVPGSSDQPVFDSGFEKYSDETIQKFLVHQGSVNNRMDVDFLQSLGETAIHLSLAKVKVLLVFTDGLDEDLERLRRTSEFLRSRGLSGLLLIGLGGAHKLEELQELEFGRGFAYRQPLSSSLPSLPSVLLKQLDTIVERTCCNMYAKCYGDDGIRGEPGSRGEQGERGLDGLPGHPGEEGDHGQRGPRGLPGLRGEEGCPGVRGPKGARGFSGEKGNPGEEGVGGLDGEQGDRGAAGPSGEKGSSGSRGLTGLPGPAGPRGEPGLRGDPGDPGIDNLIQGPKGEKGRRGHQGSPGFHGPLGEAGSVGPRGSLGRHGLPGLKGVLGETGELGSRGEPGHPGPQGPRGRQGPPGFFGQKGDPGTQGNPGLPGPSGSKGPDGPRGLKGEVGPAGERGPRGQQGPRGQPGLFGPDGHGYPGRKGRKGEPGFPGYPGVQGEDGNPGRGGEKGAKGIRGKRGNSGFPGLAGTPGDQGPPGKMGTKGSKGLADRTPCEIVDFVRGNCPCSTGISRCPAFPTEVVFTLDMSNDVAPSDFERMRNILLSLLMKLEMCESNCPTGARVAIVSYNTRTDYLVRLSDHRGKAALLQAVRKIPLERSSGSRNLGATMRFVARHVFKRVRSGLLVRKVAVFFQAGRNYDTASVSTATLELHAADIATAVVTFTEEHNLPEAGLVDGPNEFHLFTWETEGQQDVERLASCTLCYDKCRPALGCQLRAPGPQKLDMDLVFLVDSSQGVSRDIYLGALRLVDSVLKDLEVAAQPGTSWHGARAALLTHTTPGFWPGVDQAPVLEYFHLTSHGHRTEMQRQIREAASGLLQGGPALGHALEWTLENVLLTAVLPRRSRVLYAIVASETSIWDREKLRTLSQEAKCKGIALFVLAVGPGVGAQELAELAKVASAPWEQHLLRLEGVSEAEVAYASRFTEAFLNLLNSGINQYPPPELVKECGGPNRGDTLLHFFTSAKRFSRSQSGTSAAFANDSEALKSQGIFLGERKSRVASVALQEALGSHGKDRADTEDIDQETPAKGRHLGPTHGPCPMGPEEGECLNYVLK
Protein: Mitotic spindle checkpoint protein BUBR1 (BUB1-related protein 1) (O22806)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions may be to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C (By similarity).
Subcellular location: Chromosome {ECO:0000269|PubMed:19710914}. Cytoplasm {ECO:0000269|PubMed:19710914}. Nucleus {ECO:0000269|PubMed:19710914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:O60566}. Note=Cytoplasmic in interphase cells. Accumulates onto both kinetochores and the spindle microtubules in cell arrested in metaphase. Associates with unattached kinetochores in early prophase upon spindle assembly checkpoint (SAC) activation. Present in chromocenters.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Mitotic checkpoint protein BUB3.1
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 8
- Kinetochore protein NDC80 homolog
- Anaphase-promoting complex subunit 5
- Serine/threonine-protein kinase MPS1
- Anaphase-promoting complex subunit 1
- Mitotic spindle checkpoint protein MAD1
Sequence:
MAAETKVQVSDPEAEFLNSKQETGYEWELFKENVRPLKRGRNVGILNHALKSHSDHQLRKNLIEKRRNLIEAIDEYEGDDPLSPWIECIKWVQEAFPPGGECSGLLVIYEQCVRKFWHSERYKDDLRYLKVWLEYAEHCADAEVIYKFLEVNEIGKTHAVYYIAYALHIEFKNKVKTANEIFNLGISRDAKPVEKLNDAYKKFMVRTMRRSNTADEEPKENNDLPSRSFGTLLSRGDNNARRQALGSSNPQAKKLKPNQSSKTPFAIYADAVSDTTSGNQPESDKSRPEFGSWLMLGGRAERNKENNSLPRKWASFKVPQKPIVRTVAAASASTFEVFVDEEECTEEEEEKKKNDETISSSSNVLPLNGGREIKKETELLRQNPLRHFPPNSFLR
Protein: O-glycoside alpha-1,2-mannosyltransferase homolog 6 (EC 2.4.1.-) (Q9P4X2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- O-glycoside alpha-1,2-mannosyltransferase omh1
- O-glycoside alpha-1,2-mannosyltransferase homolog 2
- ERAD-associated E3 ubiquitin-protein ligase hrd1
Sequence:
MYFLILFSSNAELGEVLRTMRSVEDRFNKRFHYPWTFYGMDEFTEYFMSTTSTIASGHCEYGTKGITYTNHLQFILTISYLVHWDLSQVKPLVENNRLYQQRADALAQENLSYVYSPLFHSFQDWVVRSLLYHPQLEYDYVWRIEPGLKLVCEEKKDIFSTFKDSDIVFTNHVCERKHSGIYAMEEAIEEYKILNTQGDFSNIWVYSNNYTYCKYWPFNEILSLKQIRHNQTYTNLINYLLGSGGTYYHRWTESDILSAAFGVLRARANHMESVGFFLNDDVHYCPETIPYTGRCACL
Protein: DNA-binding protein (Hairy-related 5) (Q90467)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEQKDMRRVPKPLMEKRRRDRINQSLETLRMLLLENTNNEKLKNPKVEKAEILESVVHFLRAEQASETDPFQITRVKRARTEESDEDVESPCKRQSYHDGMRTCLLRVSNFITGKSHEFGQELEKACENIHKSHSRQVQLLSTPSLIEPQVHLYEDPSQQHLAHVQLSNSCTPSGCSKLAQRTVPAMTSSPKQPVMLCDPVWRPW
Protein: Oxidoreductase, putative (EC 1.6.5.5) (Q57TX8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Calcineurin-like phosphoesterase domain-containing protein
Sequence:
MSRLSSKAWLYTRCGPIAHVLKYETMEIVPKGNEVVVDVLQAPLHRVDAAVVNGSVLGRRRLQLPSFPRVGGSEGVGVVVANNGSSVIKEGDTVWVAPLNGLWATRVAVPCNSVHKIDSKYIPLAVNASNYITAHRLVNGFTSLRKGQVIVQNGGSSATSLAVAALGKLLGFRVLTASTPGERFDKAKQRHAEYGSEVFEYNGKGSRAMRQALGGSAAALYLNAIGGRHFDTFLGLLGKGGHAVSYGAQSGVGLMISGSNIIFNEVTMEGFLLPSYLASLSYEERQTQLEVVLQQLSSVGFKYPTVVAPSLEKMPDVWDECFVHGGTKGIVVVKK
Protein: 2-aminomuconic semialdehyde dehydrogenase (EC 1.2.1.32) (Aldehyde dehydrogenase family 8 member A1) (Q66I21)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the NAD-dependent oxidation of 2-aminomuconic semialdehyde of the kynurenine metabolic pathway in L-tryptophan degradation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
- Hydroxysteroid dehydrogenase-like protein 2
- Epoxide hydrolase 2
- Alcohol dehydrogenase iron-containing 1.
- Retinol dehydrogenase 10-B
- HBS1-like protein
- Delta-1-pyrroline-5-carboxylate synthase
- GRAM domain-containing 2Aa
Sequence:
MSKDMKYLVLENYIGGKFVPCSKLIDSFDPSTGEVYCKVPDSGAEEVNAAVRAAKEAFPDWSAKSPADRSKVLNKLADLIEARLEEFVQAESKDQGKTITFARNVDIPRSAYNFRFFASSVLHHTNDCSQMDHMGCLNYTIRCPVGVAGLISPWNLPLYLLTWKIAPAVATGNTVVAKPSEMTSVTAWMMCQLLEEAGFPPGVVNIVFGTGPRAGDALVSHPDVPLISFTGSTATARLITERSAPHCKKLSLELGGKNPAIIFADADMEQCISTTVRSSFSNQGEICLCTSRIFVERSVYPEFLTRFVEATRRWKTGVPSDPSNDNGALISKEHLQKVKGYITLALAEGAQVHCGEGVDKLALPQQNIGGYFMLPTIISGVKDSSALMQEEIFGPVTCVTPFDEEEEVISRANNVRYGLSATVWSRDVGRVHRVARKLQAGLVWTNCWLVRDLNLPFGGMKHSGIGREGGKDSYHFFTEVKSVTVKH
Protein: Protein SIEVE ELEMENT OCCLUSION B (AtSEOb) (Protein SIEVE ELEMENT OCCLUSION-RELATED 1) (AtSEOR1) (Q9SS87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Scaffold protein required to form the phloem filament matrix in sieve elements.
Interaction partners:
- Expressed protein
- Early nodulin-like protein 9
- Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 7
- Protein PHLOEM PROTEIN 2-LIKE A1
- Callose synthase 7
- Leucine-rich repeat receptor-like protein kinase TDR
- Cysteine protease XCP1
- CLAVATA3/ESR
- Protein OCTOPUS
- Protein SMAX1-LIKE 5
Sequence:
MESLIKSQHAQQLAGHKNTTGKTPSMEMIPATGLAMSSDESMMLKLIQQTHSPDAREVQVRGLLSLVEDILDRATLDSEDTNASMLPLPTEDKLMQSSMMSVLDSVSYAIDRVACEIAYKSLTGSDSHEITMSVFEHLSSFQWDGKLVLTLAAFALNYGEFWLLVQFYSKNQLAKSLAMLKLVPVQNRVTLESVSQGLNDLIREMKSVTACVVELSELPDRYITPDVPQLSRILSTIPIAVYWTIRSVIACISQINMITAMGHEMMNTQMDLWETSMLANKLKNIHDHLAETLRLCYRHIEKQRSSESLKVLHSLFDTTHIDNMKILTALVHPKPHITPLQDGLTKRKVHLDVLRRKTVLLLISDLNILQDELSIFEQIYTESRRNLVGVDGKSHMPYEVVWVPVVDPIEDFERSPILQKKFEDLRDPMPWYSVDSPKLIERHVVEFMRGRWHFMNKPILVVIDPQGNEASLNALHMIWIWGTEAFPFTRSREEELWRRETFSLNLIVDGIDSVIFNWIKPDNYIFLYGGDDLDWIRRFTMAAKATAKDSNVNLEMAYVGKRNHSHREQIRRISEVIRSENLSHSWAEPALMWFFWTRLESMLYSKIQLGKADDHDDVMQGIKKILSYDKLGGWALLSKGPEIVMIAHGAIERTMSVYDRTWKTHVPTKGYTKAMSDHHHDEVLRETGKPCGHFDFHITARSGRIPEKMNCFECQRPMEKYMSFSCCHDEKLHEDENYNF
Protein: RE02873p (Q8MT64)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRYAAETTQMDKDGPTDLERPGDWDSLSDRMRKLRRSQQQQQKEVALLADRKDALTKRPLDFDREEETRKGETMKWLESHFGSESTASNDSRDDEAGAEVEPTKKSYFNVTIKSQSHAQSHLATQQHSHPQHISHGHHPQTLPRSAERERERERERERERERERERERDRDRHPLAMTASASQERKAPANSAGGRSKYFQGISNWSERKDPGPPVNHFSSQAFRDDLQETIRRNGLKKKVSGPGSSQGSALAQETVVQPKDSYVSREDILQQKRQSLSSQFLARSMRGSRDALDDLEAIPGPGPGPSMISPRAEEPSHKRVAYGHRGNNGTHINGHALNGVAPTLVNGRGKSYEPPAPPPAAVPPLEFGGGGSQLGQNPRPTVPQRRRAIEKKLGEHSHTHSHSHSHSSHTSHSAHLPVKSQAPMPSQLNQLEPPPDYSPPPRSRSRSSSPQVDYLMTREMPASTMTLSRKQQQRTRFAPTSSYPPATGGTGNLRPPGATSVSTSNLSAMSGGVSTSKSSRMGQVIGNSLRKLVSKIRSASAERKFRMKSAASKSREQSPSPGQDPRGVGPPVTTYQQYNVIDGHIGSHDSEDSNSDNQRRRERERERERERERERERDPLKQESQSRQNFKRAESADPQLQHLEQAISPRQRYYLGEDPYSSTLYGKENHYERRPRQRNMERTDERMERLERLEREDDYYESRAPPPVTAAHTLGRYQKHGQRFSGSTPNLHQQQQDYRSAQTLPRKLHEQRTQRFGNAMEKQPAPGRGSYLSASGQQQQSRGIPHNQNQQNQQNPNPSPSINGNPNPMQAQQGPAKPARTYAKVLNRSKSFNVHGMNGSNDPSPIYIEKLTRNNYQQRQEPSFGYGLGQGPNANYKSNPHLFSGKDNSLKSGLKSPSIVNLISRSQKDLTKIAGNDEDDVGYPEQDKKQLYLRGLHQQAPDLYRVIHGDEDYGSRKYPLQAKYSLDSRSPPSVELNKDTASIVRRSSEVDHQQSHHHNQQHHQHHIQSHQQQNLRRGSGATIIELRHRK
Protein: Matrix protein (D7F443)
Organism: Avian paramyxovirus 1 (NDV) (Avian orthoavulavirus 1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MDSSRTIRLYFDSALPSSSLLAFPIVLQGTGDGKKRITPQYRIQRLDLWTDSKEDSVFITTYGFIFQIGNEEVTVGTISDNPRHELLSSAMLCLGSVPNDGDLVELARACLTMVITCKKSATNTERIVFSIVQAPRVLQSCMVVANKYSSVNAVKHVKAPEKIPGSGTLEYKVNFVSLTVVPRKDVYRIPTAALKISGSSLYNLALNVTIDVEVDPKSPLVKSLSKSDSGYYANLFLHIGLMPTVDKKGKKVTFDKIEEKIRRLNLSVGLSDVLGPSVLVKARGARTKLLAPFFSSSGTACYPIANASPQVAKILWSQTAHLRSVKVIIQAGTQRAVAVTADHEVTSTKIEKRHTIAKYNPFKK
Protein: Large ribosomal subunit protein eL18A (60S ribosomal protein L18-A) (Q10192)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL21A
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein eL31
Sequence:
MGIDIERHHVKKSQRSKPASENVYLKLLVKLYRFLARRTDSRFNKAILKRLFQSKTNRPPISISKIAALTSRKSASSQNKTTVVVGTVTDDERMLTVPKLSIAALRFTKSARARILKAGGEVLTLDQLALRAPTGSNTVLVRGKKHAREAYRHFGFGPHKHKAPYVRSEGRKFERARGRRKSRAFKV
Protein: Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (AC5) (O95622)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion.
Subcellular location: Cell membrane {ECO:0000305|PubMed:15385642, ECO:0000305|PubMed:26206488}; Multi-pass membrane protein. Cell projection, cilium {ECO:0000250|UniProtKB:P84309}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- A-kinase anchor protein 5
- Rap guanine nucleotide exchange factor 3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Adenylate cyclase type 6
- 3',5'-cyclic-AMP phosphodiesterase 4C
- Rap guanine nucleotide exchange factor 4
Sequence:
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q9VHV8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Stress-activated protein kinase JNK
- Tumor necrosis factor family member eiger
- Transcription factor kayak, isoforms A/B/F
- Transcription factor Jra
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- Mitogen-activated protein kinase kinase kinase
- Mitogen-activated protein kinase p38a
- Mitogen-activated protein kinase p38b
- Mitogen-activated protein kinase ERK-A
- Ras-related protein Rac1
Sequence:
MCVNRETQSSSNNNSNNTTTATSTARNNNSHNGRCECDGDGDSVSHIQSEMKMRIKREAPCLLLFMPIQNTNNNNRIGANQKDYPNKRSRENLACDEVTSTTSSSTAMNGGGRTPALTRSCSSPAVYDIETHPASPVFPHLLLGNGRDADDPSSVGANCVLNVTCQSPNESHLQGLKYMQIPASDTPHQNIKQYFQEAYDFIEDARKTGSRVLLHCHAGISRSATIAIAYVMRYKSLSLLEAYKLVKVARPIISPNLNFMGQLLELEQNLRKSGVLAPATPHLNSPSNPSSSSVGLSTQSSQLVEQPEEEEKREQRERGKSKSDSEAMDEDGFDYDDVDSGSGSLAGSNCSSRLTSPPITPDDEAPSTSAAASSVSELDSPSSTSSSSGICSLLQSTSSSVSPRAISKPNLLSPTRQLALFKRNSPAKLRLDLESSYAPASPIPNTMPWLSVPSTPVCEEAPDSRINHVASNLTRD
Protein: Uncharacterized protein (F4I3N6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MCSLSMQFSLLQSPPSRPCPSFLANHEPKLSTTSSSVTFPLKTNTWKCSGTGNLLVLRVKAYGSSSDSSADSSTPPNGTRQPKSRRDILLEYVQNVKPEFMEMFVKRAPKHVVEAMRQTVTNMIGTLPPQFFAVTVTSVAENLAQLMMSVLMTGYMFRNAQYRLELQQSLEQVALPEPRDQKGGDEDYAPGTQKNVSGEVIRWNNVSGPEKIDAKKYIELLEAEIEELNRQVGRKSANQQNEILEYLKSLEPQNLKA
Protein: Calmodulin-like protein, putative (Q38DQ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calmodulin, putative
- Calmodulin, putative
- Calmodulin
- Glycogen synthase kinase 3
Sequence:
MSRASIMKEAFELLQRDGKIPKASIPTALRAAGMNPSEEKLKEIMATAVDIDMAGYESLVTEHYDKTDTVEAVKEAFRVFDKDHNGTVSVAEFRHIMTTMGEKYTEEEFCDLIQGFDANGVIPYEKFVEKMLAPFTEHESA
Protein: Peroxisome assembly protein 26 (Peroxin-26) (Q7Z412)
Organism: Homo sapiens (Human)
Function: Peroxisomal docking factor that anchors PEX1 and PEX6 to peroxisome membranes. PEX26 is therefore required for the formation of the PEX1-PEX6 AAA ATPase complex, a complex that mediates the extraction of the PEX5 receptor from peroxisomal membrane.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16257970}; Single-pass type II membrane protein {ECO:0000269|PubMed:12717447}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisomal ATPase PEX1
- Peroxisomal biogenesis factor 19
- Peroxisomal targeting signal 1 receptor
- Peroxisomal biogenesis factor 3
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 2
Sequence:
MKSDSSTSAAPLRGLGGPLRSSEPVRAVPARAPAVDLLEEAADLLVVHLDFRAALETCERAWQSLANHAVAEEPAGTSLEVKCSLCVVGIQALAEMDRWQEVLSWVLQYYQVPEKLPPKVLELCILLYSKMQEPGAVLDVVGAWLQDPANQNLPEYGALAEFHVQRVLLPLGCLSEAEELVVGSAAFGEERRLDVLQAIHTARQQQKQEHSGSEEAQKPNLEGSVSHKFLSLPMLVRQLWDSAVSHFFSLPFKKSLLAALILCLLVVRFDPASPSSLHFLYKLAQLFRWIRKAAFSRLYQLRIRD
Protein: histidine kinase (EC 2.7.13.3) (O31138)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
Sequence:
MFKDLGIKGRVLLLTLLPTSLLAMVLGGYFTWVQLSDMRAQLIERGQLIAEQLAPLAATALARKDTAVLNRIANEALDQPDVRAVTFLDARQERLAHAGPSMLTVAPAGDASHLSMSTELDTTHFLLPVLGRHHSLSGATEPDDERVLGWVELELSHHGTLLRGYRSLFTSLLLIAAGLGVTALLALRMSRAINAPLELISQGVAQLKEGRMETRLPPMGSNELDELASGINRMAETLQSAQEEMQHNIDQATEDVRQNLETIEIQNIELDLARKEALEASRIKSEFLANMSHEIRTPLNGILGFTNLLQKSELSPRQQDYLTTIQKSAESLLGIINEILDFSKIEAGKLVLENLPFNLRDLIQDALTMLAPAAHEKQLELVSLVYRDTPIQLQGDPQRLKQILTNLVGNAIKFTQGGTVAVRAMLEDESDDRAQLRISVQDTGIGLSEEDQQALFKAFSQADNSLSRQAGGTGLGLVISKRLIEQMGGEIGVDSTPGEGAEFWISLSLPKSRDDNEEPGASWAAGQRVALLEPQELTRRSLHHQLTDFGLEVSEFADLDSLQESLRNPPPGQLPISLAVLGVSAAIHPPEELSQSFWEFERLGCKTLVLCPTTEQAQYHATLPDEQVEAKPACTRKLQRKLQELLQVRPTRSDKPHAMVSGRPPRLLCVDDNPANLLLVQTLLSDLGAQVTAVDSGYAALEVVQRERFDLVFMDVQMPGMDGRQATEAIRRWEAEREVSPVPVIALTAHALSNEKRALLQAGMDDYLTKPIDEQQLAQVVLKWTGLSLGQSLASMSRAPQLGQLSVLDPEEGLRLAAGKADLAADMLAMLLASLAADRQAIRQARDNDDRTALLERVHRLHGATRYCGVPQLRAACQTSETLLKQNDPAAAAALDELDKAIEALADTASATTHLSSTSLDSSEL
Protein: Uncharacterized protein (Q8IQJ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEHVNSTNARQPQHHHFDQQLQHNDSQQQFCLRWHNHQTSLLSTLPILLDQSHLTDVTISAEGRQLRAHRVVLSACSSFFMDIFRALEASNHPVIIIPGASFGAIVSLLTFMYSGEVNVYEEQIPMLLNLAETLGIKGLADVQNNNLPKTARSGGGSYMDTTNEKSSEFERPTTPSPTPTPTLTPSHTPTPSHSLPLPQLPSAALNTPLLANKLGSVNSSGMGTTPLENLFKSLQFYPSLLPQPLNFSQTALNKTTELLAKYQQQCQLYQSGMQEDQLETDCFGSKRLKGDSPPKELRRLEKSLLKNPKSSSTTNSSSSKSPQECSNPNPIVATSPVTLAPPTMAHFSPQLPVVKCSSASYPSALGQGQLYSSKPPLYSAAVTPTAAQQAAQMHHHPQPGPSPYISAEDHAKLQLHIEQYQREAAAAAAAAAGGMALVSAKSEPNLLSLSADRDKSLATAPIKPPSNSKLYATCFICHKQLSNQYNLRVHLETHQNVRYACNVCSHVSRSKDALRKHVSYRHPGAPSPCENEARRKRVSKLAATTVPTSTPMSMSASHTVTSGDVGPAPATTLGCSGQEARNPYLFLPNQFQMAAAAAAVAVAESSPASGQPSLDLAHEAPPSIKSEREPPTASNGEATGVEASASTT
Protein: Low affinity immunoglobulin gamma Fc region receptor II-b (IgG Fc receptor II-b) (CDw32) (Fc-gamma RII-b) (Fc-gamma-RIIb) (FcRII-b) (CD antigen CD32) (P31994)
Organism: Homo sapiens (Human)
Function: Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
- Galectin-3
- C-type lectin domain family 7 member A
- Tyrosine-protein kinase SYK
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- Tyrosine-protein kinase Lyn
- Immunoglobulin heavy variable 4-38-2
- B-lymphocyte antigen CD19
- Immunoglobulin lambda-like polypeptide 5
- Receptor-type tyrosine-protein phosphatase C
Sequence:
MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWINVLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPNFSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAAVVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDALEEPDDQNRI
Protein: Platelet-activating factor acetylhydrolase (PAF acetylhydrolase) (EC 3.1.1.47) (1-alkyl-2-acetylglycerophosphocholine esterase) (2-acetyl-1-alkylglycerophosphocholine esterase) (Group-VIIA phospholipase A2) (gVIIA-PLA2) (LDL-associated phospholipase A2) (LDL-PLA(2)) (PAF 2-acylhydrolase) (Q13093)
Organism: Homo sapiens (Human)
Function: Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response. At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position. Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups. Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells. Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in low-density lipoprotein (LDL) particles and uncontrolled pro-inflammatory effects. As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall. Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:11590221, ECO:0000269|PubMed:12821559, ECO:0000269|PubMed:18434304}. Note=Associates with both LDL and HDL particles in plasma (PubMed:10066756, PubMed:11590221, PubMed:12821559, PubMed:18434304). Mainly associates with pro-inflammatory electronegative LDL particles (PubMed:12821559). {ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:11590221, ECO:0000269|PubMed:12821559, ECO:0000269|PubMed:18434304}.
Interaction partners:
- Lysophosphatidylcholine acyltransferase 2
- Apolipoprotein E
- Lysophosphatidylcholine acyltransferase 1
- Apolipoprotein B-100
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Cholinephosphotransferase 1
- Apolipoprotein A-I
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Apolipoprotein A-V
- Serum paraoxonase/arylesterase 1
Sequence:
MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNILRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGTNINTTNQHIMLQNSSGIEKYN
Protein: Vesicle transport v-SNARE N-terminal domain-containing protein (Q582L5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Syntaxin, putative
- SNARE protein, putative
- Syntaxin, putative
- Gamma-soluble NSF attachment protein
Sequence:
MSNAEAYDKKLKMLEVKAQGLLRDLKTTADPIRRLRCHTEAQNTLNEIQQNYQLLKTEIQLLEGDEGKLYKNAEQEHAHELSNLKRMLQLEKAPVPVVPGDQSSSMFGALPATGDRREEARRIAQSVVTIQGTTLGSLAQAERALHDTEEVSVNATTRLIAQTEQIRNIRDRVEDLDSEVTRARKELNEFIHRMATDKIIICFYILIMIGIIIFATLKFLQK