wanglab/gogpt-training-data huggingface dataset:
Protein: BMP-2-inducible protein kinase (BIKe) (EC 2.7.11.1) (Q9NSY1)
Organism: Homo sapiens (Human)
Function: May be involved in osteoblast differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:9853615}.
Interaction partners:
- RalBP1-associated Eps domain-containing protein 1
- Phosphatidylinositol-binding clathrin assembly protein
- Protein numb homolog
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- AP-2 complex subunit beta
- Numb-like protein
- Clathrin interactor 1
- RalA-binding protein 1
Sequence:
MKKFSRMPKSEGGSGGGAAGGGAGGAGAGAGCGSGGSSVGVRVFAVGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAKKDCPVSNINNSSIPSALPEPMTASEAAARKSQIKARITDTIGPTETSIAPRQRPKANSATTATPSVLTIQSSATPVKVLAPGEFGNHRPKGALRPGNGPEILLGQGPPQQPPQQHRVLQQLQQGDWRLQQLHLQHRHPHQQQQQQQQQQQQQQQQQQQQQQQQQQQHHHHHHHHLLQDAYMQQYQHATQQQQMLQQQFLMHSVYQPQPSASQYPTMMPQYQQAFFQQQMLAQHQPSQQQASPEYLTSPQEFSPALVSYTSSLPAQVGTIMDSSYSANRSVADKEAIANFTNQKNISNPPDMSGWNPFGEDNFSKLTEEELLDREFDLLRSNRLEERASSDKNVDSLSAPHNHPPEDPFGSVPFISHSGSPEKKAEHSSINQENGTANPIKNGKTSPASKDQRTGKKTSVQGQVQKGNDESESDFESDPPSPKSSEEEEQDDEEVLQGEQGDFNDDDTEPENLGHRPLLMDSEDEEEEEKHSSDSDYEQAKAKYSDMSSVYRDRSGSGPTQDLNTILLTSAQLSSDVAVETPKQEFDVFGAVPFFAVRAQQPQQEKNEKNLPQHRFPAAGLEQEEFDVFTKAPFSKKVNVQECHAVGPEAHTIPGYPKSVDVFGSTPFQPFLTSTSKSESNEDLFGLVPFDEITGSQQQKVKQRSLQKLSSRQRRTKQDMSKSNGKRHHGTPTSTKKTLKPTYRTPERARRHKKVGRRDSQSSNEFLTISDSKENISVALTDGKDRGNVLQPEESLLDPFGAKPFHSPDLSWHPPHQGLSDIRADHNTVLPGRPRQNSLHGSFHSADVLKMDDFGAVPFTELVVQSITPHQSQQSQPVELDPFGAAPFPSKQ
Protein: CCCTC-binding factor (A0A2R8YFL0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGDAVEAIVEESETFIKGKERKTYQRRREGGQEEDACHLPQNQTDGGEVVQDVNSSVQMVMMEQLDPTLLQMKTEVMEGTVAPEAEAAVDDTQIITLQVVNMEEQPINIGELQLVQVPVPVTVPVATTSVEELQGAYENEVSKEGLAESEPMICHTLPLPEGFQVVKVGANGEVETLEQGELPPQEDPSWQKDPDYQPPAKKTKKTKKSKLRYTEEGKDVDVSVYDFEEEQQEGLLSEVNAEKVVGNMKPPKPTKIKKKGVKKTFQCELCSYTCPRRSNLDRHMKSHTDERPHKCHLCGRAFRTVTLLRNHLNTHTGTRPHKCPDCDMAFVTSGELVRHRRYKHTHEKPFKCSMCDYASVEVSKLKRHIRSHTGERPFQCSLCSYASRDTYKLKRHMRTHSGEKPYECYICHARFTQSGTMKMHILQKHTENVAKFHCPHCDTVIARKSDLGVHLRKQHSYIEQGKKCRYCDAVFHERYALIQHQKSHKNEKRFKCDQCDYACRQERHMIMHKRTHTGEKPYACSHCDKTFRQKQLLDMHFKRYHDPNFVPAAFVCSKCGKTFTRRNTMARHADNCAGPDGVEGENGGETKKSKRGRKRKMRSKKEDSSDSENAEPDLDDNEDEEEPAVEIEPEPEPQPVTPAPPPAKKRRGRPPGRTNQPKQNQPIIQVEDQNTGAIENIIVEVKKEPDAEPAEGEEEEAQPAATDAPNGDLTPEMILSMMDR
Protein: Casein kinase II subunit alpha-4, chloroplastic (CK2-alpha4) (EC 2.7.11.1) (Plastid-targeted casein kinase 2 alpha) (cpCK2alpha) (O64816)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site (By similarity). Involved in the regulation of various developmental processes. Involved in the regulation of plant growth and flowering time. Involved in retrograde signaling in plant responses to abscisic acid (ABA) and heat stress. May act as an enhancing factor in abiotic stress signaling through modulation of the expression of some molecular players in retrograde signaling. Phosphorylates RuBisCo activase (RCA) at Thr-78.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Putative casein kinase II subunit beta-4
- Casein kinase II subunit beta-3
- Casein kinase II subunit beta-1
- UPF0235 protein At5g63440
- Casein kinase II subunit beta-2
- FACT complex subunit SSRP1
- Protein CCA1
- Probable cysteine protease RD21C
- Cysteine proteinase RD21A
- Probable cysteine protease RD21B
Sequence:
MALRPCTGFTISSLRNASAANNNLFSLLSFSSSSPAKRNLLLSSLQDNLRRFASSASLYRQHLRNQQQQHQQQQQSRVKEKSETLAQKIGKSIRRAGAPSKARVYADVNVVRPKDYWDYESLAVQWGVQDDYEVVRKVGRGKYSEVFEGIHATDNEKCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQQSKTPSLIFEHVNNKDFKVLYPTLSDYDVRYYIFELLKALDFCHSRGIMHRDVKPHNVMIDHEQRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDLWSLGCMFAGMIFRKEPFFYGHDNYDQLVKIAKVLGTDELNAYLNKYRIELDPNLTSLVGRHSRKPWTKFINSENQHLAVPEAVDFVDKLLRYDHQERPTAKEAMAHPYFYPIRNAESSRTPRSQ
Protein: Heme A synthase (HAS) (EC 1.17.99.9) (Cytochrome aa3-controlling protein) (P12946)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:12206660, ECO:0000269|PubMed:16321940, ECO:0000269|PubMed:30397130, ECO:0000269|PubMed:7961419}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:30397130}.
Interaction partners:
- Protoheme IX farnesyltransferase 2
- Protoheme IX farnesyltransferase 1
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4B
- Protein CtaG
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Copper transport protein CutJ
- Quinol oxidase subunit 2
- SCO1 protein homolog
Sequence:
MNKALKALGVLTTFVMLIVLIGGALVTKTGSGQGCGRQWPLCHGRFFPELNPASIIEWSHRFASGISIILVLSLAFWSWRKITPIFRETTFLAIMSIIFLFLQALLGALAVVFGSNALIMALHFGISLISFASVLILTLLIFEADKSVRTLVKPLQIGKKMQFHMIGILIYSYIVVYTGAYVRHTESSLACPNVPLCSPLNNGLPTQFHEWVQMGHRAAALLLFVWIIVAAVHAITSYKDQKQIFWGWISCLIFITLQALSGIMIVYSELALGFALAHSFFIACLFGVLCYFLLLIARFRYESRQS
Protein: WRKY transcription factor WRKY62 (OsWRKY62) (XA21-binding protein 10) (B8BF91)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Regulates negatively basal innate immunity and XA21-mediated defense against X.oryzae pv. oryzae (Xoo) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6QHD1, ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
Sequence:
MDDDGDGSSSPTDDSAAAGLLPLFSRSPAEDLEEKLRRAMEENARLTRALDAILAGHHAHQRALLAPSLSPPPPSATARAPSVSTSCAAREDAAPAVAAAAASTACPSRQQPPTAEPRPKVRTVRVRADAADATDANSMAETVKDGYQWRKYGQKVTRDNPYPRAYFRCAFAPSCPVKKKLQRCAEDRSMLVATYEGEHNHALSTQTTEFVASGCTTSQHAGGSSSSPLPCSISINSSGRTITLDLTNQAGSGSIASCGVEAAAVSGELVTVLSPELRRHLVEEVVQVLKNDAEFVEAVTNAVAARVVDQIPHIPVHL
Protein: Globin domain-containing protein (A0A1D8PD58)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSTTFRYSAASDFHQPLGSNKNNVFERNNSTVSSTNSLMSNNSDTNTAATAATSGSTTNNVKRMHSSLISKYNSNRSTIFTNDTDSISSSMSYDNNSTLASSVSPNSPANHHSSKHQHQLPSYMMNKSPQYIHQSTSRHSNLNNTNNLLHNTHSNHSQHSQHQHILNEDLVTLNSSMDNLEDGFYKLIRLDTRISFESYYVEQKQEQYKVKLQLNKHQIDLLRYTWNQMLLEESNEDEIFDDGGIDNYDLDEEGNIEENINVYYANNDSIPGAFPTGYNNSRRRIIKRKSSRNVNGSGSTNTNTMTRLDSTTIASSLFCRQLYFNLLSKDPTLEKMFPSIKHQAANMAGILSLTISQLENLSILDEYLAKLGKLHSRVLNIEEAHFKLMGEAFVQTFQERFGSKFTKELENLWIKLYLYIANTLLQTGIDPVLKLTRYESNGSFTTSTNIDLTNGDSILLDDTDTDNDNVSVSNILDPKHQQQQYGGSSFNQDDNDNNNDGGVHPSTNTVVLTKSNISIIESVAPHHQQQKNSSGSSAATPTAPSKKSKFSIRKKKKENCVVM
Protein: Small ribosomal subunit protein mS39 (Pentatricopeptide repeat domain-containing protein 3 homolog, mitochondrial) (A1Z9A8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial protein that may have a role in mitochondrial translation.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96EY7}.
Interaction partners:
- LD06441p
- GH07821p
- Small ribosomal subunit protein mS31
- LD24471p
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS5m
- Mitochondrial ribosomal protein S11
- IP05433p
Sequence:
MYLSRQLRLLPRANIACSLSSSGAHYTTAAPAEDAPIEIPNRIERSPTDLLQALASTVARDYTAPHYKYHDDPFLIPMSNAAKRTYAMSKESGRKAAKWIKEEHRELFMHQEAQPAIEKFAPSMVYTEDSVVDETSLAQLISQGELKDAVLVYNLLEQKGNPISPELKQSLLELVCFHNNQEPIPEEYIEERWFLQNNKRRERSGKTWKDGDLAEKLYSEIEPKTPQSYASLIRGMAKYLQCERAYALLQEAGEKQVQLDTNTFNSVIEIVSFLKDTAEQRWQLCKDLLNEMSQQKLRPNLGTLNAVLQCISTFGNFKVARAAALQALPEFKQLGVNPSLGSYYYLLIIFCRERGPVSHVIVDILNDISGKEFQIQHPKDTYFFATAMDVCRNHLHDKSLAKKVDELLHTGKNYDLVGDSFKESIYYRNYLALLCQTESTEDFMLSYDLLVPNIYIPEPGIMEEILRAIEINGAVEYVPRLWSDMVVFDHTHRESLLLYVLRILVDNKPNPDSPAQAQLPEQGAKVALDMFERVEEAIKRLRKVSFTGQMLGDILTLLVRGGSYEKATEVFAHIDKNQHRIPGTPSLNALIEFVDASVQEKSPSQALFALQYAVENNFDSRELAKRIHEGFTLNETHLSKLKSLVGESFLDK
Protein: Lysophospholipase (EC 3.1.1.5) (G8BBB9)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Glycerophosphodiester phosphodiesterase
- Lysophospholipid acyltransferase
- Lysophospholipase NTE1
Sequence:
MQRYILLYIYLLATVFAAVWPFQQEENTLGATPSTPWWEGIFGGATSTSAQSSSTEQQQSQQQSSSVVTEASSTTTPTSSSQPWYAGLLGGSTSSTQASSTPAPSSTSQSERSSSQSASLSIPAASTNSESPFGGWLGGIFGGESSGSSSQAQSTDETESNSDGDGVANPYSPVNVTCSADVLVREGDGLSEGEKNYIEAKQEQTNKFLISFLNNRANLSNFDAESFINDNSDEHNITIGLSFSGGGYRAMLAGAGSILALDNRFEDSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNGSSQIWDLEASILNPNSGDLITLARFYTGVGTAIVSKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSVRNLTSFKDHSMPYSILVANGKTIEDTEISSNSTFIVEISPYESGNFDTLNAFVDTEYLGSSLEDGESHQCVRNYDNAGFIMGTSSSVFNEVFANLDDYDVSTVLRPIFDQIMSVVTDTKGDVAVYKPNPFFQSSYAQIDTIVNNNTLSLVDGGENGQNVPFYPLIQTDRGVDVIFAFDNSADTEQNWPNGTSFTETYKWQFTNQGKGTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSNIIEFHDEKDLNETDVPLIVYLSNHHESYLANFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTEDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQEYCWTGTAEDAPQVSAFGSGSSSSSSSSSVSSSSTVSSSCQRNNSSIAGESRTSNSSSTTTDSSATTATGGGIVIIGGPNLGSSSTPAESTTEPTIEPTTPVESTTTNEPTTSNGPTTSNGPTTSNGPTTSTPPSSYTGHGIRAASSSSSFFIVAVHLCMTYLVTFF
Protein: Hyaluronan synthase 1 (EC 2.4.1.212) (DG42 protein) (Hyaluronate synthase 1) (Hyaluronic acid synthase 1) (HA synthase 1) (xHAS1) (P13563)
Organism: Xenopus laevis (African clawed frog)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKEKAAETMEIPEGIPKDLEPKHPTLWRIIYYSFGVVLLATITAAYVAEFQVLKHEAILFSLGLYGLAMLLHLMMQSLFAFLEIRRVNKSELPCSFKKTVALTIAGYQENPEYLIKCLESCKYVKYPKDKLKIILVIDGNTEDDAYMMEMFKDVFHGEDVGTYVWKGNYHTVKKPEETNKGSCPEVSKPLNEDEGINMVEELVRNKRCVCIMQQWGGKREVMYTAFQAIGTSVDYVQVCDSDTKLDELATVEMVKVLESNDMYGAVGGDVRILNPYDSFISFMSSLRYWMAFNVERACQSYFDCVSCISGPLGMYRNNILQVFLEAWYRQKFLGTYCTLGDDRHLTNRVLSMGYRTKYTHKSRAFSETPSLYLRWLNQQTRWTKSYFREWLYNAQWWHKHHIWMTYESVVSFIFPFFITATVIRLIYAGTIWNVVWLLLCIQIMSLFKSIYACWLRGNFIMLLMSLYSMLYMTGLLPSKYFALLTLNKTGWGTSGRKKIVGNYMPILPLSIWAAVLCGGVGYSIYMDCQNDWSTPEKQKEMYHLLYGCVGYVMYWVIMAVMYWVWVKRCCRKRSQTVTLVHDIPDMCV
Protein: Guanine nucleotide-binding protein subunit beta-2 (Q20636)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in regulating dopamine-mediated locomotion behavior.
Interaction partners:
- Regulator of G-protein signaling 7
- Regulator of G-protein signaling egl-10
- Latrophilin-like protein 1
- Guanine nucleotide-binding protein subunit alpha
- G protein gamma domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein alpha-12 subunit
- Phosducin thioredoxin-like domain-containing protein
Sequence:
MSTIAGESSSSSKMPENSQPTTTEKGSEYLEQLANEAEELRKKLDQERHKLNDIPIQQAAERLDVMGALGVKQRRILKGHVGKVLCMDWSLDKRHIVSSSQDGKVIVWDGFTTNKEHALTMPTTWVMACAFSPSSQMIACGGLDNKCSVVPLSFEDDIIQKKRQVATHTSYMSCCTFLRSDNLILTGSGDSTCAIWDVESGQLIQNFHGHTGDVFAIDVPKCDTGNTFISAGADKHSLVWDIRSGQCVQSFEGHEADINTVRFHPNGDAFATGSDDATCRLFDLRADRQVCVYEKESILFPVNGVDFSLSGRILFAGYGDYRVGVWDSLKCARHSVLYGHENRISCLRTSPDGTAVCSASWDCTIRIWA
Protein: Malate synthase A (MSA) (EC 2.3.3.9) (P08997)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Isocitrate lyase
- Citrate synthase
- Phosphate acetyltransferase
- NADP-dependent malic enzyme
- Acetyl-coenzyme A synthetase
- Malate synthase G
- Isocitrate dehydrogenase kinase/phosphatase
- Malate dehydrogenase
- Phosphoenolpyruvate carboxylase
- Glyoxylate/hydroxypyruvate reductase A
Sequence:
MTEQATTTDELAFTRPYGEQEKQILTAEAVEFLTELVTHFTPQRNKLLAARIQQQQDIDNGTLPDFISETASIRDADWKIRGIPADLEDRRVEITGPVERKMVINALNANVKVFMADFEDSLAPDWNKVIDGQINLRDAVNGTISYTNEAGKIYQLKPNPAVLICRVRGLHLPEKHVTWRGEAIPGSLFDFALYFFHNYQALLAKGSGPYFYLPKTQSWQEAAWWSEVFSYAEDRFNLPRGTIKATLLIETLPAVFQMDEILHALRDHIVGLNCGRWDYIFSYIKTLKNYPDRVLPDRQAVTMDKPFLNAYSRLLIKTCHKRGAFAMGGMAAFIPSKDEEHNNQVLNKVKADKSLEANNGHDGTWIAHPGLADTAMAVFNDILGSRKNQLEVMREQDAPITADQLLAPCDGERTEEGMRANIRVAVQYIEAWISGNGCVPIYGLMEDAATAEISRTSIWQWIHHQKTLSNGKPVTKALFRQMLGEEMKVIASELGEERFSQGRFDDAARLMEQITTSDELIDFLTLPGYRLLA
Protein: Zinc carboxypeptidase, putative (Q383Q1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSRIEKSVRGKGAVKLRGFLKSKEQLFATKLSSPRVECRAGNEEKGAMGEKDVTGGRHVHGVVAPHRTLDTGTASVPLPANLPPDGKGKKLLNPLRKKLLRDLSADEGGSLQHLPAKPTGHKELGAIRIATADVFPAGEAPHRPAALSSAVLSSPMQGLKTAAGKLNPPVGIGRKKRQQKLQKAQLASTVRVERLRSDGTSRCGKKGSVKVPSECSSLNSSITCTVNTNDCAELDRESGVDDIDDPNDDNAQELSANELGDELAPYDEVDEEEAVQRYMGSHRASTSPKKTEDSVSLNRCLSDPSLSNTLCDARAAPLDRPNSAIGSCAAPEDLQRSLDEKMEESSRRPSTAGQLGEGTSSFGTQKASELFNDSLCRSLSLYDAFFLNEDGTTWLVDDRVLARCLNYIGLMDYEHELHGLRRTTGNNLSASAWAQLSSPVKRNVMPSSVASAAPPLRCTTSPNFVNSSNSFSVGQSKLCKAPESRGGRPDFPTLFLDIDETMRWLSGQEYVIGTILACCTRDSDASEDGNVQPYLSPAVHPIKQIATIVRECYPHWGSTVRFADAWEKQVVLVLGTSSPSHQLLFPFPEEGIFFSSDMEGGNIARVERMPESTLLHLQQYPQQPNGIGFSLWMEPEPGCGQRLWFRFAFAGVKPHTSVTLRLVNIQPTTKLYGRNGMRPVWRAGNCLRQWVPVAQCSYRTTNDEADGELTFVITPRTNDVIHVAFCVPYTYADLLCHITHWHNLVKNSTCDIWFEERVLCYTQDGRKLHMLIITSSSTKTNQRHRSKRKVEGSNSANNGACGPTACNANSNGGGGNPSRKPIVGPYSQFEKGKKVVLVSGRVHPGETTASHGVHGAISFLLSRDPLAAKLRDNFIFYIVPMLNPDGVSRGHTRLDQNGFNLNRCYNRPIPQTQPTVSALRKVFDHLRQVFDDRFFMYLDFHSHVSQSSCFAFGNCLPATVQHWNMLFPKIISLHAKELFGYSICRFGRGHMLSKEGSSRVLFGAGLIHSYTIELTYFTNNRLYIDGLLAGGTSNIMDGESWEDRYTHTQIVPQRSPVAHNASTVTPLNEQGTAVGAVKSSKCVRSNSQQKRLKKRDVTKIPSDCGNGKPELLRQIRVPCILAQSAEVGRSCMLSLLDYCSVDNYISPQFAAYGGMERMLRDVKRHMGSPTAAKPGSCRLQFIYKQQQQLQQ
Protein: Kyphoscoliosis peptidase (EC 3.4.-.-) (Q8C8H8)
Organism: Mus musculus (Mouse)
Function: Probable cytoskeleton-associated protease required for normal muscle growth. Involved in function, maturation and stabilization of the neuromuscular junction. May act by cleaving muscle-specific proteins such as FLNC.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line.
Interaction partners:
Sequence:
MELKKDSNAVAIDMLLIVHSEKRRAAQATHLDPQANPGALLQNRGGFQGVRNGIRKWQELEENSFQGNLPEKQCLQQPQVITSYDNQGTQLTVEIHPQDAMPQLLKKFSLAKRLQGDKNGNMRPRQPGGKDAHAYPWDRSSLKSMPLDLRLFEKLDASASQVTVKSGLNELVSDLLQEAHSDLERVRAIWIWICHHIEYDVEAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRVAGVQCVTVPGYSKGFGYQTGQSFSGEFDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKFTFLYNEFYFLTHPALFIEDHFPDNKNWQLLKPPQSLRQFENSMYHKSEFYNKGMLSAHPETSMIRTVNGKATITIESRAPTLFMFMLNGKQEHGLLSLRKNGMKLEVYPPTMGTHKLQIFAKGNSEIYSSVLEYTLKCNYVDFSVQLPSELHQPVGPSWFSEQMGITKPSHSDPIIHTSDGRCAISFSVEEGVSVLASLHGDDGPITEETQRRYIFQLNRGKRTELKVQLPHAGKFALKIFVKKRQEQGNFIFVFNYLLCCANTKVNWPMFPESFGNWGQDNELLEPLSGVLPANRNVAFKLKLHGIAKALVKGQDTWPLTLNPEGYWEGSCNTAGCQEVYVMVLENANHNFYSYILKYKVNDQ
Protein: coagulation factor Xa (EC 3.4.21.6) (F1QLC3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Prothrombin
- Antithrombin-III
- Coagulation factor VIII, procoagulant component.
- Coagulation factor V
- Tissue factor
- Coagulation factor IX
- Furin
- Carboxypeptidase B2
- Alpha-1-antitrypsin precursor
- Coagulation factor VII.
Sequence:
MSWVFWNFISLFVTHSVCAEVFLNTRDANQVLIRQRRANSLFEEMKKGNMERECIEERCNYEEAREIFEDVKKTDEFWHKYVDGDACLSHPCVNGGQCKDAIGPYTCFCQQGFKGYNCEIVIPELCENENGGCDHFCEVMEKNVVCSCANGYELAPNGKSCQSQDPFKCGVIYPKKTRSIFFHTPNITESENEEETELEATIEPVYNHSNPLNNQTDSMFGLHELEIIEEEPILPVVSTAGDGRIVNGVECPPGDCPWQALLINENNMGFCGGTILTEHFILSAAHCMNESLSIRVVVGEYDTLVPEGREATHDVDEILIHKNYQPDTYHNDIALIKLSKPIKFTKYIIPACLPEMKFAERVLMQQDDGLVSGFGRVREGGLSSTILQKLTVPYVNRAKCIESSNFKISGRMFCAGYDQEEKDACQGDSGGPHVTRFKNTWFITGVVSWGEGCARKGKYGVYTQVSKYIMWINNAMTKVMPETGASLKPKAKRELRHKTPIRRV
Protein: Auxin efflux carrier component 1a (OsPIN1a) (Auxin efflux carrier component 1) (OsPIN1) (Ethylene-insensitive root 1 homolog) (OsPIN1b) (Q5SMQ9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts as a component of the auxin efflux carrier. Seems to be involved in the polar auxin transport which may promote adventitious root emergence and control tillering.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MITAADFYHVMTAMVPLYVAMILAYGSVKWWRIFTPDQCSGINRFVALFAVPLLSFHFISTNNPYTMNLRFIAADTLQKLMVLAMLTAWSHLSRRGSLEWTITLFSLSTLPNTLVMGIPLLKGMYGEFSGSLMVQIVVLQCIIWYTLMLFMFEYRGARMLITEQFPDTAANIASIVVDPDVVSLDGRRDAIETETEVKEDGRIHVTVRRSNASRSDIYSRRSMGFSSTTPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMVGRSSNFGAADAFGVRTGATPRPSNYEDDASKPKYPLPASNAAPMAGHYPAPNPAVSSAPKGAKKAATNGQAKGEDLHMFVWSSSASPVSDVFGGGAPDYNDAAAVKSPRKMDGAKDREDYVERDDFSFGNRGVMDRDAEAGDEKAAAAAGADPSKAMAAPTAMPPTSVMTRLILIMVWRKLIRNPNTYSSLIGLIWSLVCFRWNFEMPAIVLKSISILSDAGLGMAMFSLGLFMALQPHIIACGNKVATYAMAVRFLAGPAVMAAASFAVGLRGTLLHVAIVQAALPQGIVPFVFAKEYSVHPSILSTAVIFGMLIALPITLVYYILLGL
Protein: Palmitoyltransferase Hip14 (EC 2.3.1.225) (Huntingtin-interacting protein 14 homolog) (Q9VUW9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable palmitoyltransferase which is required for photoreceptor synaptic transmission and for the correct expression and localization of palmitoylated protein Csp and synaptosomal-associated protein Snap25. Probably palmitoylates Csp. Probably also palmitoylates the dorsal-ventral patterning protein Sog and promotes its secretion and activity and the stabilization of the membrane-bound form. Required for synaptic vesicle exocytosis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18032660, ECO:0000269|PubMed:18719403, ECO:0000269|PubMed:20599894}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000269|PubMed:18032660, ECO:0000269|PubMed:18158335}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the Golgi apparatus in non-neuronal cells and located primarily in presynaptic terminals in neurons. {ECO:0000269|PubMed:18032660}.
Interaction partners:
- Huntingtin, isoform A
- Palmitoyltransferase
- Palmitoyltransferase
Sequence:
MYQSACQAATTGSCVPGTGQQPDNERQSALIAQQPPTAPVEPDYSGFDIVKATQYGAIARVRELVESGWDVNQPDSETVTLLHWAAINNRRDIIRYFLEKGATVDAVGGELNATPLHWATRQGHLGAVVLLMAAGADPRIRDAEGCSCIHIAAQFAHTALVAYFIAKGVDPDLQDRGGMTALMWAAWKVCALDPVRLLLTLGANPAMVDYTHGNTALHWAILARNATAISTLVLKSKASLDVPNLRGETPLSMLESQTGAIWIGAKVMDRVKEAALTSQQRRSLLSKLRHDKRLRWWSMVACPFTAFYLAGIVFTVNTLYIIKFFLLGCLYSIFHTIGKALFDEHLMALLPLSVYLATKAWFYVTWLMYIDDAVSFTATVCFLISSLLLWVCFLKSWKGDPGIIRPTREQRFKTIIELSERGGIGFEPASFCSGCLVRRPIRSKHCSVCDRCVARFDHHCPWVGNCIGLKNHSYFMGFLWMLLIMCAWMLYGGSKYYVNQCNVRFDDFLGAMRAIGNCDAWVGWVMGNALLHMSWVILLTICQTYQVICLGMTTNERMNRGRYRHFQAKGGHSPFTRGPIQNLVDFLECSCFGLVQPKRVDWMNYYDYDAQTHQTIEKEPLLSVDCPDGMAGDHQYV
Protein: Uncoordinated 115a, isoform E (A0A0B4LGZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFGVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNAIHSYRSPPKPGYGFKTTTLPYIRNGFSSDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSMLVHEPAKIYPYHLLLITNYRLPSDVDRCNLERHLSDIEFEHILQCARSEFYRLPQWRRNELKRRVKLF
Protein: Myb/SANT-like DNA-binding domain protein (F4JHK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLWYNDMHRILREPGMDQYGIPVERKEMKHKGRNVIWSVGMDKCLIEALAVQAKNGNKVDKCFNDKAYTAACVAVNTRFNLNLTSQKAINRLKTIKKRYRVMRDILSRDGFWWNSSTKMIDCESDELWRRYIAVNPDAKAFRGKQIEMYEELRTVCGDYQTPGKYNKVKKESSHHLNDVKQFEEDSVSFPLGSSEEHSDTDGTESYAGASEYMHEESQDLPPPRDPLRRPSKRSRNSDPCQEAMLVVASSIRRLADAVVQSKTLINTEELLKAVMEIDELEEAKQMYAFEYLNGDPVKARAFMAYNNRMRKMFLFRQFWWWK
Protein: Growth hormone (A4GX94)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
AFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Phosphocarrier protein HPr (Histidine-containing protein) (P0AA04)
Organism: Escherichia coli (strain K12)
Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
Subcellular location: Cytoplasm.
Interaction partners:
- PTS system glucose-specific EIIA component
- Phosphoenolpyruvate-protein phosphotransferase
- PTS system mannitol-specific EIICBA component
- PTS system mannose-specific EIIAB component
- PTS system glucose-specific EIICB component
- PTS system N,N'-diacetylchitobiose-specific EIIA component
- PTS system fructose-specific EIIB'BC component
- Autoinducer-2 kinase
- Regulator of sigma D
- PTS system N-acetylglucosamine-specific EIICBA component
Sequence:
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE