wanglab/gogpt-training-data huggingface dataset:
Protein: Intermembrane phospholipid transport system binding protein MlaD (P64604)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19383799}; Single-pass type II membrane protein {ECO:0000305|PubMed:19383799}; Periplasmic side {ECO:0000305|PubMed:19383799}.
Interaction partners:
- Intermembrane phospholipid transport system permease protein MlaE
- Intermembrane phospholipid transport system binding protein MlaB
- Intermembrane phospholipid transport system ATP-binding protein MlaF
- Intermembrane phospholipid transport system binding protein MlaC
- Intermembrane phospholipid transport system lipoprotein MlaA
- Acid stress protein IbaG
- Lipophilic envelope-spanning tunnel protein B
- Intermembrane transport protein PqiB
- Phospholipase A1
Sequence:
MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSIGGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFEDPELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVGTTK
Protein: Nicotinamide riboside kinase 2 (M0R0T8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTNGGKTTLTNSLLRALPNCCVIHQDDFFKPQDQIAVGEDGFKQWDVLESLDMEAMLDTVQAWLSSPQKFARAHGVSVQPEASDTHILLLEGFLLYSYNLPGRHEVPRGALP
Protein: Cleavage and polyadenylation specificity factor subunit 5 (Q57WN8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR017888}. Cytoplasm {ECO:0000256|PIRNR:PIRNR017888}.
Interaction partners:
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage stimulation factor 50 kDa subunit
- Cleavage and polyadenylation specificity factor-like protein, putative
- Uncharacterized protein
- RNA-binding protein, putative
- RNA-binding protein, putative
- Suppressor of forked domain-containing protein
Sequence:
MSLKAKIDVFPFDGYLLQDPSVVSVMQAVVRGNKTGGTGVGNSGGASGNETGSGGVGGGNANKRREAGGGTTNSERRIKTPLEKLMSLRARCREQQRVQSVEGVLLVHAHDHPHVLLLRHNVKTTNRSRVLPATNTNSTAVYRLPGGRCRNGEPEELCLLRKLGRDLLNESKRLTSSSTAEEERSEVVVDVGSAHPNGTAVTASSSSFRVGEVLARWYRPHFDPLMYPYVPAHVAENDVREVRTIFLVHMPPRMLLTGTYGDEELVAAPLFDLYDNTAKYGVLIASIPTLLSRVNINYCR
Protein: Kinesin family member 13B (A0A0G2K8Z9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- ArfGAP with dual PH domains 1
- Disks large homolog 4
Sequence:
MTAFFPYFFSAEIDLHTKCVVDVEANKVILNPINTNLSKGDIFAYDHCFWSMDESVREKYAGQDDVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQGAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIINHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQTSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHGIIDIMPEGQVMLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEEREASLKNDSSSEHGGCRRRLLPSEVSSEINFNFEYAQMEVTMKALGSNDPMQSILSSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPERQNCRGVDRLSFHSPQCQQRLRQWAEEREATLNNSLMRLREQIVKANLLVREASYIAEELDKRTEYKVTLQIPASSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLENRLLDMRDLYQEWKECEEDSPVSRSYFKRADPFYDEQENHSLIGVANLQYAVPIINQKGEVAGRLHVEVMRLSGAIGERIAGGDDPTEVSSEKEVRRQVKILQATGLPQHLCHFVFCKYDFWDQQEPVTVAPEVDTSSSPTSKEPQCMVVFDHCSEFSVNITEDFIEYLSEGALAIEVYGHKMNDPRKNPALWDLGIIQAKTNESSDRWSEVTRKLEFWVQILEQNENGEYCPVEVIAAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRSPKTHENIHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKHDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMEAHIPVVFLDLNADDFSSQDNLDDPEAGWDATLTGEEEEEFFELQIVKHHDGEVKAEASWDSAVHNCPQLSKGTPADERVFLILRVAVQLSHPADMQLVLRKRICVHVHGRQGFAQSLLKKMTHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENAASADSEACIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLNRRSISSPSMNRLSGSRQELSPSHSLSSNKGRWESQQDVSQTLVSRGIASGPPALSVSPQNNQSPDPGLNPASYLNPVKSLVPQMPKLLKSLFPDRRGRHSSPLVQQPVPRILVQPTFSDARATRTEEAQQGSPGPSGALESMVKMAAPTVKICDKPVRVSSPPSTMVVTQPQEGQDGPPSPLSEASSGYFSHSVSTATLSETLTLGLDTTGLGSQTPGSPPALCQVTQEPELAFLSCTQSHPTDPEEPHIPPATPTQSTELEVPRPPLLSDPTPAVPTSPFRIRKVRPSELTSFTGMLGGASSGAQEDPVVSEDPSHARGQTLGRLEVTSDSEDASEVPEWLREGEYVVVGTNKTGIVRYIGPTDFQEGTWIGVELDLPAGKNDGSIGGKQYFRCNPGYGLLVRPGRVRRAAGTGRRRSSGLQPQGAPEARRSATISGSATNLASLTAALAKGDRSYKNPENRKSWAS
Protein: Cofilin-2 (Cofilin, muscle isoform) (P45591)
Organism: Mus musculus (Mouse)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere.
Subcellular location: Nucleus matrix. Cytoplasm, cytoskeleton. Note=Colocalizes with CSPR3 in the Z line of sarcomeres. {ECO:0000250|UniProtKB:Q9Y281}.
Interaction partners:
- LIM domain kinase 1
- Actin nucleation-promoting factor WASL
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- LIM domain kinase 2
- Protein phosphatase Slingshot homolog 1
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- WD repeat-containing protein 1
- Protein phosphatase Slingshot homolog 3
Sequence:
MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGSVVVSLEGKPL
Protein: Jupiter microtubule associated homolog 2 (H3BMT0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKPPGGESSNLFGSPEEATPSSRPNRMASNIFGPTEEPQNIPKRTNPPGGKGSGIFDESTPVQTRQHLNPPGGKTSDIFGSPVTATSRLAHPNKPKDHVFLCEGEEPKSDLKAAR
Protein: Transposase InsH for insertion sequence element IS5H (P0CE53)
Organism: Escherichia coli (strain K12)
Function: Involved in the transposition of the insertion sequence IS5.
Interaction partners:
- Transposase InsH for insertion sequence element IS5Y
Sequence:
MSHQLTFADSEFSSKRRQTRKEIFLSRMEQILPWQNMVEVIEPFYPKAGNGRRPYPLETMLRIHCMQHWYNLSDGAMEDALYEIASMRLFARLSLDSALPDRTTIMNFRHLLEQHQLARQLFKTINRWLAEAGVMMTQGTLVDATIIEAPSSTKNKEQQRDPEMHQTKKGNQWHFGMKAHIGVDAKSGLTHSLVTTAANEHDLNQLGNLLHGEEQFVSADAGYQGAPQREELAEVDVDWLIAERPGKVRTLKQHPRKNKTAINIEYMKASIRAKVEHPFRIIKRQFGFVKARYKGLLKNDNQLAMLFTLANLFRADQMIRQWERSH
Protein: Zinc finger MYM-type protein 4 (Zinc finger protein 262) (Q5VZL5)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization.
Interaction partners:
- E3 ubiquitin-protein ligase MIB1
- Zinc finger MYM-type protein 2
- REST corepressor 1
Sequence:
MAEREVESGPRKRFEQKSGAVFDEIVENCGGIMDTEMSEDIDHNLTPTLDSMSYGMPNQTGSENSLLDEDDYFLNSGDLAGIPVVGSDNEDEQDFSSKDNLVSSIHTDDSLEVERRVTQHESDNENEIQIQNKLKKDFPKQFDQVSVFKSIRKDFSLVRENSKETFSGKEKNRDLTYEREKRLDKPHKDLDSRLKSSFFDKAANQVEETLHTHLPQTPETNFRDSSYPFANKESIGSELGNSFASNIRIKEEPLDDEYDKAMAPQQGLLDKIKDEPDNAQEYSHGQQQKTQEGELKISAVFSVSGSPLAPQLTTGFQPSLASSGMNKMLPSVPATAVRVSCSGCKKILQKGQTAYQRKGSTQLFCSTLCLTGYTVPPARPPPPLTKKTCSSCSKDILNPKDVISAQFENTTTSKDFCSQSCLSTYELKKKPIVTINTNSISTKCSMCQKNAVIRHEVNYQNVVHKLCSDACFSKFRSANNLTMNCCENCGGYCYSGSGQCHMLQIEGQSKKFCSSSCITAYKQKSAKITPCALCKSLRSSAEMIENTNSLGKTELFCSVNCLSAYRVKMVTSAGVQVQCNSCKTSAIPQYHLAMSDGSIRNFCSYSCVVAFQNLFNKPTGMNSSVVPLSQGQVIVSIPTGSTVSAGGGSTSAVSPTSISSSAAAGLQRLAAQSQHVGFARSVVKLKCQHCNRLFATKPELLDYKGKMFQFCGKNCSDEYKKINNVMAMCEYCKIEKIVKETVRFSGADKSFCSEGCKLLYKHDLAKRWGNHCKMCSYCLQTSPKLVQNNLGGKVEEFCCEECMSKYTVLFYQMAKCDACKRQGKLSESLKWRGEMKHFCNLLCILMFCNQQSVCDPPSQNNAANISMVQAASAGPPSLRKDSTPVIANVVSLASAPAAQPTVNSNSVLQGAVPTVTAKIIGDASTQTDALKLPPSQPPRLLKNKALLCKPITQTKATSCKPHTQNKECQTEDTPSQPQIIVVPVPVPVFVPIPLHLYTQYAPVPFGIPVPMPVPMLIPSSMDSEDKVTESIEDIKEKLPTHPFEADLLEMAEMIAEDEEKKTLSQGESQTSEHELFLDTKIFEKDQGSTYSGDLESEAVSTPHSWEEELNHYALKSNAVQEADSELKQFSKGETEQDLEADFPSDSFDPLNKGQGIQARSRTRRRHRDGFPQPRRRGRKKSIVAVEPRSLIQGAFQGCSVSGMTLKYMYGVNAWKNWVQWKNAKEEQGDLKCGGVEQASSSPRSDPLGSTQDHALSQESSEPGCRVRSIKLKEDILSCTFAELSLGLCQFIQEVRRPNGEKYDPDSILYLCLGIQQYLFENGRIDNIFTEPYSRFMIELTKLLKIWEPTILPNGYMFSRIEEEHLWECKQLGAYSPIVLLNTLLFFNTKYFQLKNVTEHLKLSFAHVMRRTRTLKYSTKMTYLRFFPPLQKQESEPDKLTVGKRKRNEDDEVPVGVEMAENTDNPLRCPVRLYEFYLSKCSESVKQRNDVFYLQPERSCVPNSPMWYSTFPIDPGTLDTMLTRILMVREVHEELAKAKSEDSDVELSD
Protein: Band 4.1-like protein 5 (Erythrocyte membrane protein band 4.1-like 5) (Q6NYK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Photoreceptor inner segment {ECO:0000256|ARBA:ARBA00004437}.
Interaction partners:
Sequence:
MLSFLRRTLGRRSIRKHAEKARLREAQRATTHIPAAGDAKSIITCRVSLLDGTDVSVDLPKKAKGAELFEQIMYHLDVVEKDYFGLRFMDSAQVPHWLDVTKSIKKQVKIGPPYCLHMRVKFYSSEPNNLHEELTRYLFVLQLKQDILSGKLECPFDTTVELASYALQAELGDYDPAEHGLDLVSEFRFIPNQTEDMEVAIYNAWKECRGQTPAQAEINYLNKAKWLEMYGVDMHMVKARDGNEYSLGLTPTGVLVFEGETKIGLFFWPKITRLDFKKCKLTLVVVEDDEQVMQETEEGKEQEHTFVFRMDHPKACKHLWKCAVEHHAFFRLRGPVQKSSARSGFIRMGSRFRYSGKTEYQTTKANKARRSASFERRPSRRYSRRTMLNRGPNKSSDNHNNGVSPSIEKKPTHTRPPWSGMPVVSSPPSAPGPMEIETLPRSPGGSQSDKRSMPIVTDLLETCVDEVLQATVPMATVEEAGPGAAHTSASSVTEETLSLTEAAARLKQLEIENTPVSVPARTNVNLNMNNQDDVVKLTEKSLNSVSSSPVLNQLKAPDELKSNILKAQAEAALKDSRDELGLTPDKNCNLQEAAARLTGRGGRMGSTTSLPVSGRAERQESWDMLKQPGLLPSSTSSLEEKADDFISSVPPLSSDPVNEAHSSKVKVEDPEPLTAPLTDNLIDFTDPLPVVPPPKPTITPRWIIPASAPTQSGTFTNGLLDCPTKVSSHHPEGSVSPLPQLSQTHNVIATSIVAHSTKDNNHKPKGLLTTEL
Protein: TSC complex subunit 2 (Tuberin) (A0A0G2KHX4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- TBC1 domain family member 7
- GTP-binding protein Rheb
- Ras homolog, mTORC1-binding.
- TSC complex subunit 1a.
- TSC complex subunit 1b
- Glycogen synthase kinase-3 beta
- DNA damage-inducible transcript 4 protein
- DUF3384 domain-containing protein.
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MENSMSSDFLHVLVNLVKFNSCYLDENVSLMVQKICLLCNRTTSSTDIEVALQVLDAVVCYNCLPSDSLTVFIITLCRTVNVKEFCESCWKLMRKVLGTHLGHSAIYTMCRIMEERVYSEDAALLRGAVFFVGMALWGAHRLPALKNTPTLVLPSFYKAMSCANEVVSYEIVLSITRLIKKYGRELQVVTWDILLSIIDRLLQQIQTMGSPDLKVIVYELLSTIEELYEQNDFHGSSARFFSLVEKCADKRPDASVLTLVSYRAQAIQPAKDGWLQNLLKLMDKFFRNESRTMIRIKVLHILSFVLSTNRQLYEEELIEVVVIPQLGQIAEDRDPSVRKQATQLLVDLAEGCSTHHFSSLLDIIEKVASRPLSCSVEGDRELCVESPLEDVRTAILGLLDILQSKLYSLPASHASRVYELLISHLQLHYKNKYCSAISGAIRLKVFDFLLLMRADSLHRLGVPNKDGALRFSPYCHCDPGESEKRVSEKKPTGSVSPPAGSPTPAAPPSSIRTAYLPYSLAFSVLLQCLKTETDWKVLKLVLDKMSCTIQYKVLILTSPCNIDNLCATLCSMVTDRIILERLKKTPDGFSLTDVQLAVVPVLTAITSYHSYLDQLRQRDLVQCLEKGLIYRCAKQCVVALTMCTVEMPDIMIKLLPALIVKLTHISATVAMASPMLEFLSTLVRLPHLYANFVAEQYVSVFAISLPYTNPSKFNQYIVSLAHHVIAMWFIRCRLPFRKDFVQYITKGLRSNALLPFDDTHEQSSFRARSTSLNERPKSLRTTKVAKQGPSANSPVKDLKDLSAMDAFRSRSISVSEHAVRRMQTSSTTCSLGSADENAVMQADDALKTVHLELTETCLDMMARYVFSNFSALPKRSPIADFLLSGGPSMTWLVGNKLVTITTSGGSRTQALLGLDMTERHGGGEMTRSDPSLHTRQTKEAPAKLESQSSQQINTNTRTRVRSISGGHALRAGPAQSLSPLVASPEGEYSGPLPPPGPPLDVLSSQRGMEEHPPPSACNPSPPLKHKHSLAEFVPMLTQGWAEIFIRRPSGNTSWLMCLENPPSPFSSELGNLPLQELSSVLMAMDGVKEPPAERPTDVSQPQGKPAPIQRSNTVASLSSLCSSESSGRFHRSISWADSVVMEESGRSMASVSPAESKEVEEFEAVPSEPIFMNTSTTAPGMMSRSSSTSSQDDDKSTLEEVSEGGIPIDQPPLSLCTPGAQDPELSFTQSSSSSSTLNKSSSSPELQTLPEAFSKASSQSVDPAPTSKIPTVQACVEAPGESAGSTAGTSCSSSSVSVSSSSTSRMRLEFPPVQTGPLSPTGHRPRGHTISVSAPSSRRDRKTLERDARGGATNVEKSSGLSPSFVFLQLYHSPFFGNEANKPLLLPKSQLIDRAVKVLDQMPPYDTHKIGVVFVGAGQANNEVSILSNEYGSKRYAQFLTGLGKLIHLKDCDPDQIFLGGLDQYGDDGEFTYCWHDDIMQAIFHIATLMPNRESDRGCCNKKRHIGNDFVVVVYNDSGEDYKLGTIKGQFNFVEVLIKPLDYESNLVTLQCRKDLEGLVDTSVAKIVSDRNLPLLVRQMALHANMASLVHQCRANPSDAYASKWLARLRHIKRIRTRAQEEIQSRPSHGISLTQGHASMQNKPAHQPPGAAQNPDAGQRKRLVSTVDDFTDFV
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (Q9VH81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- Cytosolic Prostaglandin E synthase
- Hsp90 co-chaperone Cdc37
- Heat shock protein 83
- Raf homolog serine/threonine-protein kinase Raf
- Heat shock protein 75 kDa, mitochondrial
- Cysteine and histidine-rich domain-containing protein morgana
- LD23779p
- AT08303p
- FK506-binding protein 59
Sequence:
MSSSELEVQKAADCQQEAKVPASVEITGSKQPEEDTNARTKAELDFAAAEQYKNQGNEMLKTKEFSKAIDMYTKAIELHPNSAIYYANRSLAHLRQESFGFALQDGVSAVKADPAYLKGYYRRAAAHMSLGKFKQALCDFEFVAKCRPNDKDAKLKFTECNKIVKMRAFERAIAVDKPEKTLSEMYSDMENITIEDDYKGPQLEDGKVTLKFMKELMEHYKAQKRLHRKFAYKILCEIDTYMRAQPSLVDITVPDEEKFTICGDIHGQFYDLMNIFEINGLPSEKNPYLFNGDFVDRGSFSVECIFTLFGFKLLYPNHFFLARGNHESINMNQMYGFTGEVTAKYTSAMADIFTQVFNWLPLCHCINQKILVMHGGLFSTEDVTLDHIRRIERNCQPPEEGLMCELLWSDPQQWMGLGQSKRGVGIQFGPDVTEKFCKDNNLDYIIRSHEVKDMGYEVAHNGKCITVFSAPNYCDTMGNMGAFITITGNNLKPNYKSFEAVPHPDVKPMAYANSLMNWLA
Protein: Proteasome subunit alpha type (H0YMA1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAE
Protein: Iron-sulfur cluster assembly scaffold protein IscU (O31270)
Organism: Azotobacter vinelandii
Function: A scaffold on which IscS assembles Fe-S clusters. Cluster assembly on IscU homodimers proceeds sequentially from 1 2Fe-2S per dimer, to 2 2Fe-2S per dimer and finally 1 4Fe-4S per dimer. Subsequently IscU transfers the Fe-S cluster to other acceptor proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. The clusters are very sensitive to O(2).
Interaction partners:
Sequence:
MAYSDKVIDHYENPRNVGKLDAQDPDVGTGMVGAPACGDVMRLQIKVNEQGIIEDAKFKTYGCGSAIASSSLATEWMKGRTLEEAETIKNTQIAEELALPPVKIHCSVLAEDAIKAAVRDYKHKKGLV
Protein: Carnitine O-acetyltransferase (Carnitine acetylase) (EC 2.3.1.137) (EC 2.3.1.7) (Carnitine acetyltransferase) (CAT) (CrAT) (P43155)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation. Responsible for the synthesis of short- and branched-chain acylcarnitines. Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates.
Subcellular location: Endoplasmic reticulum {ECO:0000305}. Peroxisome {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000305|PubMed:23485643}.; SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome {ECO:0000305|PubMed:23485643}.
Interaction partners:
- Peroxisomal multifunctional enzyme type 2
- Mitochondrial carnitine/acylcarnitine carrier protein
- Vesicular acetylcholine transporter
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal targeting signal 1 receptor
- Sterol carrier protein 2
- Citrate synthase, mitochondrial
Sequence:
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIEYTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNAARLAHYLEKALLDMRALLQSHPRAKL
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (Q9W6N3)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
IQADALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEFNPQHSLLVQFRNLSHNEPHMPHNATFPDSFQQPNSTPFSISPNSPYPPSPASSTYPSSPASSGPSSPFQLPADTPPPAYMPPDDQMGQDNSQSMDTSNTMIPQIMPNISTRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIES
Protein: Fatty acid-binding protein homolog 8 (O02324)
Organism: Caenorhabditis elegans
Function: Lysosomal lipid chaperone which binds to a wide range of unsaturated fatty acids, including high affinity binding to oleic acid and oleoylethanolamide, to transport them into the nucleus. As part of a lysosome-to-nucleus retrograde lipid signaling pathway, translocates into the nucleus where it activates the transcription of genes promoting longevity and activation of mitochondrial beta oxidation.
Subcellular location: Lysosome {ECO:0000269|PubMed:25554789}. Nucleus {ECO:0000269|PubMed:25554789}.
Interaction partners:
- Lipase lipl-4
- Nuclear hormone receptor family member nhr-49
- Nuclear hormone receptor family member nhr-80
- Nose resistant to fluoxetine protein 5
- Fatty acid-binding protein homolog 4
Sequence:
MVSMKEFIGRWKLVHSENFEEYLKEIGVGLLIRKAASLTSPTLEIKLDGDTWHFNQYSTFKNNKLAFKIREKFVEIAPDERSYNTLVTFENGKFISHQDKIKENHHSSVFTTWLENGKLLQTYQSGSVICRREFVKE
Protein: RE33408p (Q7YU43)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESMEYEMARNMTLLFFLERLLDKGEPRTVHDLSCQFGNKEFTKEMRQIAGGSQSGLKKFLAQYPAIFLVDGDYVQVNAYQHHNADDGGCGGKRDYIQEAKDYFKNKMLQYGAAAEVPVRSLLGHRSQASPQVRHISGQHIKEFTDFLMKHTDTFKVTDDYVMLVGCENMTDLPARDRLHLPQSNIDTRGTQQMLDFFAQCIEVKGPLLVDQLFHLLTTNFPQDQWLRMFKTPGDLSSFLKLFADCFHIQANLVTLLQKPKLSDTHIQQAQAQTREQFNALNNNNSASIRKQEPTPGGGGVGGVSSVQQRLQSPALRTNGHTNNNNGSNGSNNNNNNNNSIACPNFKLNAPVSNVMGGQSQGFGQPKSEASSGFDSYVPMSELKLENLCENNYPSANTCYGPINNSSQQTQQVQTQQQQQPQHATQNPAEQRLNSVNQTLKQRINTLVIRTLAENLEKDKQSLANQQGGPISPHASPVHSIANSSSNQNAGSAANNANSNSNANPNNANHSPSHSYFVGDTWKIKVLQNTTVIANVKQSVFVTDIILKYAAKNESIVVSLDCEGINLGLKGEITLIEIGTTRGEAFLFDVQSCPAMVTDGGLKTVLEHDQVIKVIHDCRNDAANLYLQFGILLRNVFDTQAAHAILQYQESGKQVYKAKYISLNSLCEQYNAPCNPIKDQLKQIYRRDQKFWAKRPLTREMMLYAAGDVLVLIHDQLFGNLARQIKPENRALFSELCTEQILMQIKPNEVKIRKKQRKVSTEVSDLKQKLAQTSKSIVLSNREIRLLRYMDLTEDEKERLKGYYKVAKKLEKMESAGNPSKDQSDSEDEQEPNENDAFPSLDSVPSDNSLSGTFSPRFSSEPPSLTESMQMLEEILQNKSMDRIARIDKLEAILTTATSLPCEQIIASNSMQEQLGSSIATTENLQIIREKSKNIKNCNCQGERSVTPIMRTTDKRVVKLVDAESQTLSTGDVVITKIFFQDEHERAKEAALLSNSPAKRVSPT
Protein: Neoxanthin synthase, chloroplastic (EC 5.3.99.9) (Lycopene beta-cyclase) (EC 5.5.1.19) (K4C9E2)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Involved in the synthesis of neoxanthin, the last product of carotenoid synthesis and a precursor of abscisic acid. Involved in the beta-carotene biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:11029576}.
Interaction partners:
- Violaxanthin de-epoxidase
- Zeaxanthin epoxidase, chloroplastic
- 9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic
- 9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic
- Carotenoid cleavage dioxygenase 4
- Carotenoid cleavage dioxygenase 4
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Prolycopene isomerase, chloroplastic
- Zeta-carotene desaturase
- Zeta-carotene desaturase, chloroplastic/chromoplastic
Sequence:
METLLKPFPSLLLSSPTPYRSIVQQNPSFLSPTTKKKSRKCLLRNKSSKLFCSFLDLAPTSKPESLDVNISWVDPNSNRAQFDVIIIGAGPAGLRLAEQVSKYGIKVCCVDPSPLSMWPNNYGVWVDEFENLGLEDCLDHKWPMTCVHINDNKTKYLGRPYGRVSRKKLKLKLLNSCVENRVKFYKAKVWKVEHEEFESSIVCDDGKKIRGSLVVDASGFASDFIEYDRPRNHGYQIAHGVLVEVDNHPFDLDKMVLMDWRDSHLGNEPYLRVNNAKEPTFLYAMPFDRDLVFLEETSLVSRPVLSYMEVKRRMVARLRHLGIKVKSVIEEEKCVIPMGGPLPRIPQNVMAIGGNSGIVHPSTGYMVARSMALAPVLAEAIVEGLGSTRMIRGSQLYHRVWNGLWPLDRRCVRECYSFGMETLLKLDLKGTRRLFDAFFDLDPKYWQGFLSSRLSVKELGLLSLCLFGHGSNMTRLDIVTKCPLPLVRLIGNLAIESL
Protein: GPI inositol deacylase (Q95P05)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MSRLYIFYKLLLFTALLQLTVVCPSIHTAKAEARESKSLGSSDTWGCVLCTAVVATVSQLGQLHQIPAKDALGLFCSFFRSAEAVLCKTASLILLEGALQLIDEGRTPDKVCQIMKYCDTEECILFPPDKNDTLPLHKLRSAYRLDGRKLVDACRTFPTLCRPLFEDSAHDKDGDRFSTYPAKRGTDWRGRDCDDDDARVYPGRNSTDSQRDENCNGIYGVEESSKKTYEELWCSNSSPMGVIAVGDSATADFGIPLGYVSILDLSSEAVANIIPVLDNEIDWPMLSGLTGFANSTRYEPDVDGPMTSVYSKLVELNRCNHRDYQNLGHNGARSGSILSILDSVARNRSESVKPAYVFFSMVGNDVCPRPQDAPTPLDYYHSLSEAVKKADSFLPPGSHVLIVSLVDARAAIGSIVNRIHPIGTLNSDVTYGNLYDYLNCLQVSPCWGWLNSNESVRNETWERASAMNSMISRVVDESTNLENVKVHALGDVIGEVVSSFEGPLWKLVNPVDGFHPSQIATALMGARVFAKMQDLGILPTENPFNGDIQRRFGDQGGY
Protein: Erythroid membrane-associated protein (hERMAP) (Radin blood group antigen) (Scianna blood group antigen) (Q96PL5)
Organism: Homo sapiens (Human)
Function: Possible role as a cell-adhesion or receptor molecule of erythroid cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11783959}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:11783959}.
Interaction partners:
- Xanthine dehydrogenase/oxidase
- Perilipin-2
- Very-long-chain enoyl-CoA reductase
- Lactadherin
Sequence:
MEMASSAGSWLSGCLIPLVFLRLSVHVSGHAGDAGKFHVALLGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGSYRCLIQVGNLSKEDTVILQVAAPSVGSLSPSAVALAVILPVLVLLIMVCLCLIWKQRRAKEKLLYEHVTEVDNLLSDHAKEKGKLHKAVKKLRSELKLKRAAANSGWRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCLHDGGKNTAPLVICSELHKSEESIVPRPEGKGHANGDVSLKVNSSLLPPKAPELKDIILSLPPDLGPALQELKAPSF
Protein: Fructose-bisphosphate aldolase (EC 4.1.2.13) (H3BQN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALVRIGRRWAGCLGGWDSEKSPSHSTPLPA