wanglab/gogpt-training-data huggingface dataset:
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (EC 3.6.4.-) (Q9VMX6)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- GEO08380p1
- Replication protein A 70 kDa DNA-binding subunit
- CG9273 protein
Sequence:
MSTCSSSEIAEKKRIALAKLQAKKSQLLASAPATNGKSTTSATGATQHANNGKSNPNQPQAKSPLNFYRSPTGEQKKINRSGPTPGDNKSSSFLNALKAIKQTSNRELSRGAAHPYQRPNGGNERNKPTLSLSSDKEKPVAVLLGNSITCNLYLISTHRFAAQTSGYHEQLVTVFKNMPTKCYDGQTRIWSFDLSDYQSLKTHAADLKPYVHMNGIPKKVLDLCGQPPVVPERSVLASIEPKLADQLMPFQQDGVCFAIAQKGRIMICDEMGLGKTYQALAVADYFKDDWPLLVCTTASTRDSWAKHIMDLLPKVPIHYVQVLNNNQLYVGEAKVLITSYNMMERHEDKLMQRKFGFIIFDESHTLKNSKAKCTTTAKRLTDQAKRVVLLSGTPALSRPLELFTQLQMIDGKFMNFMEFTTRYCDGKQSTFGWDANGQSNLEELKVILHLKYMLRRTKVEVLPQLAEKNRETVVLDPALVWTNAETKETLDAFNKELKTAKGRATEEILLRFYARTAEVKTRAVCAYLKTLVKEQKKFIIFAHHRVMMDAISDFLSGLKVHYIRIDGQTRSDHRSDSVDTFQKKSSCKVALLSLKACNSGITLTAAEIIVFAELDWNPSTLAQAESRAHRIGQTKPVICRYLIAHNTADDIIWNMLKNKQEVLSKVGIFAENLQKATHTAAPTSSHKIEEYFSPSTSTSLEPERNSIKQYFSTIPAKEPPEQNNNTEMTKVNKAESDIAAFFNDDDDEAFLELDI
Protein: ATP binding cassette subfamily A member 1 (A0A8I6ATT1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVSRLFSDAQRILLYSQKDTSIRDMHKVLRTLQQIKHPNSNLKLQDFLVDNETFSGFLQHSLSLPRSAVDNLLQADVSLQKVFLQGYQLHLASLCNGSKLEEIIRLGDLEVSALCSLPREKLDAAERELRSNMDILKPVMTKLNSTSLLPTQHLAEATTTLLDSLGGLAQELFSTKSWSDMRQEVMFLTNVNNSGSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDTDTFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLIGKILYTPDTPATRQVMAEVNKTFQELALFHDLEGMWEELSPQIWTFMESSQEMDLVRTMLDSRGNDQFWERKLDGLDWTAQDIMAFLAKNPEDVQSPNGSVYTWREAFNETNQAIQTISRFMECVNLNKLEPIPTEVRLINKSMELLDERKFWAGIVFTGITPDSVELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYVQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKSIVYEKEARLKETMRIMGLDNGILWFSWFISSLIPLLVSAGLLVIILKLGDLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRTNLAAACGGIIYFTLYLPYVLCVAWQDYVGFSIKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFKSPVEEDGFNLTTSVSMMLFDTFIYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEEIDEKSHPGSSQKGASEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMNSIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSCLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLHPFTEDDAVDPNDSDLDPESRETDLLSGMDGKGSYQLKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPNLELQPWMYNEQYTFVSNDAPEDMGTQELLNALTKDPGFGTRCMEGNPIPNTPCLVGEEDWTTGPVPQTLMDLFQNGNWTMKNPSPSCQCSSDKIKKMLPVCPPGAGGLPPPQRKQKTADILQNLTGRNISDYLVKTYVQIIAKRYGGFSLGVSDSQALPPSQEVNNAIKQMKKLLKLTKDSSADRFLSSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSQYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFICGVKPVIYWLSNFVWDMCNYVVPATLVVIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTNNKFNDINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLVTVLIQYRFFIRPRPVKARLPPLNDEDEDVRRERQRILEGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKTSTFKMLTGDTAVTRGDALLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHLEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYASNYSGGNKRKLSTAIALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQEFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
Protein: Dolichol-phosphate mannosyltransferase subunit 3 (DPM synthase complex subunit 3) (Dolichol-phosphate mannose synthase subunit 3) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 3) (Mannose-P-dolichol synthase subunit 3) (MPD synthase subunit 3) (O94633)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stabilizer subunit of the dolichol-phosphate-mannose synthase complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol kinase sec59
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GPI mannosyltransferase 2
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dol-P-Man:Man
- Mannose-1-phosphate guanyltransferase
- GPI mannosyltransferase 3
Sequence:
MQRIHKVILYYVSLTILYRVTYLFDLEEPWSTLRPYTPYLFILAFGSYLGITLLYNVATTNDKPEAYVDLVKDIKEAQDALRSKGMTIED
Protein: acid phosphatase (EC 3.1.3.2) (Q9VAD0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWNHPSQRWLILICVICLLSFALANSLHGYANAEGHPVEISATLPGQLKFVHVIYRHGDRTPVDPYPTDPWGDRKFWPTGWGDLTNLGKQEHYDLGKWLRNRYSNLLPPIYSNENIYVQSTDVDRTLMSAQSNLAGLYEPQGEDIWNTDINWQPIPIHTSPEREDPILAAKAPCPAYDYELASLESSPEFKALTEKHRNLFAYLSEKGGRPVKTFIDAQYLNNTLFIENLYNMTLPKWTKMVYGREELTYVSNFAFAISSYTRKLARLKAGPLLKDIFQRFKEKSSGSLKPDRSMWVYSAHDTTVASVLNALKLFELHSPPYTACIMMELRVDETNTPLVSIFYKNTTAEPLPLDIPGCGPSCPLTKLMNIYEDVLPVDWERECKLSTMMMTYEEANLGTATGILILIVIALLFASYGLMIYYRRRNYKLYSSYSQMA
Protein: Sugar transporter ERD6-like 14 (Q8GXK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar transporter.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- ABC transporter G family member 10
Sequence:
MAEESLLPSHTEDVSASPNKSSSLLSEISNASTRPFVLAFTVGSCGALSFGCIVGYTAPTQSSIMKDLNLSIADFSFFGSILTVGLILGALICGKLADLVGRVYTIWITNILVLIGWLAIAFAKDVRLLDLGRLLQGISVGISSYLGPIYISELAPRNLRGAASSLMQLFVGVGLSAFYALGTAVAWRSLAILGSIPSLVVLPLLFFIPESPRWLAKVGREKEVEGVLLSLRGAKSDVSDEAATILEYTKHVEQQDIDSRGFFKLFQRKYALPLTIGVVLISMPQLGGLNGYTFYTDTIFTSTGVSSDIGFILTSIVQMTGGVLGVLLVDISGRRSLLLFSQAGMFLGCLATAISFFLQKNNCWETGTPIMALISVMVYFGSYGLGMGPIPWIIASEIYPVDVKGAAGTVCNLVTSISSWLVTYSFNFLLQWSSTGTFMMFATVMGLGFVFTAKLVPETKGKSLEEIQSAFTDSTSEDSTIF
Protein: Trafficking kinesin protein 1 (A0A8I6AI05)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
LDATALHDDTSASSVPLSEACNHAVLACSPGIPEEHYVSEAIEDAPSYRGHRDACTITDVCNSTNLPEVEIISLLEEQLPHYKLRADTIYGYDHDDWLHTPLISPDANIDLTTEQIEETLKYFLLCAERVGQMTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLGLFPMDSLAAEIEGTMRKELQLEEPESPDITHQKRVFETVRNVNQVVKQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSHVVLDNKTNSILLETEAADLGNEEHNKKPGTPGTPGSHDLETALRRLSLRRENYLSERRFFEEEQERKLRELAEKGELHSGSLTPTESIMSLGTHSRFSEFTGFSGMSFSSRSYLPEKLQIVKPLEGSATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVYCLNDFEEDDTGDHISLAGLATSTTIQHMETSAHHPGKCMSQTNSTFTFTTCRILHPSDELTRVTPSLNSAPAPSCSSTSHLKSTPVATPCTPRRLSLAESFTNVRESTTTMSTSLGLVWLLKERGISAAVYDPQSWDRAGRGSLLHSYTPRMAVIPSTPPNSPMQTPSASPPSFEFKCTSPPYNNFLASKPASSILREVREKKHVRSSESQTDVSVSNLNLVDKVRRFGVARVVNSGRAHIPTLTEDQGPLLCGPTGPAHALVPGGLVPEGLPLGCPSGIRRNRSFPTMVGSSVQMRAPVILTSGILMGAKLPKQTSLR
Protein: Cytokine induced apoptosis inhibitor 1 (H3BT65)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMHLWPCRRTGKREVKGTDELPTQVSLWKLLPGRCLPLCQLPLPWDASLQTWGKGASE
Protein: Endo-beta-N-acetylglucosaminidase (EC 3.2.1.96) (Endoglycosidase BI-1) (EndoBI-1) (B7GPC7)
Organism: Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Function: Endoglycosidase with broad specificity that cleaves the chitobiose core of high mannose and complex N-linked glycans. Is able to release N-glycans from diverse host glycoproteins such as human and bovine lactoferrin, immunoglobulins A and G, and ribonuclease B. Is active directly on human breast milk - a complex matrix of lipids, oligosaccharides, and proteins with disparate glycosylation types - successfully removing a significant proportion of the total amount of N-glycans. Does not recognize O-linked glycans or free human milk oligosaccharides (HMO).
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTFIKQMMPRYVASMTAGIVAAAMAATCAFAPVANADAVSPTQETIQSTGRHFMVYYRAWRDVTMKGVNTDLPDDNWISMYDIPYGVDVVNIFSYVPSGQEEQAQPFYDKLKSDYAPYLHSRGIKLVRGIDYTGVAVNGFRTFMKEQNKTESEATEADYDAYAKQVIDKYMISVGLDGLDIDMEAHPNDADVKISDNVIRALSKHIGPKSAKPDTTMFLYDTNGSYLNPFKNVAECFDYVAYQQYGSSSDRTARAAADYQPYIGNEFVPGLTFPEEGDMNNRWYDATEPYEESHFYQVASYVREHNLGGMFVYALDRDGRNYDEDLRRIVPSNLLWTKTAIAESEGMALDTAKTAANHYLDRMSLRQVIDDNAASADKARDMVGKAANLYETNKAVLGGDYGEGFSNTYDPTLEAGLLGIDISVLQQQIDKSSEIIGADTAESDAKTALRMARDAAIDGLTGKIYTADQVSAWSQALKAALDATVPVPTPDSTDQNGNRDKVTNHKVQGQPKQLSATGISTDIIVAVGVTLAIAGVALSLSRKLS
Protein: Eukaryotic translation initiation factor 4E homologous protein, isoform D (A0A0B4JDB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSMEKVANKQYETKNWPDIVDSDDSDVDNQIDVDNLPPLEVGPGENRLQHTYCLWFSRKETQRAAADYSKSLHMVGRCASVQQWWSLYSHLIRPTALKPYRELLLFKQGIIPMWEDPANSKGGQWLIRLRKNKVDRAWENVCMAMLGEQFLVGDEICGVVLQTKYPEDSLSVWHRTATDMTSTTRIRDTLRRILNIPLTTALEYKIHCDSLKYVSMPRRQNHKLGNLFYRNRYGFNSRYGKS
Protein: Tubulin alpha-4A chain (EC 3.6.5.-) (Alpha-tubulin 4) (Alpha-tubulin isotype M-alpha-4) (Tubulin alpha-4 chain) (P68368)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-4A chain
- Tubulin beta-4B chain
- Tubulin beta-2A chain
- Tubulin beta-5 chain
- Microtubule-associated protein
- Tubulin beta-6 chain
- Tubulin beta-3 chain
- Tubulin beta-1 chain
- Tubulin beta-2B chain
- Cell division control protein 42 homolog
Sequence:
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE
Protein: Inositol transporter 4 (Myo-inositol-proton symporter INT4) (Protein INOSITOL TRANSPORTER 4) (O23492)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plasma membrane inositol-proton symporter. Mediates high-affinity myoinositol-proton symport across the plasma membrane. Active with myoinositol, scylloinositol and D-chiroinositol. Low activity with mucoinositol and alloinositol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16603666, ECO:0000269|PubMed:22253225}; Multi-pass membrane protein {ECO:0000269|PubMed:16603666, ECO:0000269|PubMed:22253225}.
Interaction partners:
- Acid phosphatase/vanadium-dependent haloperoxidase-related protein
- Embryo defective 2739
- Uncharacterized protein At5g65660
- Protein SIEL
- Integrator complex subunit
- Cysteine-rich receptor-like protein kinase 18
- Cation/H
- Inositol diphosphatase DSP2
- Probable inactive purple acid phosphatase 2
- Cleavage and polyadenylation specificity factor subunit 3-I
Sequence:
MVEGGIAKADKTEFTECWRTTWKTPYIMRLALSAGIGGLLFGYDTGVISGALLFIKEDFDEVDKKTWLQSTIVSMAVAGAIVGAAVGGWINDKFGRRMSILIADVLFLIGAIVMAFAPAPWVIIVGRIFVGFGVGMASMTSPLYISEASPARIRGALVSTNGLLITGGQFFSYLINLAFVHTPGTWRWMLGVAGVPAIVQFVLMLSLPESPRWLYRKDRIAESRAILERIYPADEVEAEMEALKLSVEAEKADEAIIGDSFSAKLKGAFGNPVVRRGLAAGITVQVAQQFVGINTVMYYSPSIVQFAGYASNKTAMALSLITSGLNALGSIVSMMFVDRYGRRKLMIISMFGIIACLIILATVFSQAAIHAPKIDAFESRTFAPNATCSAYAPLAAENAPPSRWNCMKCLRSECGFCASGVQPYAPGACVVLSDDMKATCSSRGRTFFKDGCPSKFGFLAIVFLGLYIVVYAPGMGTVPWIVNSEIYPLRYRGLGGGIAAVSNWVSNLIVSESFLSLTHALGSSGTFLLFAGFSTIGLFFIWLLVPETKGLQFEEVEKLLEVGFKPSLLRRREKKGKEVDAA
Protein: Golgi resident protein GCP60 (Acyl-CoA-binding domain-containing protein 3) (DMT1-associated protein) (DAP) (Golgi complex-associated protein 1) (GOCAP1) (Golgi phosphoprotein 1) (GOLPH1) (Q7TNY6)
Organism: Rattus norvegicus (Rat)
Function: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells. Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H3P7}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also mitochondrial (via its interaction with PBR). {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Translocator protein
- Golgin B1
- Golgin-45
- Non-selective voltage-gated ion channel VDAC1
- Acyl-CoA-binding protein
- Natural resistance-associated macrophage protein 2
- TBC1 domain family, member 22a
- Steroidogenic acute regulatory protein, mitochondrial
Sequence:
MAAQLNVEQLEVSLDGLTLSPDSEERPGAEGAPLQTPPSSPPRDGLGSGTAGQQREPGEAAAEGAAEEARRMEQHWGFGLEELYGLALRFYKIKDGKAFHPTYEEKLKFVALHKQVLLGPYNPDTSPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNKCCPLLSAYVASHRIEKEEEEKRRKAEEERRQREEEERERLQKEEEKRKREEEDRLRREEEERRRIEEERLRLEQQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQQAALQKQQEVVVAGASLPASTKVNTAGASDPLPVNGQAKTHTENPEKVLEPEAAEEALENGPKDSLPVIAAPSMWTRPQIKDFKEKIRQDADSVITVRRGEVVTVRVPTHEEGSYLFWEFATDSYDIGFGVYFEWTDSPNAAVSVHVSESSDDEEEEEEENVTCEEKAKKNVNKPLLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYTR
Protein: BCL6 corepressor like 1 (H7C4B2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPVLTPVHTSSKALLSTVLSRSQRTTQAAGGNVTSCLGSTSSPFVIFPEIVRNGDPSTWVKNSTALISTIPGTYVGVANPVPASLLLNKDPNLGLNRDPRHLPKQEPISIIDQGEPKGTGATCGKKGSQAGAEGQPSTVKRYTPARIAPGLPGCQTKELSLWKPTGPANIYPRCSVNGKPTSTQVLPVGWSPYHQASLLSIGISSAGQLTPSQGAPIRPTSVVSEFSGVPSLSSSEAVHGLPEGQPRPGGSFVPEQDPVTKNKTCRIAAKPYEEQVNPVLLTLSPQTGTLALSVQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLAGDTKPKNQVLATYMSHELVLATPQNLPKMPELPLLPHDSHPKELILDVVPSSRRGSSTERPQLGSQVDLGRVKMEKVDGDVVFNLATCFRADGLPVAPQRGQAEVRAKAGQARVKQESVGVFACKNKWQPDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSDLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAK
Protein: Growth hormone (H6UQ63)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPHETVATFPTMPLSNMFANAVLRAQHLHLLAAETYKEFERTYIPEDQWYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMEVVRFSLVFIQSWLTPVQYLSKVFTNKLVFGTSDRVFEKLKDLEEGIQALMRELEDRSPRGPQLLRPTYDKFDIHLRHGDALLNNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: Large ribosomal subunit protein bL17 (50S ribosomal protein L17) (O51456)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein bL33
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL25
- Large ribosomal subunit protein bL36
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL5
Sequence:
MKTKLGFNRLSRKSSHRRALLKNMVISFFKHEKISSTKTKLFEVKRFAERLITRAKVDTVHNRRELSKFIHDKHILNKLFTKISPVFRQRSGGYTRMIKLGKRYGDAAEMAILELVEKPLKVE
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q6IPK9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LTPCPVQTPRLGKALIHCWTDPGQPLGEQQRVRRQRTETSEPTMRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHVKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL
Protein: Polyadenylate-binding protein (PABP) (Q38DU2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Probable eukaryotic initiation factor 4A
- Pab1p-dependent poly
- Eukaryotic translation initiation factor 4E, putative
- Nuclear cap-binding protein subunit 2
- Regulator of nonsense transcripts 1, putative
- PAB1-binding protein 1
- Eukaryotic release factor 3, putative
Sequence:
MAAFAAASPSIWVGGLDPNLNEQKLYDHFVRVGPVASVRVCVDSVTQKSLGYGYVNFQNPADAEKALDQAGVKLGTKHIRIAKIQRDPSKRRSGVTNIIVKKLPPTVDTYALKEMFSKYGRLTAIGLATDEKGESRGYARISYEKEESAVDAVRELNGVSIDDCAITVERYQPHHREEQLKQYTNLYVKNLDPSVDDEKLKEVFSPFGEVTSAKVRDLAGRPTVGFGYVAYATHEAAAKAVEELDDKESPLAKEGMKLSVCRFRSREERKRERERLRRERQQQHSKYPNLYVKNFDDTVTSERLKALFDPFGETVSVSVMMDKATKVSRCFGFVSFKEQSSAAQAIQELHGSTALGPRPLFVSYALRKDARRQTLEDMRNKQPRMRQPPMGGLMGGMMGPQLSFMNPPAMFNGMHFMNTRMPMMPSTMGMGGPMRPMGPTPMNQVRARPGPQRPPMQSMMAPQQQSHPQIPQPPVAQGQNLSTVLASMTPDQQKNVLGERLYNYIVRNNPSFAAKVTGMLLEMDNSEILNLLDNHSLLDTKVQEALDVLNRHIGM
Protein: Cholesterol 24-hydroxylase (CH24H) (EC 1.14.14.25) (Cholesterol 24-monooxygenase) (Cholesterol 24S-hydroxylase) (Cytochrome P450 46A1) (Q9Y6A2)
Organism: Homo sapiens (Human)
Function: P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning (By similarity). Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain. May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WVK8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WVK8}. Microsome membrane {ECO:0000250|UniProtKB:Q9WVK8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WVK8}. Postsynapse {ECO:0000250|UniProtKB:Q9WVK8}. Presynapse {ECO:0000250|UniProtKB:Q9WVK8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WVK8}.
Interaction partners:
- 24-hydroxycholesterol 7-alpha-hydroxylase
- Cytochrome P450 7A1
- Cholesterol 25-hydroxylase
- Sterol 26-hydroxylase, mitochondrial
- NADPH--cytochrome P450 reductase
- 7-dehydrocholesterol reductase
- Delta
- Sterol O-acyltransferase 1
- Lysosomal acid lipase/cholesteryl ester hydrolase
- Sterol O-acyltransferase 2
Sequence:
MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC
Protein: Sulfotransferase 1C1 (ST1C1) (EC 2.8.2.-) (Phenol sulfotransferase) (Q80VR3)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hydroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). Also shows activity towards cinnamyl alcohol at pH 6.4 but not at pH 5.5, and towards a number of phenolic odorants including eugenol, guaiacol and 2-naphthol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8641270}.
Interaction partners:
Sequence:
MPLEKLKDLHLDEQNMQPETREVNGILMSKMMSENWDKIWNFQAKPDDLLIATYAKAGTTWTQEIVDMIQNDGDVQKCQRANTYDRHPFIEWTLPPPLNSGLDLANKMPSPRTLKTHLPVQMLPPSFWKENSKIIYVARNAKDCLVSYYYFSRMNKMLPDPGTLGEYIETFKAGKVLWGSWYDHVKGWWDVKDKHRILYLFYEDMKEDPKREIKKIVKFLEKDISEEVLNKIIHHTSFDVMKQNPMANYTTLPSSIMDHSISPFMRKGMPGDWKNYFTVAQSEDFDEDYRKKMAGSTITFRTEI
Protein: Par-1, isoform S (EC 2.7.11.-, EC 2.7.11.26) (E1JGM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTAMRTTLQSVPEALPADSVSNGTASNVAAPAAPVSSATNAVPPLAAVSSTTATYATNSISTSSHSVKDQQQQQQQQQHDSANANIVSLPPTTTPVANTNTMMPIVTSSNSATSNSTAATPTPASGAAATGGVGSVSQGPATVSASAANTNHSHQHSHQHHHHVANNMTTDGARLSSNNSAVVASSAINHHHHHTPGSGVAPTVNKNVLSTHSAHPSAIKQRTSSAKGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETKMASAVKSSRHFPRNVPSRSTFHSGQTRARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPNQ
Protein: 17-beta-hydroxysteroid dehydrogenase 13 (17-beta-HSD 13) (EC 1.1.1.-) (EC 1.1.1.62) (Alcohol dehydrogenase PAN1B-like) (Hepatic retinol/retinal dehydrogenase) (EC 1.1.1.105) (Short-chain dehydrogenase/reductase 9) (Q8VCR2)
Organism: Mus musculus (Mouse)
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:Q7Z5P4}. Endoplasmic reticulum {ECO:0000305|PubMed:18359291}. Lipid droplet {ECO:0000269|PubMed:18359291}. Note=Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation. {ECO:0000269|PubMed:18359291}.
Interaction partners:
- Transmembrane 6 superfamily member 2
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
Sequence:
MNLILEFLLLVGVIIYSYLESLVKFFIPRRRKSVTGQTVLITGAGHGIGRLTAYEFAKQKSRLVLWDINKRGVEETADKCRKLGAVVHVFVVDCSNRAEIYNSVDQVKREVGDVEIVVNNAGAIYPADLLSAKDEEITKTFEVNILGHFWIIKALLPSMLRRNSGHIVTVASVCGHGVIPYLIPYCSSKFAAVGFHRALTAELDTLGKTGIQTSCLCPVFVNTGFTKNPSTRLWPVLEPEEVARSLINGILTNKKMIFVPSYINISLILEKGPGFSSKHPHGGSQQPVTPIPGDLTPSSDFLKH