wanglab/gogpt-training-data huggingface dataset:
Protein: Steroid 17-alpha-hydroxylase/17,20 lyase (EC 1.14.14.19) (EC 1.14.14.32) (17-alpha-hydroxyprogesterone aldolase) (CYPXVII) (Cytochrome P450 17A1) (Cytochrome P450-C17) (Cytochrome P450c17) (P30437)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction.
Subcellular location: Membrane {ECO:0000305}.
Interaction partners:
Sequence:
MAWFLCMCVFSVVGLGLLLLQVKLRRSLETRGGPPSLPVFPLIGSLLSLRSNQAPHVLFQKLQQKYGHTYSLMMGPHTVILVNHHQHAKEVLLKKGKIFAGRPRTVTTDLLTRDGKDIAFADYGATWRFHRKTVHGALCMFGEGSASIEKIICREALSLCDTLRESGSASLDLSPELTRAVTNVVCSLCFSSSYCRGDPEFEAMLQFSQGIVDTVAKDSLVDIFPWLQVFPNADLRLLKQCVSIRDKLLQKKYEEHKSDYSDHEQRDLLDALLRAKRSAENNNTAEITMETVGLSEDHLLMTVGDIFGAGVETTSTVLKWAIAYLIHHPQVQQRIQEELDSVVGGDRTPQLSDRGSLPYLEATIREVLRIRPVAPLLIPHVAQTDTSIGKFTVRKGARIIINLWSLHHDEKEWKNPEMFDPGRFLNEEGTGLCIPSPSYLPFGAGVRVCLGEALAKMEIFLFLSWILQRLTMTVSPGQPLPSLEGKFGVVLQPVKYKVNATPRAGWEKSHLQTS
Protein: Recombination-promoting nuclease RpnD (EC 3.1.21.-) (B7NGZ6)
Organism: Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Function: A low activity DNA endonuclease yielding 3'-hydroxyl ends (Probable). Expression of a repaired protein increases the frequency of recA-independent recombination, but also decreases viability probably via DNA damage as measured by induction of the SOS repair response; in a RecA strain expression has no effect on viability but does induce the SOS repair response. RecA-independent DNA recombination leads to replacement of recipient genes with large segments of donor DNA rather than DNA addition to the donor strain; increased expression of RpnD leads to smaller replacement segments, suggesting this protein may play a role in generating crossover events. Upon expression enhances RecA-independent DNA recombination 4.7-fold, concomitantly reducing viability by 94% and inducing DNA damage. May play a role in horizontal gene transfer.
Interaction partners:
Sequence:
MTNFTTSTPHDALFKTFLTHPDTARDFMEIHLPKDLRELCDLDSLKLESASFVDEKLRALHSDILWSVKTREGDGYIYVVIEHQSREDIHMAFRLMRYSMAVMQRHIEHDKRQPLPLVIPMLFYHGSRSPYPWSLCWLDEFADPTTARKLYNAAFPLVDVTVVPDDEIVQHRRVALLELIQKHIRQRDLMGLIDQLVVLLVTECANDSQITALLNYILLTGDEARFNEFISELTRRMPQHRERIMTIAERIHNDGYIKGEQRILRLLLQNGADPEWIQKITGLSAEQMQALRQPLPERERYSWLKS
Protein: Ergosterol biosynthetic protein 28 homolog (Q9UKR5)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Lathosterol oxidase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Squalene synthase
- Sigma non-opioid intracellular receptor 1
- Lanosterol synthase
- 7-dehydrocholesterol reductase
- Delta
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Sequence:
MSRFLNVLRSWLVMVSIIAMGNTLQSFRDHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKTLYHITLWTFLLALGHFLSELFVYGTAAPTIGVLAPLMVASFSILGMLVGLRYLEVEPVSRQKKRN
Protein: Lysine-specific histone demethylase 1B (EC 1.14.99.66) (Flavin-containing amine oxidase domain-containing protein 1) (Lysine-specific histone demethylase 2) (Q8CIG3)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4.
Subcellular location: Nucleus {ECO:0000269|PubMed:19727073}. Chromosome {ECO:0000250|UniProtKB:Q8NB78}. Note=Found in actively RNAPolII-transcribed gene bodies. {ECO:0000250|UniProtKB:Q8NB78}.
Interaction partners:
- Polycomb group protein ASXL1
- Putative Polycomb group protein ASXL2
- Forkhead box protein K1
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Host cell factor 1
- Cytokine-like nuclear factor N-PAC
- Histone-lysine N-methyltransferase NSD3
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- REST corepressor 2
- Histone H3.2
Sequence:
MAASRGRSKKRSNLELSPDNLPLRSSGRQAKKKAVEIPDEDEDGSSEKKYRKCEKAGCTAAYPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYSAWKRVWTSNGKTEPSPKAFMADQQLPYWVQCTKPECGKWRQLTKEIQLTPHMARTYRCGMKPNTITKPDTPDHCSFPEDLRVLEVSNHWWYPMLIQPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTHRATVTAATTTTGSASPGEMEPSKAAPSSLVLGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLTVAAGQHLLPKHYHNKSVLVVGAGPAGLAAARQLHNFGMKVTVLEAKDRIGGRVWDDKSFKGVVVGRGPQIVNGCINNPVALMCEQLGISMRKLGERCDLIQEGGRITDPTVDKRMDFHFNALLDVVSEWRKDKTLLQDVPLGEKIEEIYRAFVKESGIQFSELEGQVLQFHLSNLEYACGSSLHQVSARSWDHNEFFAQFAGDHTLLTPGYSTIIEKLAEGLDIRLKSPVQSIDYTGDEVQVTTTDGMGHSAQKVLVTVPLAILQRGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASQRGLFAVFYDMDSQQSVLMSVITGEAVASLRTMDDKQVLQQCMGILRELFKEQEIPEPTKYFVTRWSTEPWIQMAYSFVKTFGSGEAYDIIAEEIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
Protein: Glutathione s-transferase kappa 2 (EC 2.5.1.18) (Q18973)
Organism: Caenorhabditis elegans
Function: Has roles in respiratory and lipid metabolism.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19663909}.
Interaction partners:
- Glutathione S-transferase kappa 1
- Glutathione S-transferase omega
- Probable glutathione S-transferase 9
- Putative cuticle collagen 155
- glutathione transferase
- Nematode cuticle collagen N-terminal domain-containing protein
- CaeNaCin
- Glutathione S-transferase omega
- Probable glutathione S-transferase 6
- Probable glutathione transferase omega-2
Sequence:
MPNRKVVKFFFDVISPYSYFGFEGITRHRSVWKTPIQMKPFFFAGVVRHTENPGLPLRIPIKEKYMHKDLLFSAQYWGIPFRLPKDYTNMMLNTSSIVPQRILVASQLRDNVLMEDVARGLWHRFYAYGKPIFTKSQVAEVLRDLHVKDVDELVMMSDSAEVKNILRENTDEAIGNGCFGAPWMHITDGHGKVLQTVFGSDRLPQVADFLAEPFKGPMREKKPNA
Protein: PH domain-containing protein (Q551S0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Protein tipD
- Cytosolic purine 5'-nucleotidase
- Intermembrane lipid transfer protein tipC
Sequence:
MSLSSSVSISPSISSSSISNNRNSRDLEDKYGDSVVFPCPSKFEKIIPLDERYITHATFLKNKSSETTFIGLLTSNRFYKVDSDTLKKIWSIDLFDMHSIEGDESPDPKTLRIVYHVKQTPSLVGGLVSGGGGSNGNHNGGGGFDNNNNPEMSPPDSPTIQSRLSSSSSKRGSSSSSSSSSGGGGGGGGGGGGGSGGGSGSGGISNDNYISEKIFITESEEIRDQWLVSLRLLTRQTFQKYFESTFIPAPAIYQLHIYAYKTNRKGKNQIRCILVSTERCYNISIKTPSLEIGKVKWSFPIAALKTLQVFKSAPNILVLTLDNKENSKVKEVQQFILKDLIERNLLTNELRRIYAKLTKQSLTKDEKDELPKKFGKGK
Protein: Hyaluronan mediated motility receptor (Intracellular hyaluronic acid-binding protein) (Receptor for hyaluronan-mediated motility) (CD antigen CD168) (O75330)
Organism: Homo sapiens (Human)
Function: Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenisis (By similarity).
Subcellular location: Cell surface {ECO:0000250|UniProtKB:Q00547}. Cytoplasm {ECO:0000269|PubMed:31429579}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00547}.
Interaction partners:
- Disks large-associated protein 5
- CD44 antigen
- Targeting protein for Xklp2
- Aurora kinase A
- Breast cancer type 1 susceptibility protein
- Protein FAM83D
- G2/mitotic-specific cyclin-B1
- Cyclin-dependent kinase 1
- Breast cancer type 2 susceptibility protein
- Abnormal spindle-like microcephaly-associated protein
Sequence:
MSFPKAPLKRFNDPSGCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQKESKQNLNVDKDTTLPASARKVKSSESKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEGNTNCYRAPMECQESWK
Protein: At4g00080 (F6N15.9 protein) (Plant invertase/pectin methylesterase inhibitor superfamily protein) (O81309)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative methylesterase 13, chloroplastic
- Protein PHLOEM PROTEIN 2-LIKE A6
- Bnm1 like protein
- At3g20340
- At5g46950
- RPW8-like protein 2
- HVA22-like protein b
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- CLAVATA3/ESR
- Late embryogenesis abundant protein M17
Sequence:
MAANNKLFFVLLSLFPLIIFSATATSSKDYDTKAYVHSWCRTTLYPKLCVRSMSRYVRSRAVQNPRDLARFALKASLYRAKYTKAFLLKEVKNLETTLRPQYYASVHDCLDQIRDSVNQLSLAIAELDRVSRRQGKSQGDLHWHINNLQTWTSTALTDAETCVSQFPGRRMSKLKATIKGKVKNVEETTSNALAFIEHYAAARYRARRP
Protein: Prion-like protein doppel (PrPLP) (Prion protein 2) (Q9UKY0)
Organism: Homo sapiens (Human)
Function: Required for normal acrosome reaction and for normal male fertility (By similarity). Can bind Cu(2+).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12200435, ECO:0000269|PubMed:15218028}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12200435}.
Interaction partners:
- Major prion protein
- Shadow of prion protein
- Tribbles homolog 3
Sequence:
MRKHLSWWWLATVCMLLFSHLSAVQTRGIKHRIKWNRKALPSTAQITEAQVAENRPGAFIKQGRKLDIDFGAEGNRYYEANYWQFPDGIHYNGCSEANVTKEAFVTGCINATQAANQGEFQKPDNKLHQQVLWRLVQELCSLKHCEFWLERGAGLRVTMHQPVLLCLLALIWLTVK
Protein: Metabotropic glutamate receptor 8 (mGluR8) (O00222)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Metabotropic glutamate receptor 4
- Metabotropic glutamate receptor 7
- Guanine nucleotide-binding protein G
- Adhesion G protein-coupled receptor B3
Sequence:
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHSI
Protein: Rab-GAP TBC domain-containing protein (Q6Q4F1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVGKVLGIKDLEQFSSRRTSVYLDPECDKFFELPLFIAASSNDITTKCQCFQFSPGKEPALRSYTEIQQLLQQGKKRDVKNILRENSWPINSPIRAQLWPMLCGQHQTKQQMLDGFYWEMVHQVFGTTELSEKPIMLPAFVDATHCLPYHLTSTGRAVADRIVNVLGYDCPDITYSPVMYPITSILLHFMSEEEAYICLAGLVGSKEKVFINQTKLQHEVTWKTVMQIAKKHTKSATSYFQRICPGLKLERIFMDWCWWILAGLPFQHL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F6U4U2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPESHFVAQAGMQWCDHSSM
Protein: Multiple inositol polyphosphate phosphatase 1 (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Q9UNW1)
Organism: Homo sapiens (Human)
Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity). Through the regulation of intracellular inositol polyphosphates, may control intracellular cation homeostasis, including that of calcium and iron, hence affecting free cation availability required for neural cell signaling.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O35217}. Secreted {ECO:0000269|PubMed:33257696}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol-tetrakisphosphate 1-kinase
- Inositol polyphosphate-5-phosphatase A
- Bisphosphoglycerate mutase
- Inositol-trisphosphate 3-kinase C
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase A
- Inositol polyphosphate 5-phosphatase K
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Enolase 4
Sequence:
MLRAPGCLLRTSVAPAAALAAALLSSLARCSLLEPRDPVASSLSPYFGTKTRYEDVNPVLLSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGASSTGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLITSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVEKNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKVLEYLNDLKQYWKRGYGYTINSRSSCTLFQDIFQHLDKAVEQKQRSQPISSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNYKKQMHRKFRSGLIVPYASNLIFVLYHCENAKTPKEQFRVQMLLNEKVLPLAYSQETVSFYEDLKNHYKDILQSCQTSEECELARANSTSDEL
Protein: Chromosome 19 open reading frame 2 (cDNA FLJ10575 fis, clone NT2RP2003295, highly similar to RNA polymerase II subunit 5-mediating protein) (Q6NX55)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MWRGCARSRKRKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSDAAGDIVDIREEIKCDFEFKAKHRIAHKPHSKPKTSDIFEADIANDVKSKDLLADKELWARLEELERQEELLGELDSKPDTVIANGEDTTSSEEEKEDRNTNVNAMHQVTDSHTPCHKDVASSEPFSGQVNSQLNCSVNGSSSYHSDDDDDDDDDDDDNIDDDDGDNDHEALGVGDNSIPTIYFSHTVEPKRVRINTGKNTTLKFSEKKEEAKRKRKNSTGSGHSAQELPTIRTPADIYRAFVDVVNGEYVPRKSILKSRSRENSVCSDTSESSAAEFDDRRGVLRSISCEEATCSDTSESILEEEPQENQKKLLPLSVTPEAFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEASEETGKRVSKFKAARLQQKD
Protein: Secretory component protein SHR3 (Q02774)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in amino acid permease processing and required for the efficient translocation of structurally related amino acid permeases from the endoplasmic reticulum to the plasma membrane. SHR3 may function as a permease-specific 'adaptor' molecule that functions in conjunction with the SEC62/SEC63 complex. Yeast cells may require SHR3 to expedite the processing of permeases to ensure their rapid expression at the plasma membrane in response to changing environmental conditions.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- General amino-acid permease GAP1
- Histidine permease
- Protein SSH4
- 3-ketoacyl-CoA thiolase, peroxisomal
- Glucose-signaling factor 2
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
- Acetyl-CoA acetyltransferase
- Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2
- Probable electron transfer flavoprotein subunit beta
- Acyl-CoA-binding protein
Sequence:
MFSYSDFCSIGTAMILSATTFLMGVFFSNMPYDYHLLFNPNSTQEHFDLALRHYQILHETPLPVIVTLCVVAGIGLVGGTIKVFKPNPELQMFEYCSLGLYVLAICVFLTNVKTGIDCSVSHNWGEVTENQGLAVIASSNIILLVMFAGVIILQIGLWYSNWDLQKRLKEFYAQEEREAANAGKKTEKVDNAKKNDNKSKGAQKRKNAKK
Protein: Asnovolin H dehydrogenase nvfC (EC 1.1.99.-) (Novofumigatonin biosynthesis cluster protein C) (Short chain dehydrogenase nvfC) (A0A2I1BSW8)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSLHDYVLIITGSASGIGLATATIALDEGARVLGVDISSPPRSLIDHSNFKFVEGNLSLEPTPRRVVEACVKAFGGRIDGLLNIAGVMDLNQSVDSLSDTMWESCIAINLTAPVKLMREVIPIMRQQKSGSIVNVASKAALSGAVSGVAYTASKHGLVGATKNVAWRFKQENIRCNAVCPGAVDGTSIHRGLETSQFDSEALGTMSLIHEAHMRDRERGIHIQPEDIARSLLFLVSSRSNGINGAIIPIDNAWSTI
Protein: Cytosolic iron-sulfur assembly component 2A (MIP18 family protein FAM96A) (Q9H5X1)
Organism: Homo sapiens (Human)
Function: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component and in collaboration with CIAO1 specifically matures ACO1 and stabilizes IREB2, connecting cytosolic iron-sulfur protein maturation with cellular iron regulation. May play a role in chromosome segregation through establishment of sister chromatid cohesion. May induce apoptosis in collaboration with APAF1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22683786}.
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- MMS19 nucleotide excision repair protein homolog
- Cytosolic iron-sulfur assembly component 3
- Cytosolic iron-sulfur assembly component 2B
- Iron-responsive element-binding protein 2
- Cytosolic Fe-S cluster assembly factor NUBP1
Sequence:
MQRVSGLLSWTLSRVLWLSGLSEPGAARQPRIMEEKALEVYDLIRTIRDPEKPNTLEELEVVSESCVEVQEINEEEYLVIIRFTPTVPHCSLATLIGLCLRVKLQRCLPFKHKLEIYISEGTHSTEEDINKQINDKERVAAAMENPNLREIVEQCVLEPD
Protein: Hemoglobin subunit alpha-D (Alpha-D-globin) (Hemoglobin alpha-D chain) (P84791)
Organism: Aythya fuligula (Tufted duck) (Anas fuligula)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
Sequence:
MLTAEDKKLITQLWEKVAGHQDDFGNEALQRMFVTYPQTKTYFPHFDLHPGSEQVRGHGKKVAAALGNAVKSLDNISQALSELSNLHAYNLRVDPVNFKLLAQCFQVVLAAHLGKDYTPDMHAAFDKFLSAVAAVLAEKYR
Protein: Annexin A4 (35-beta calcimedin) (Annexin IV) (Annexin-4) (Carbohydrate-binding protein p33/p41) (Chromobindin-4) (Endonexin I) (Lipocortin IV) (P32.5) (PP4-X) (Placental anticoagulant protein II) (PAP-II) (Protein II) (P13214)
Organism: Bos taurus (Bovine)
Function: May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A).
Subcellular location: Zymogen granule membrane {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein {ECO:0000250|UniProtKB:P50994}.
Interaction partners:
- CD63 antigen
Sequence:
MAAKGGTVKAASGFNAAEDAQTLRKAMKGLGTDEDAIINVLAYRSTAQRQEIRTAYKTTIGRDLMDDLKSELSGNFEQVILGMMTPTVLYDVQELRKAMKGAGTDEGCLIEILASRTPEEIRRINQTYQLQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDESNYLDDALMRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRIAQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAERLYKSMKGLGTDDDTLIRVMVSRAEIDMLDIRANFKRLYGKSLYSFIKGDTSGDYRKVLLILCGGDD
Protein: Dromyosuppressin (TDVDHVFLRFamide) (P61849)
Organism: Drosophila melanogaster (Fruit fly)
Function: Myoinhibiting neuropeptide.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MSFAQFFVACCLAIVLLAVSNTRAAVQGPPLCQSGIVEEMPPHIRKVCQALENSDQLTSALKSYINNEASALVANSDDLLKNYNKRTDVDHVFLRFGKRR
Protein: LD29371p (Q86PA6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATSDDEPMHLYEVFQNCFNKIANKQPTGTVGADRGGGGGYHSPYGSLGVENGMYPSDFNSMHDTVNGGNNRYANASTVDQYFDSAAAGSGGAWCQPQMSSANSYMGQSAYQNSGPLSGHSIDQQQQQVHQADGLGMGGGGGGGVGADGMHCPVTTGLPPISSFRPTSGGIGGPGAGQQAPVNVNVNPPAVFNSPQAHNHNHTVQAQHSALSTAGPLGHHSLNHTPHAHSHTLPLPHALPHGHTLPHPHHSQQNSPAVQSSDAFSGAGASVKVAGAGNSSAAALRQQMYMPADQSISSFGSNPSTPVNSPPPLTQSVVGGGGEPSVSGGSGWGHSVLNGGPSSSYASEMVPVSSLHTMASVFQGVRMEERLDDALNVLRNHCEPEMLAGVNQSLASIDNIDALTSFVPNSPSHLGSGGNSGSVSNTSNAALVHEVLALGAAAAAGTSGQSVGGAGSLASLKLDRSASTSLPKQTKKRKEHTAISNSVPAGVSTTSSLTSLDISDTKPTSSIESSNSGLQQHSQGKGTKRPRRYCSSADEDDDAEPAVKAIREKERRQANNARERIRIRDINEALKELGRMCMTHLKSDKPQTKLGILNMAVEVIMTLEQQVRERNLNPKAACLKRREEEKAEDGPKLSAQHHMIPQPQQVGGTPGSSYHSQPAQLVPPSSPASATGAAIIADHQHHDHIPTRQPGQQRPATPLAAAAAATITARTRPASAIACTTQEPLLEIVVVPLFHKNRMY