wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleotide exchange factor SIL1 (BiP-associated protein) (BAP) (Q9H173)
Organism: Homo sapiens (Human)
Function: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12356756, ECO:0000269|PubMed:16282978}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Hypoxia up-regulated protein 1
- Ubiquitin-like protein FUBI
- DnaJ homolog subfamily B member 9
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
Sequence:
MAPQSLPSSRMAPLGMLLGLLMAACFTFCLSHQNLKEFALTNPEKSSTKETERKETKAEEELDAEVLEVFHPTHEWQALQPGQAVPAGSHVRLNLQTGEREAKLQYEDKFRNNLKGKRLDINTNTYTSQDLKSALAKFKEGAEMESSKEDKARQAEVKRLFRPIEELKKDFDELNVVIETDMQIMVRLINKFNSSSSSLEEKIAALFDLEYYVHQMDNAQDLLSFGGLQVVINGLNSTEPLVKEYAAFVLGAAFSSNPKVQVEAIEGGALQKLLVILATEQPLTAKKKVLFALCSLLRHFPYAQRQFLKLGGLQVLRTLVQEKGTEVLAVRVVTLLYDLVTEKMFAEEEAELTQEMSPEKLQQYRQVHLLPGLWEQGWCEITAHLLALPEHDAREKVLQTLGVLLTTCRDRYRQDPQLGRTLASLQAEYQVLASLELQDGEDEGYFQELLGSVNSLLKELR
Protein: Branched-chain alpha-ketoacid dehydrogenase kinase (BCKDH kinase) (BCKDHKIN) (BDK) (EC 2.7.11.1) ([3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial) (EC 2.7.11.4) (O55028)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.
Subcellular location: Mitochondrion matrix. Mitochondrion {ECO:0000250|UniProtKB:O14874}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Protein phosphatase Mn
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Sequence:
MILTSVLGSGPRSWSSLWPLLGSSLSLRARSTSATDTHHVELARERSKTVTSFYNQSAIDVAAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRINPLFGHLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
Protein: Apoptosis inducing factor BLCAP (Bladder cancer 10 kDa protein) (Bc10) (Bladder cancer-associated protein) (P62952)
Organism: Homo sapiens (Human)
Function: May regulate cell proliferation and coordinate apoptosis and cell cycle progression via a novel mechanism independent of both p53/TP53 and NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19783793, ECO:0000269|PubMed:22969892, ECO:0000269|PubMed:29190807}. Nucleus {ECO:0000269|PubMed:19783793, ECO:0000269|PubMed:29190807}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronatin
Sequence:
MYCLQWLLPVLLIPKPLNPALWFSHSMFMGFYLLSFLLERKPCTICALVFLAALFLICYSCWGNCFLYHCSDSPLPESAHDPGVVGT
Protein: Upstream stimulatory factor 2 (Class B basic helix-loop-helix protein 12) (bHLHb12) (FOS-interacting protein) (FIP) (Major late transcription factor 2) (Upstream transcription factor 2) (Q15853)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.
Subcellular location: Nucleus.
Interaction partners:
- Upstream stimulatory factor 1
- Histone acetyltransferase p300
- Transcription factor Sp1
- Mediator of RNA polymerase II transcription subunit 1
- Breast cancer type 1 susceptibility protein
- A disintegrin and metalloproteinase with thrombospondin motifs 12
Sequence:
MDMLDPGLDPAASATAAAAASHDKGPEAEEGVELQEGGDGPGAEEQTAVAITSVQQAAFGDHNIQYQFRTETNGGQVTYRVVQVTDGQLDGQGDTAGAVSVVSTAAFAGGQQAVTQVGVDGAAQRPGPAAASVPPGPAAPFPLAVIQNPFSNGGSPAAEAVSGEARFAYFPASSVGDTTAVSVQTTDQSLQAGGQFYVMMTPQDVLQTGTQRTIAPRTHPYSPKIDGTRTPRDERRRAQHNEVERRRRDKINNWIVQLSKIIPDCNADNSKTGASKGGILSKACDYIRELRQTNQRMQETFKEAERLQMDNELLRQQIEELKNENALLRAQLQQHNLEMVGEGTRQ
Protein: Protein naked cuticle homolog 2 (Naked-2) (hNkd2) (Q969F2)
Organism: Homo sapiens (Human)
Function: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity (By similarity). Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15064403, ECO:0000269|PubMed:17553928}. Cytoplasm {ECO:0000269|PubMed:15064403, ECO:0000269|PubMed:17553928}. Cytoplasmic vesicle {ECO:0000269|PubMed:15064403, ECO:0000269|PubMed:17553928}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-2
- Protein naked cuticle homolog 1
- Protransforming growth factor alpha
- 14-3-3 protein epsilon
Sequence:
MGKLQSKHAAAARKRRESPEGDSFVASAYASGRKGAEEAERRARDKQELPNGDPKEGPFREDQCPLQVALPAEKAEGREHPGQLLSADDGERAANREGPRGPGGQRLNIDALQCDVSVEEDDRQEWTFTLYDFDNCGKVTREDMSSLMHTIYEVVDASVNHSSGSSKTLRVKLTVSPEPSSKRKEGPPAGQDREPTRCRMEGELAEEPRVADRRLSAHVRRPSTDPQPCSERGPYCVDENTERRNHYLDLAGIENYTSRFGPGSPPVQAKQEPQGRASHLQARSRSQEPDTHAVHHRRSQVLVEHVVPASEPAARALDTQPRPKGPEKQFLKSPKGSGKPPGVPASSKSGKAFSYYLPAVLPPQAPQDGHHLPQPPPPPYGHKRYRQKGREGHSPLKAPHAQPATVEHEVVRDLPPTPAGEGYAVPVIQRHEHHHHHEHHHHHHHHHFHPS
Protein: 1-phosphatidylinositol-4-phosphate 5-kinase (A0A1D8PJ31)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Translocon subunit
- 1-phosphatidylinositol 4-kinase
- Peptidyl-prolyl cis-trans isomerase
- Phosphatidylinositol 4-kinase PIK1a
- Phosphatidylinositol-3-phosphatase
- Phosphoinositide phospholipase C
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- Phosphatidylinositol 4-kinase
- phosphoinositide 5-phosphatase
- phosphoinositide 5-phosphatase
Sequence:
MLSTISPSSSSAPHPPQDHFHNDSSKSGDKNSSLPAQFQTQPSDDELTIKLPLLTSENLLQRQEEEEQVQVQKGNPIVESSNNKNTTFTTTTNNNNNDNDNHRSPSTPTSFKGTRSETNSNYTHETTPSSLDHNDSKSTLPPSDTSYQFNLKINNPRSSFDIDPLHKPISNNHEQHHSGANHTIKSPQPVSQPTADPISIPQKTKTITSSTTTTTTETPKNIRRHTSPMPMPMLPRRSLDGHVGSSKLQKFTSRTDSAIALTRHSINIDRPTNRSTFGGTGSPRALPISSTHEIQRMRDSILLKRHMKKRPTEEDKVLVGNKISEGHENFVMAYNMLTGIRVAVSRCSGVMRKLTEEDFKATKKLSFNFDGSELTPSSKYDFKFKDYCPEVFRELRQIFGIDPADYLVSITGKYILSELGSPGKSGSFFYYSRDFRFIIKTIHHSEHKQLLRMLKDYHHHVKDNPNTLISQFYGLHRVKMPLFGGGSRKVHFVVMNNLFPPHRDIHLKYDLKGSTWGRNTTIFPGWDEKELSKHTLKDLNWLERHQKIQFGPEKRHIFFKQLEADVKLLQKVNVMDYSLLLGIHDVKKGNTADIEKQLSVFEPKSFDKRALINTNPRDLDRQQDLPNDVFPGRSKYVFYGHDGGIRATSEENIPTSEIYYLGIIDCLTNYSLKKRLETCWRSLSHPRNTISAVPAREYGDRFLEFIKKGTTQLKKKRN
Protein: Cullin 4B (A0A8I6B5A8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFPTGFSSPNPSAASAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSSNSSNEREDFDSTSSSSTPPQPRDSASPSTSSFCLGVPVATSSHVPIQKKLRFEDTLEFVGFDTKMAEESSSSSSSSSPTAATSQQQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQTKTIDGILLLIERERNGEAIDRSLLRSLLNMLSDLQIYQDSFEQRFLQETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIASVEKQLLGEHLTAILQKGLNSLLDENRIQDLSLLYQLFSRVRGGVQVLLQHWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDTCFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA
Protein: Synaptopodin (Q8N3V7)
Organism: Homo sapiens (Human)
Function: Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8CC35}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8CC35}. Perikaryon {ECO:0000250|UniProtKB:Q8CC35}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q8CC35}. Postsynaptic density {ECO:0000250|UniProtKB:Q8CC35}. Synapse {ECO:0000250|UniProtKB:Q8CC35}. Cytoplasm, cytosol {ECO:0000269|PubMed:30661770}. Note=Localized at the tight junction of cells. In brain, localized to the postsynaptic densities and in the perikarya. Associated with dendritic spines of a subset of synapses. {ECO:0000250|UniProtKB:Q8CC35}.
Interaction partners:
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Alpha-actinin-4
- Nephrin
- CD2-associated protein
- Actin, cytoplasmic 1
- Podocin
- Podocalyxin
- Actin, cytoplasmic 2
- Wilms tumor protein
- Tight junction protein 1
Sequence:
MLGPHLPPPPLAPSEGRPTPCAFQIPDGSYRCLALEAEESSGEEGLQGEVGPTDLEEDEGVSRSGDDSACRVTQGTPQLPKALGIQPPSCSREEQGASQHDDRASQDWDVVKAGQMMTASPSPGPGPRVAQKPALGRSTSLTEKDLKEAKARSQQIAAQLTTPPSSNSRGVQLFNRRRQRVNEFTLESHGQRGQKPSQESLRVLPSSLPGHAPGLSLSSTSLPEPGPPRHPSPQSPDRGVPGHSMEGYSEEASLLRHLEKVASEEEEVPLVVYLKENAALLTANGLHLSQNREAQQSSPAPPPAEVHSPAADVNQNLASPSATLTTPTSNSSHNPPATDVNQNPPATVVPQSLPLSSIQQNSSEAQLPSNGTGPASKPSTLCADGQPQAPAEEVRCSTLLIDKVSTPATTTSTFSREATLIPSSRPPASDFMSSSLLIDIQPNTLVVSADQEMSGRAAATTPTKVYSEVHFTLAKPPSVVNRTARPFGIQAPGGTSQMERSPMLERRHFGEKAPAPQPPSLPDRSPRPQRHIMSRSPMVERRMMGQRSPASERRPLGNFTAPPTYTETLSTAPLASWVRSPPSYSVLYPSSDPKSSHLKGQAVPASKTGILEESMARRGSRKSMFTFVEKPKVTPNPDLLDLVQTADEKRRQRDQGEVGVEEEPFALGAEASNFQQEPAPRDRASPAAAEEVVPEWASCLKSPRIQAKPKPKPNQNLSEASGKGAELYARRQSRMEKYVIESSSHTPELARCPSPTMSLPSSWKYPTNAPGAFRVASRSPARTPPASLYHGYLPENGVLRPEPTKQPPYQLRPSLFVLSPIKEPAKVSPRAASPAKPSSLDLVPNLPKGALPPSPALPRPSRSSPGLYTSPGQDSLQPTAVSPPYGGDISPVSPSRAWSPRAKQAPRPSFSTRNAGIEAQVWKPSFCFK
Protein: Mitochondrial Rho GTPase 2 (MIRO-2) (EC 3.6.5.-) (Ras homolog gene family member T2) (Q8JZN7)
Organism: Mus musculus (Mouse)
Function: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Colocalizes with MGARP and RHOT2 at the mitochondria. {ECO:0000250}.
Interaction partners:
- Trafficking kinesin-binding protein 1
- Trafficking protein, kinesin binding 2
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase PINK1, mitochondrial
- Mitofusin-2
- Unconventional myosin-XIX
- Mitofusin-1
- WD repeat-containing protein 90
- Kinesin heavy chain isoform 5A
- Kinesin-1 heavy chain
Sequence:
MRRDVRILLLGEAQVGKTSLILSLVGEEFPEEVPARAEEITIPADVTPEKVPTHIVDYSEAEQTEEELQEEIHKANVVCVVYDVSEETTIEKIRTKWIPLVNGRTATGPRLPIILVGNKSDLRPGSTMEAVLPIMSQFPEIETCVECSAKHLRNISELFYYAQKAVLHPTAPLYDPEAKQLRPACAQALTRIFRLSDQDRDHGLSDEELNAFQKSCFGHPLAPQALEDVKRVVCKNVSGGVQNDRLTLEGFLFLNTLFIQRGRHETTWTILRRFGYSDSLELTPDYLYPALHVPPGCSTELNHRGYQFVQRMFEKHDQDHDGVLSPTELQNLFSVFSGAPWGPELLHTVPTQAGCLPLHGYLCQWTLMTYLDVQQCLAHLGYLGYPTLCEQDSQAQAITVTREKKLDQEKGQTQRSVLMCKVLGARGVGKSAFLQAFLGNSLGEARDPPEKFPLHTINTVRVNGQEKYLILCEVNADSLLDTSLDTTCDVACLMFDSSDPKTFVHCATIYKRYYMDGQTPCLFIASKADLPEGVAPPGLSPAEFCRRHRLPAPASFSCLGPAMPSTDVFTQLATMATFPHLVHTELHPTSFWLRGVLVAVGTAVAAVLSFSLYRVLVKSR
Protein: Nucleoporin 98-96 (Q868A8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SKYGLGDSDEEDELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGNSDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASESSSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPRSIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVKGNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLVSKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELVDLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAVFRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYNDAFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCSPLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKAVKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDISAKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALERLPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
Protein: Fatty acyl-CoA synthetase B (EC 6.2.1.3) (Long chain fatty acyl coenzyme A-synthetase 2) (LC-FACS 2) (Long-chain-fatty-acid--CoA synthetase 2) (Q1ZXQ4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Long chain fatty acid acyl-CoA synthetases catalyze the formation of a thiester bond between a free fatty acid and coenzyme A during fatty acid metabolic process.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14629118}.
Interaction partners:
- AMP-dependent synthetase/ligase domain-containing protein
- Fatty acyl-CoA synthetase A
- Palmitoyl-protein thioesterase 1
- Palmitoyl-protein thioesterase 2
- Palmitoyl-protein thioesterase 3
- Lipase
- Uncharacterized protein
- Serine aminopeptidase S33 domain-containing protein
- Uncharacterized protein
- Maleylacetoacetate isomerase
Sequence:
MINNWLAVGLLVVSGILAFNWKRKHPYGQTVEIGEKPENGGRIRRNSACADHLISFLEDDEIYTLYDSLVKSCKKYGERKCFGERKKDSNGNLGKFEWISYNTYLERCEYIQQGLCELGLKPKSKVGIFSKNRLEWLIVHSASFIQSYCVVSFYETLGVESLSYVTEHAEIGLAFCSAETLQKTLDIAKGVKVLKTIICFDSIDKEHYNIAKELGVTLYTYDEIMKKGKEANGKHKHTPPTPDTLSTIMYTSGTTGPPKGVMITHKNLTSVVCAVSDFIKVYDTDVHYSYLPYAHVLERVVILAAFHFGAAIGIFSGDISNILVEVKLLSPTLFIGVPRVFERIKTNVFKEISKKPALLRTLFNGAYNLKYLSIQHGFKLPIIEKVLDLVFFSKIKQALGGKVRVILSGSAPLSFDTEVFLRVVMCCCVLQGYGASEGCGGDACKRLDDESVGTIGPPFASNEIKLVDVPELGYDSNGEVQTGEVCLRGPSISSGYYKDEEKTREEFKDGWFHTGDIGRWNRDGSLSIVDRKKNIFKLSQGEYVAVEKIETIVVKSEYVEQVCIYGDSQKSCVIAIIHPHPESCSEWAGSKKTDKDIKEICKNQDFIKVVLDDIIKNCKKSGLHGFEIPKAIHLTPEAFSDQNNLLTPSFKLKRHEIKKYFEDEIKKLYSKLD
Protein: Retinol dehydrogenase 8 (EC 1.1.1.300) (Photoreceptor outer segment all-trans retinol dehydrogenase) (Q9N126)
Organism: Bos taurus (Bovine)
Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity.
Subcellular location: Membrane {ECO:0000305|PubMed:10753906}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lecithin retinol acyltransferase
- Beta-carotene oxygenase 1
- Cytochrome P450 26A1
- Aldehyde dehydrogenase 1A1
- Aldehyde dehydrogenase 1 family member A2
- All-trans-retinol 13,14-reductase
- Aldehyde dehydrogenase 1A1
- Diacylglycerol O-acyltransferase 1
- Cytochrome P450 family 27 subfamily C member 1
- aldehyde oxidase
Sequence:
MADAPRTVLISGCSSGIGLELAVQLAHDPRQRYQVVATMRDLGKKGTLETAAGEALGQTLTVAQLDVCSDESVAQCLNCIQGGEVDVLVNNAGVGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPSMKRRRQGHIVVVSSVMGLQGVVFNEVYAASKFAMEGFFESLAVQLLQFNIFISLVEPGPVVTEFEGKLLEQVSTAEFPGTDPDTLSYFRDLYLPASRELFHNVGQSPQDVAKVIVKVIGSARPPLRRRTNTRYTPLIALKAMDPSGSLYVRTSHCLLFRWPRLLNLGLRCLACSCFRTPVWPR
Protein: Uncharacterized oxidoreductase C8E4.04 (EC 1.-.-.-) (O42888)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized oxidoreductase C215.11c
- Zinc-type alcohol dehydrogenase-like protein C337.11
- Zinc-type alcohol dehydrogenase-like protein C2E1P3.01
- Zinc-type alcohol dehydrogenase-like protein C16A3.02c
- Putative S-
- 3-keto-steroid reductase erg27
Sequence:
MSIKEFAKNAREAYFTLPNGDKIPSIGLGTWRSGKDETKNAVCAALKAGYRHIDTAHIYGNEKEIGEGIRESGVPRTDIWVTSKLWCNAHRAGLVPLALEKTLQDLNLEYIDAYLIHWPFALLSGPEELPRNEKGELIYEDVPIEETWQAMEELLETGKVRYIGISNFNNEYLDRVLKIAKVKPTIHQMELHPYLPQTEYLEKHKKLQIHVSAYSPLANQNDAYNSDISKLIEHKTLVDIANARGEGITPANIAISWAVKRGTSVLPKSVNESRIVSNFLYIPLTDKEMEAINNIGVVRRFSHGKFAPKPMFVGLQDGTPKQTHA
Protein: BolA-like protein 1 (Q3E793)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoyl synthase (LS) and succinate dehydrogenase (SDH). Required during the last step of iron-sulfur protein assembly when the iron-sulfur cluster is inserted into the target protein. Probably acts together with the monothiol glutaredoxin GRX5, earlier than BOL3 and NFU1 in the [4Fe-4S] cluster insertion process. Not required for [2Fe-2S] cluster insertion into mitochondrial proteins.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:27532772, ECO:0000305|PubMed:27532773}.
Interaction partners:
- BolA-like protein 3
- BolA-like protein 2
- Monothiol glutaredoxin-3
- NifU-like protein
- Monothiol glutaredoxin-5
- Fe-S cluster assembly protein DRE2
- Lipoyl synthase, mitochondrial
- Monothiol glutaredoxin-4
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron-sulfur assembly protein 2
Sequence:
MFKRAMSTDGPVARTILKRLECGFPDYKNFAFGLYNDSHKHKGHAGVQGNVSAETHFRIEMVSKKFEGLKLPQRHRMVYSLLQDEMAQANGIHALQLSLKTPQEYESKAK
Protein: Ferric reduction oxidase 2 (AtFRO2) (EC 1.16.1.7) (Ferric-chelate reductase 2) (Protein FERRIC CHELATE REDUCTASE DEFECTIVE 1) (P92949)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavocytochrome that transfers electrons across the plasma membrane to reduce ferric iron chelates to form soluble ferrous iron in the rhizosphere. May be involved in the delivery of iron to developing pollen grains. Acts also as a copper-chelate reductase. Involved in glycine betaine-mediated chilling tolerance and reactive oxygen species accumulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16813577}; Multi-pass membrane protein {ECO:0000269|PubMed:16813577}.
Interaction partners:
- Fe
- ATPase 2, plasma membrane-type
- Transcription factor ORG2
- Transcription factor ORG3
- Transcription factor FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR
- Transcription factor bHLH100
- Transcription factor bHLH101
- Transcription factor bHLH47
- Protein DETOXIFICATION 43
- Metal transporter Nramp3
Sequence:
MEIEKSNNGGSNPSAGEEFKDMIKGVTKFLMMVIFLGTIMLWIMMPTLTYRTKWLPHLRIKFGTSTYFGATGTTLFMYMFPMMVVACLGCVYLHFKNRKSPHHIDRETKGGVWSKLRKPMLVKGPLGIVSVTEITFLAMFVALLLWCFITYLRNSFATITPKSAAAHDESLWQAKLESAALRLGLIGNICLAFLFLPVARGSSLLPAMGLTSESSIKYHIWLGHMVMALFTVHGLCYIIYWASMHEISQMIMWDTKGVSNLAGEIALAAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVLHVGISFSFIALPGFYIFLVDRFLRFLQSRENVRLLAARILPSDTMELTFSKNSKLVYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSIVIKKEGKWSTKLHQRLSSSDQIDRLAVSVEGPYGPASADFLRHEALVMVCGGSGITPFISVIRDLIATSQKETCKIPKITLICAFKKSSEISMLDLVLPLSGLETELSSDINIKIEAFITRDNDAGDEAKAGKIKTLWFKPSLSDQSISSILGPNSWLWLGAILASSFLIFMIIIGIITRYYIYPIDHNTNKIYSLTSKTIIYILVISVSIMATCSAAMLWNKKKYGKVESKQVQNVDRPSPTSSPTSSWGYNSLREIESTPQESLVQRTNLHFGERPNLKKLLLDVEGSSVGVLVCGPKKMRQKVAEICSSGLAENLHFESISFSW
Protein: Varicose (A1XXK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVRWSARSRRQARQDKVELLARNNKVNGEDDTSDNAAFRNSTDLSDHDEIFLKGLLRSNSNTHHKELMLNPTEPQPVPLFLPAHLNNKPICDDIIRKFSPSRRLESRELAKLLAQPHFRALLRAHDEIGALYE
Protein: Endoplasmic reticulum-Golgi intermediate compartment protein (F8VR88)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}.
Interaction partners:
Sequence:
MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVSLIAFTTMALLTIMEFSVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMVASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGH
Protein: Caspar, isoform C (A0A0B4LFH2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSENKDEALTSFQSITGIDDVGEAFSHLEAADWNLVEALSRVIPHEDAPLTSPHPILVPEPPARNAVESTNGFRPPGFDEMPGTSNASGFFAAALQNQNQNLNLNQPHIQQRFPTQLTSSINLDPASSQNNNQNVITFNIHFNQQLYQLRLPSEATVEQLKRKIFAETSVPVCRQAIRGWPPSKASDAQQLGTRLCNLDLSPENELILVDLTEDGFMDTEQDEVTQRVDKDFTIFIQFESDPPLTLSLPGRMTVQEVKMNVFDIKSIPVRHQEWTGWPNGCDNDTTLAQSGIGLSHRFAVRSTERSAPTNSNQHNAFDVVTVDSESSTDEFEDATDFNNAEYIFTDSPPAQPPNRHLIPNDTDDEISGSTQFVENYKARYGEPCPEFFVGSLENAKQLACLRSAKERKLLAIYLHHGKSILSNVFCDQLMKHESIIQTFKEKFVLYGWDMTYESNKDMFLSSLTACISSNASLTARNIKLDKLPAIMLVGKSRQLGSNCEVLSVIHGNIGLDDLLTRLIETCEMFEEQLQVEIRQEDERAARDQVKAEQDMAYQETLQADMAKDAAKRQKEAAQLAERKRMESERAEEDARRESIRLVAQQSLPQEPSEQETGTSKIRVRKPTGDFLERRFFINNNLQDLLNFVTANGFLIEEYKLISSWPRRDLTAIESSQTLESLKLYPQETVILEER
Protein: X-ray repair cross complementing 6 (F7EV16)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ILTAEWSLQPTKYKYSGRDSLIFLVDASRAMFESQGEDELTPFDMSIQCIQSVYTSKIISSDRDLLAVVFYGTEKDKNSVNFKSIYVLQDLDNPGAKRVLELDRFKGQQGKKHFRDTIGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDDPHGNDSAKASRARTKASDLRDTGIFLDLMHLKKRGGFDVSLFYRDIISIAEDEDLGVHFEESSKLEDLLRKVRAKETKKRVLSRLKFKLGKDVALMVGVYNLVQKANKPFPVRLYRETNEPVKTKTRTFNVNTGSLLLPSDTKRSLTFGTRQIVLEKEETEELKRFDEPGLILMGFKPMVMLKNHHYLRPSLFLYPEESLVNGSSTLFSALLTKCVEKEVIAVCRYTARKNVSPYFVALVPQEEELDDQNIQVTPAGFQLVFLPYADDKRKVPFTEKVMANPEQIDKMKAIVQKLRFTYRSDSFENPVLQQHFRNLEALALDMMESEQVVDLTLPKVEAIKKRLGSLADEFKELVYPPGYNPEGKIAKRKADNEGSASKKPKVELSEEELKDLFAKGTLGKLTVPALRDICKAYGLKSGPKKQELLEALSRHLEKN
Protein: UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) (P0C0F4)
Organism: Streptococcus pyogenes
Function: Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Hyaluronan synthase
- UDP-glucose 6-dehydrogenase
- Glucose-1-phosphate thymidylyltransferase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Bifunctional protein GlmU
- dTDP-glucose 4,6-dehydratase
Sequence:
MKIAVAGSGYVGLSLGVLLSLQNEVTIVDILPSKVDKINNGLSPIQDEYIEYYLKSKQLSIKATLDSKAAYKEAELVIIATPTNYNSRINYFDTQHVETVIKEVLSVNSHATLIIKSTIPIGFITEMRQKFQTDRIIFSPEFLRESKALYDNLYPSRIIVSCEENDSPKVKADAEKFALLLKSAAKKNNVPVLIMGASEAEAVKLFANTYLALRVAYFNELDTYAESRKLNSHMIIQGISYDDRIGMHYNNPSFGYGGYCLPKDTKQLLANYNNIPQTLIEAIVSSNNVRKSYIAKQIINVLKEQESPVKVVGVYRLIMKSNSDNFRESAIKDVIDILKSKDIKIIIYEPMLNKLESEDQSVLVNDLENFKKQANIIVTNRYDNELQDVKNKVYSRDIFGRD