wanglab/gogpt-training-data huggingface dataset:
Protein: Sulfotransferase 2A1 (ST2A1) (EC 2.8.2.2) (Bile salt sulfotransferase 1) (EC 2.8.2.14) (Hydroxysteroid sulfotransferase) (ST) (P52843)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism (By similarity). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06520}.
Interaction partners:
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Sulfotransferase
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Nuclear receptor subfamily 1 group I member 2
- Cytochrome P450 3A11
- UDP-glucuronosyltransferase 1A1
Sequence:
MMSDYNWFEGIPFPAISYQREILEDIRNKFVVKEEDLLILTYPKSGTNWLIEIVCLIQTKGDPKWIQTVPIWNRSPWIETDIGYSALINKEGPRLITSHLPIHLFSKSFFSSKAKAIYLVRNPRDILVSGYFFWGNTNLVKNPGSLGTYFEWFLKGNVLFGSWFEHVRGWLSMREWDNFLVLYYEDIKKDTKGTIKKICDFLGKNLGPDELDLVLKYSSFQAMKENNMSNFSLIKEDQVTNGLKLMRKGTIGDWKNHFTVAQAEAFDKVFQEKMAGFPPGIFPWE
Protein: Centromere protein F (E9PY14)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSWALEEWKEGLPSRALQKIQELEGQLEKLKKEKQQRQFQLDSLEAALQKQKQKVEDGKTEGADLKRENQRLMEICEHLEKSRQKLSHELQVKESQVNLQESQLSSCKKQIEKLEQELKRCKSEFERSQQVAQSADVSLNPCSTPQKLFATPLTPSSTYEDLKEKYNKEVEERKRLEEEVKALHAKKVSLPVSQATMNHRDIARHQASSSVFPWQQENTPSRLSSDALKTPLRRDGSAAHFLGEEVSPNKSSMKTGRGDCSSLPDLKSKMTELELRLQGQEKEMRSQVNKCQDLQLQLEKTKVELIEKERILNKTRDEVVRSTAQYDQAAAKCTTLEQKLKTLTEELSCHRQNAESAKRSLEQRIKEKEKELQEELSRQHQSFQALDSEYTQMKTRLTQELQQVKHLHSTLQLELEKVTSVKQQLERNLEEIRLKLSRAEQALQASQVAENELRRSSEEMKKENSLIRSQSEQRTREVCHLEEELGKVKVSLSKSQNFAEEMKAKNTSQEIMLRDLQEKLNQQENSLTLEKLKLALADLERQRNCSQDLLKKREHHIDQLNNKLNKIEKEFETLLSALELKKKECEELKEEKNQISFWKIDSEKLINQIESEKEILLGKINHLETSLKTQQVSPDSNERIRTLEMERENFTVEIKNLQSMLDSKMVEIKTQKQAYLELQQKSESSDQKHQKEIENMCLKANKLTGQVESLECKLQLLSSEVVTKDQQYQDLRMEYETLRDLLKSRGSSLVTNEDNQRSSEDNQRSSEDNQRGSLAFEQQPAVSDSFANVMGRKGSINSERSDCSVDGGRSPEHIAILQNRVTSLESSLESQNQMNSDLQMRCEELLQIKGEVEENLSKAEQIHQNFVAETNQCISKLQEDAAVHQNIVAETLATLESKEKELQLLKEKLEAQQTEVQKLNKNNCLLEGTLKELQLLSDTLSSEKKEMNSIIS
Protein: GATA transcription factor 4 (AtGATA-4) (O49743)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDVYGMSSPDLLRIDDLLDFSNDEIFSSSSTVTSSAASSAASSENPFSFPSSTYTSPTLLTDFTHDLCVPSDDAAHLEWLSRFVDDSFSDFPANPLTMTVRPEISFTGKPRSRRSRAPAPSVAGTWAPMSESELCHSVAKPKPKKVYNAESVTADGARRCTHCASEKTPQWRTGPLGPKTLCNACGVRYKSGRLVPEYRPASSPTFVLTQHSNSHRKVMELRRQKEQQESCVRIPPFQPQ
Protein: Small t antigen (ST) (ST-AG) (P03081)
Organism: Simian virus 40 (SV40)
Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters. Late during the infection cycle, ST may induce dephosphorylation of host eIF4E-binding protein EIF4EBP1 leading to the inhibition of cap-dependent translation. May establish and maintain high levels of viral genomes during persistent infection in cell culture.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:6323762}. Host nucleus {ECO:0000269|PubMed:6323762}.
Interaction partners:
Sequence:
MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEVFASSLNPGVDAMYCKQWPECAKKMSANCICLLCLLRMKHENRKLYRKDPLVWVDCYCFDCFRMWFGLDLCEGTLLLWCDIIGQTTYRDLKL
Protein: ILK associated serine/threonine phosphatase (Integrin-linked kinase associated phosphatase) (F8SNU6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLFGDLPEPERSPRPAAGKEAQKGPLLFDDLPPASSTDSGSGGPLLFDDLPPASSGDSGSLATSISQMVKTEGKGAKRKTSEEEKNGSEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITEECRPPSSLMRCNQCRENREEMPFGHFQAY
Protein: Mitochondrial glutathione transporter SLC25A39 (Solute carrier family 25 member 39) (Q9BZJ4)
Organism: Homo sapiens (Human)
Function: Mitochondrial transporter required for glutathione import into mitochondria. Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles. Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters, as well as erythropoiesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11139402, ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:37917749}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RUN domain-containing protein 3A
Sequence:
MADQDPAGISPLQQMVASGTGAVVTSLFMTPLDVVKVRLQSQRPSMASELMPSSRLWSLSYTKLPSSLQSTGKCLLYCNGVLEPLYLCPNGARCATWFQDPTRFTGTMDAFVKIVRHEGTRTLWSGLPATLVMTVPATAIYFTAYDQLKAFLCGRALTSDLYAPMVAGALARLGTVTVISPLELMRTKLQAQHVSYRELGACVRTAVAQGGWRSLWLGWGPTALRDVPFSALYWFNYELVKSWLNGFRPKDQTSVGMSFVAGGISGTVAAVLTLPFDVVKTQRQVALGAMEAVRVNPLHVDSTWLLLRRIRAESGTKGLFAGFLPRIIKAAPSCAIMISTYEFGKSFFQRLNQDRLLGG
Protein: Vacuolar transporter chaperone complex subunit 1 (SPX-dependent polyphosphate polymerase VTC subunit 1) (Vacuolar membrane polyphosphate polymerase accessory subunit 1) (PolyP polymerase) (Q57UM0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. VTC1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion.
Subcellular location: Acidocalcisome membrane {ECO:0000269|PubMed:17635107}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Short-chain dehydrogenase, putative
- Putative enoyl-CoA reductase
Sequence:
MASVIEKGLASICCVTTSSKPWAEGEADGDVKYEDLRGPGGRNTSGSVSDKRICVPQKIDPKTFFANERTFLKWMSISVMIGMMSLTLLNFGDTSSNASELAGLVLLPVSILFMIHSLFVFKDRANKIYMREPMRYDDTKGPTILVLVLGVSLGIAAIFSVQKQYYRTASSSFNDGPRFS
Protein: Cryptochrome-1 (Q7ZU27)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVVNTVHWFRKGLRLHDNPSLRDSIKGADNLRCVYILDPWFAGSSNVGISRWRFLLQCLEDLDASLRKLNSRLFVIRGQPTDVFPRLFKEWKISRLSYEYDSEPFGKDRDAAIRKLATEAGVEVFVRISHTLYDLDKIIEFNGGQSPLTYKRFQTLISRMDPVEMPAETITAEIMGKCSTPVSDDHDDKFGVPSLEELGFETEGLSTAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYRKVKKNSTPSLSLYGQLLWREFFYTAATNNPHFDKMEFNPICVQIPWDRNPEALAKWAEGQTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSVNAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPILRGFPAKFIYDPWNAPESVQKVAKCIIGVHYPKPMVNHAEASRINIERMKQIYQQLSCYRGLGLLATIPSNTANNEDSNGAGPSSGDTQESTHITVHTLPASSQSEFPAFAVSCGQQLVNSVQPQPGYSGAGMVGQAHKQTQRVRGMTAFKRHGEDRTTDFPSKIQRNDGI
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (P75189)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
- Pyruvate kinase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Transketolase
- Probable ATP-dependent 6-phosphofructokinase
- Large ribosomal subunit protein uL4
Sequence:
MSAQTGTDLFKIADLFAYQVFDSRGFPTVACVVKLASGHTGEAMVPSGASTGEKEAIELRDGDPKAYFGKGVSQAVQNVNQTIAPKLIGLNATDQAAIDALMIQLDGTPNKAKLGANAILAVSLAVAKAAASAQKTSLFKYLANQVMGLNKTEFILTVPMLNVINGGAHADNNIDFQEFMIMPLGANSMHQALKMASETFHALQKLLKQRGLNTNKGDEGGFAPNLKLAEEALDLMVEAIKAAGYQPGSDIAIALDVAASEFYDDTTKRYVFKKGIKAKILDEKEWSLTTAQMIAYLKKLTEQYPIISIEDGLSEHDWEGMETLTKTLGQHIQIVGDDLYCTNPAIAEKGVAHKATNSILIKLNQIGTLTETIKAINIAKDANWSQVISHRSGETEDTTIADLAVAACTGQIKTGSMSRSERIAKYNRLLQIELELGNNAKYLGWNTFKNIKPQKA
Protein: Stromal interaction molecule 2 (D4A5X1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein orai-3
- Calcium release-activated calcium modulator 2 protein
- Stromal interaction molecule 1
- Calcium release-activated calcium channel protein 1
- Short transient receptor potential channel 1
- Transient receptor potential Ca2+ channel 6A
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Short transient receptor potential channel 3
- Store-operated calcium entry-associated regulatory factor
- Nuclear factor of activated T-cells 5
Sequence:
MNAAGCRAPRAAGEGSGLAPGGSLLPRRRGPGQLAASECPAAPVSAPPAAAPGRALGRPSRRRWAAMLLFGLLVAGVADGCDLVPRHLRGRRASGSAGAAASPSAAAAGERQALLTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTVAKPAGSLARSSSLCRSRRSIVPSSPQSQRAQLPAHAPLAAHPRHPHHPQHSLPSPDPDILSVSSCPALYRNEEEEEAIYFTAEKQWEVPDTASECDSLNSSIGRKQSPPSSLEIYQTLSSRKISRDELSLEDSSRGDSPVTADVSRGSPECVGLTETKSMIFSPASRVYNGILEKSCSMHQLSSGIPVPNPRHTSCSLAGSDSKPVQEASSVSRVGSIPHDLCHNGEKSKKPSKIKSLFKKKSK
Protein: E3 ubiquitin-protein ligase Godzilla (EC 2.3.2.27) (Q9VI20)
Organism: Drosophila melanogaster (Fruit fly)
Function: Endosomal E3 ubiquitin-protein ligase that regulates the recycling endosome pathway by mediating ubiquitination of Synaptobrevin (Syb). Also acts as a regulator of transcytosis in wing imaginal disks by catalyzing ubiquitination of Syb: ubiquitination of Syb promotes transcytosis of wingless (wg) to the basolateral surface.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:23353890}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Kinesin-like protein Klp98A
Sequence:
MSKRSCQILTLLGLCLVCHEATLVGGHVLVYRKATSQLIEEFNDLPAQFGPNLPSNGLKVYVVPARRPYYGCDSLDRPPHLKYPPSAKFVALVARGECVFERKIRVAQNASYSAVIVYNNEGDDLEQMSAENITGIRIPSVFVGHTTGKALATYFTTEVVLIINDELPFNINTQLILPFSILIGMCFIIMVIYMIYKCIREQRRLRRHRLPKSMLKKLPVLRYTKNNANNKYDTCVICLEDFIEDDKLRVLPCSHPYHTHCIDPWLTENRRVCPICKRKVFTKGEARASRSRQPSLDNVTDTDDDTTPLLQQQQSNGRQVGQVSSASSAGGAAGSSSSVAAAAVAGTTRHGTFRRGHAGRNPFEESQSSDDENALLASTVRPATSSGAHERINPFDRAPNLPAHLAEQLTESRRSVWSRINFASFFRRQPAVISVAAPPYLERVESGTSAMGLPVTGTIAVASPASNNILNPNLSGSFKDEDDMPPHRSIYEPIAISTPAADSATVDDSAFLQTPTQGGIGVAALPHSASDRQFLI
Protein: Acyltransferase 3 domain-containing protein (Q9I1M7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslA
- PslJ
- PslH
- PslD
- PslF
- PslE
- PslI
- Alginate biosynthesis protein AlgA
- PslG
- FAD-dependent oxidoreductase 2 FAD-binding domain-containing protein
Sequence:
MKKRWIQMDVTRGVGILIIVFGHSWFVASSPTVLYPLLSPFILPLFFFISGVFFRTEQPFGEMALRKADALLKPFFVTMLGYVILRDLLRGQPLLPDIGGVLYASVDTLPWQALWYLPHFWVATLFAWFMLRVIQRLGLSLAASCVLLAVQLGLGILFLKTFWQIPVEFGGEQYLLPGLPFSLDITLISSAHFMFGYVLRDVLRRHQSSLLTLCIALAVTTASFLYYPTVVDMAQRRYDHWFWATVQAVSGVYLCWALSGLMMKIDWLGKAMTYIGQSTLILLIFHGEIQHKTFNLLVHLGLSEPAAASVALVISVIVSLLIGEVIKRVALLRALYFPFPVRKKTAAVQGGGEAR
Protein: Heat shock protein 60, mitochondrial (60 kDa chaperonin) (Protein Cpn60) (O74261)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins (By similarity).
Subcellular location: Mitochondrion.
Interaction partners:
- 10 kDa heat shock protein
- Heat shock protein SSC1, mitochondrial
- Hsp70 family ATPase
- GrpE protein homolog
- Cofilin
- Heat shock protein 78
- Heat shock protein HSP70
- T-complex protein 1 subunit alpha
- Endoplasmic reticulum chaperone BIP
- Heat shock protein homolog SSE1
Sequence:
MLRVNSKSSIKTFVRHLSHKELKFGVEGRAALLKGVNTLADAVSVTLGPKGRNVLIEQQFGAPKITKDGVTVAKAITLEDKFEDLGAKLLQEVASKTNESAGDGTTSATVLGRSIFTESVKNVAAGCNPMDLRRGSQAAVEAVIEFLQKNKKEITTSEEIAQVATISANGDKHIGDLLANAMEKVGKEGVITVKEGKTLEDELEVTEGMKFDRGFISPYFITNTKTGKVEFENPLILLSEKKISSIQDILPSLELSNQTRRPLLIIAEDVDGEALAACILNKLRGQVQVCAVKAPGFGDNRKNTLGDIAILSGGTVFTEELDIKPENATIEQLGSAGAVTITKEDTVLLNGEGSKDNLEARCEQIRSVIADVHTTEYEKEKLQERLAKLSGGVAVIKVGGASEVEVGEKKDRYEDALNATRAAVEEGILPGGGTALIKATKILDEVKEKAVNFDQKLGVDTIRAAITKPAKRIIENAGEEGAVIVGKIYDEPEFNKGYDSQKGEFTDMIAAGIIDPFKVVKNGLVDASGVASLLATTECAIVDAPQPKGSPAAPPAPGMGGMPGMF
Protein: L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (LDH muscle subunit) (LDH-M) (P06151)
Organism: Mus musculus (Mouse)
Function: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+).
Subcellular location: Cytoplasm.
Interaction partners:
- L-lactate dehydrogenase B chain
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Pyruvate carboxylase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Fructose-bisphosphate aldolase A
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Glucose-6-phosphate isomerase
Sequence:
MATLKDQLIVNLLKEEQAPQNKITVVGVGAVGMACAISILMKDLADELALVDVMEDKLKGEMMDLQHGSLFLKTPKIVSSKDYCVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPHCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWVLGEHGDSSVPVWSGVNVAGVSLKSLNPELGTDADKEQWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGINEDVFLSVPCILGQNGISDVVKVTLTPEEEARLKKSADTLWGIQKELQF
Protein: Aquaporin NIP2-1 (Low silicon protein 1) (NOD26-like intrinsic protein 2-1) (OsNIP2;1) (Silicon influx transporter LSI1) (Q6Z2T3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Silicon influx transporter responsible for silicon transport from the external solution to the root cells. Is coupled with the silicon efflux transporter LSI2 in both exodermal and endodermal root cells for an efficient silicon transport across the cells into the stele. Silicon is beneficial to plant growth and helps plants to overcome abiotic and biotic stresses by preventing lodging (falling over) and increasing resistance to pests and diseases, as well as other stresses. Is coupled with LSI2 transporter in roots for efficient uptake of arsenite, which is further dispatched in shoots and grains. Mediates uptake of methylated arsenic species in roots.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16572174}; Multi-pass membrane protein {ECO:0000269|PubMed:16572174}.
Interaction partners:
- Silicon efflux transporter LSI2
- Os01g0673500 protein.
- Katanin
- Katanin p60 ATPase-containing subunit A1
- Os09g0515100 protein
- glycerol kinase
- 26S protease regulatory subunit 4, putative, expressed
- Os01g0668300 protein
- Os01g0668200 protein
- 26S proteasome regulatory subunit 7B
Sequence:
MASNNSRTNSRANYSNEIHDLSTVQNGTMPTMYYGEKAIADFFPPHLLKKVVSEVVATFLLVFMTCGAAGISGSDLSRISQLGQSIAGGLIVTVMIYAVGHISGAHMNPAVTLAFAVFRHFPWIQVPFYWAAQFTGAICASFVLKAVIHPVDVIGTTTPVGPHWHSLVVEVIVTFNMMFVTLAVATDTRAVGELAGLAVGSAVCITSIFAGAISGGSMNPARTLGPALASNKFDGLWIYFLGPVMGTLSGAWTYTFIRFEDTPKEGSSQKLSSFKLRRLRSQQSIAADDVDEMENIQV
Protein: Killer cell lectin-like receptor subfamily H, member 1 (Q8K4F1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQLSEMNEGRLTYAELKLSLKSKDKPQPTQKKREYPWRISVVILGTVCLCLLISSIVFGYLFFQGTSKFKIQCEKDANKNAVSSMEVVDPSALPPTTGKGCYKCQGRWFCCGEKCYYFSEEEKTWDESEASCRLLGSHLAKIDNREEQNFIQSRLNYSYWVGLRKKGGQFLWVHQEDEKISSDLDFHMTTHLADAACGYIKPKLLNNAQCSRLFPYICKKNFTCLLTSENW
Protein: Pre-mycofactocin synthase (PMFT synthase) (EC 1.4.3.26) (P9WND7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the enzyme cofactor mycofactocin (MFT). Catalyzes the oxidative deamination of AHDP (3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one), forming an alpha-keto amide moiety on the resulting molecule, which is called pre-mycofactocin (PMFT). This reaction occurs via a 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one intermediate, which converts to PMFT. The alpha-keto amide moiety is the redox-active center for the redox activity of mycofactocin.
Interaction partners:
- Mycofactocin maturase MftC
- Peptide chaperone MftB
- Mycofactocin precursor peptide peptidase
- Pre-mycofactocin glycosyltransferase
- Mycofactocin precursor peptide
- Pyruvate kinase
- Putative L-lactate dehydrogenase
- 2-oxoglutarate oxidoreductase subunit KorA
- Pyruvate carboxylase
- Putative malate oxidoreductase
Sequence:
MAEAWFETVAIAQQRAKRRLPKSVYSSLIAASEKGITVADNVAAFSELGFAPHVIGATDKRDLSTTVMGQEVSLPVIISPTGVQAVDPGGEVAVARAAAARGTVMGLSSFASKPIEEVIAANPKTFFQVYWQGGRDALAERVERARQAGAVGLVVTTDWTFSHGRDWGSPKIPEEMNLKTILRLSPEAITRPRWLWKFAKTLRPPDLRVPNQGRRGEPGPPFFAAYGEWMATPPPTWEDIGWLRELWGGPFMLKGVMRVDDAKRAVDAGVSAISVSNHGGNNLDGTPASIRALPAVSAAVGDQVEVLLDGGIRRGSDVVKAVALGARAVMIGRAYLWGLAANGQAGVENVLDILRGGIDSALMGLGHASVHDLSPADILVPTGFIRDLGVPSRRDV
Protein: Homoserine O-acetyltransferase (EC 2.3.1.31) (Homoserine O-trans-acetylase) (O60062)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Homoserine dehydrogenase
- Probable cystathionine gamma-synthase
- Homocysteine synthase
- Tryptophan synthase
- Serine racemase
- Threonine dehydratase, mitochondrial
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Serine hydroxymethyltransferase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Cystathionine beta-lyase
Sequence:
MESQSPIESIVFTDSCHPSQQENKFVQLISDQKIAIVPKFTLECGDILYDVPVAFKTWGTLNKEGNNCLLLCHALSGSADAGDWWGPLLGPGRAFDPSHFFIVCLNSLGSPYGSASPVTWNAETHSVYGPEFPLATIRDDVNIHKLILQRLGVKQIAMAVGGSMGGMLVLEWAFDKEFVRSIVPISTSLRHSAWCISWSEAQRQSIYSDPKFNDGYYGIDDQPVSGLGAARMSALLTYRSKCSFERRFARTVPDASRHPYPDRLPTPLTPSNAHWVVHNEGNRNRRERPCRSNGSSPTSESALNSPASSVSSLPSLGASQTTDSSSLNQSSLLRRPANTYFSAQSYLRYQAKKFVSRFDANCYISITKKLDTHDITRGRGSDSPKEVMKDLSLPVLVLGIESDGLFTFDEQVEIAKSFPNATLEKIISAEGHDGFLLEFTQVNSHIQKFQKEHLIDIMSQTNSFERLDSQVNDTNRESVFGEMEDITSW
Protein: GH09628p (Q7K3V9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVYPSDTSDANNEELALEHSVAHGNVHGNGTGTGGSSPGTTTAPNGDNKVNQRHYEPAERFIITKNVVVIGLAFMIHFTAFHGTSNLQSSVNADKALGTTTLAVIYGSLILSNIFLPMTVIRWFGCRLTMALALFAYMPYIAAQFYPRFETLIPAALMVGFGGGPLWCSKCTYLSTVSEALTQVRGNKSRKDVNTVKFFGLFFIFYQMAQVWGNLISSSVLTLSAPAAQSAANDSFELEVQRELERNRVAELCGARFCPGVGAEANPNLVPPAPEQIQLLNSIFLTCMAAAVVMMIFGVSSLKRYGVKRGDTGDGMSGLKLLTVTINLLRKRRQILMLPITMFIGLEEAFLAVDFTRSFVACGWGISRIGFAMICFGVANAVAAGIAGALVERIGRVTLAALCAVVNLCLLTYMYTWEAREGDYMSYCTFAAVWGICDGVWLVVVNAFYGILFPNHLIAAYSNFRLWESTGSVIGYVISSQLCTSTKLVILIIFILVGCVGYGLIEYRFWQKQKNLEVMLSD
Protein: Rho GTPase activating protein 32 (A0A8I6GFW8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
METESENGSVGDDSVFWLDSEGTTQLTDGEEEEREESFRKMKSSIHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKSCGSTASMKVKHVKKSTPPGLMGCDNIHRLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEIMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDILKDSPESVTQMLAAYLSRLSTIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYSTVFWSLSFIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGKISAVMQEGAASLTRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEVLGNRCNSYDNLPHDNESEEEVGLLHIPALVSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSLGFTRDKLGASKKDVEAGGSQSQTPGSTASSEPVSPVQEKLSPFFTLDLSPTEDKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMNISEPISVTLPPRVSEVIGTVSNTVSQNASPPSWDKSVEERDVINRSPTQLGKMKPGEREAQERCEPEAQPQEQGAAEEVELPGTEERPVSSSQSKAVPSGQSQTGAVTHDPPQDPVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQTLKRPGPSQAGCTSYGDMAVATSEEKLPSSYSSVTLDKTYFQTDRPAEQFHLQINGLGNCDQPLPETAAMGGPTHPNTTDSGEQLHQVDLIGNSLHRNHLSGDPEKARSTSAPLADSEKSDGHGSFPEDHAGKTSVSTVSFVGQGQSPLHFSSGDQPLSYLGTSMDKPHHSSELTEKSPMPSTLPRDKAHPLSGSPEENTSTATMAYMMTTPPRAETSTREASRAMAEQPTAADFVAATLQRAHRTNRPLPPPPSQRPTEQPPGVGQVQEAPSIGVNNSHKQVQGAAPAPERPPEPRAMADPAPIFVSDGSAAAQCPMAISAAQPGLPEKVRESSRAPPLHLRAETFPGHSCGFAAPVPPTRTVESKMAAAMHSSAAEANNSSNYHSFVPSSASADDVLPLPPPIAQPKHASQKIAYSSFARPDVTTEPFGPENCLHFNMTPNCQFRPQSVPPHHNKLEPHQVYGTRSEPPASMGPRYNTYVAPGRSMSGHHSKPCSRVEYVSSLGSSVRNPCCPEDILPYPTIRRVQSLHAPPPSMIRSVPISRTEVPPDDEPAYCPRPVYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLSNRDFAFYNPRLQGKNAYNYAALPPRPRASATGYFSSNDHNVVNMPPTADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPIMSQYDNMAPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKEGRHPAKAVSPEGDERFYRKHPESEFDRAHHHGGYGSQQVEKPSLPQKQSSLRNRKLHDMGCSLPEHRAHQEASHRQLCESKNGPPYPQGAGQLDYGSKGMPDASEPNSYHNSGKYVTSGQESLRLNHKEVRLSKDVDRPRARQPPAPEKHSRDCYKEEEHFTQSVVPPPKPERSHSLKLHHTQNLERDPSMLYPYQTHSKRQSSVTVVSQYDNLEDYHSLPQHQRGGFGGGGMGAYVPSGFVHPQSRTYATALGQGAFLPTELSLPHPDTQIHAE
Protein: Chaperone protein dnaJ 11, chloroplastic (AtDjC11) (AtJ11) (Q9FYB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a continuous role in plant development probably in the structural organization of compartments.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11516154}. Note=Probably also in other plastids.
Interaction partners:
- Chaperone protein dnaJ 8, chloroplastic
- Chaperone protein dnaJ 10
- Heat shock 70 kDa protein 17
- Heat shock 70 kDa protein 4
- AT3g62190/T17J13_150
- CHP-rich zinc finger protein-like
- Cytochrome P450 716A2
- GrpE protein homolog
- CAP superfamily protein
- Heat shock 70 kDa protein 5
Sequence:
MLSSSPTSFTHPFLSSSPPLSPISPPSRTARISPPLVSASCSYTYTEDSPRLHQIPRRLTTVPASLYDVLEVPLGATSQDIKSAYRRLARICHPDVAGTDRTSSSSADEFMKIHAAYCTLSDPEKRSVYDRRMLRRSRPLTVGTSGLGSYVGRNWETDQCW