wanglab/gogpt-training-data huggingface dataset:
Protein: Microfibrillar-associated protein 3-like (Testis development protein NYD-SP9) (O75121)
Organism: Homo sapiens (Human)
Function: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. May a have a role in metastasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24735981}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:24735981}. Cytoplasm {ECO:0000269|PubMed:24735981}. Note=Mainly localized in the nucleus (PubMed:24735981). {ECO:0000269|PubMed:24735981}.
Interaction partners:
Sequence:
MDRLKSHLTVCFLPSVPFLILVSTLATAKSVTNSTLNGTNVVLGSVPVIIARTDHIIVKEGNSALINCSVYGIPDPQFKWYNSIGKLLKEEEDEKERGGGKWQMHDSGLLNITKVSFSDRGKYTCVASNIYGTVNNTVTLRVIFTSGDMGVYYMVVCLVAFTIVMVLNITRLCMMSSHLKKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLIMNCRTIMEEIMEVVGLEEQGQNFVRHTPEGQEAADRDEVYTIPNSLKRSDSPAADSDASSLHEQPQQIAIKVSVHPQSKKEHADDQEGGQFEVKDVEETELSAEHSPETAEPSTDVTSTELTSEEPTPVEVPDKVLPPAYLEATEPAVTHDKNTCIIYESHV
Protein: Uncharacterized protein DDB_G0289357 (Q54HM2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein DDB_G0286393
- Aspartyl aminopeptidase
- RBR-type E3 ubiquitin transferase
Sequence:
MSNSDKNNNNNTNNNNNNNNNNNGNFGIWEEPDDDSTNENEELFNNLITKTTKFIDDDEEEEEEESSWDTLYAKHVETSNTTQPFNNSNSNNNNFQTQPTNISTLNPNNNNSNNSSSGSSSSRGVRTPRGTRSNSPPQPSKNETVQKESSGDISEGFTLIDSPNDNNDNKNNNKNNNNDSNIVDDDEDEEEFPTLSKKNQKRKPKKSTSSPSSTSSPIVSPQTQTSKLESSMDVSPSSGKQSWSELLKNVADEDINNNNNNNNNNNSNQYHQEEENYYDSDDYDSSPFAIINNSSTTTNNNNNNNNNTTTTTTTTTTTNSSSLPIVNSQSFEEGEEITSDIKIGIKPKTVTVPFQSTLSLRARTKQIKKVQQQQQQSSKSKPNNNNNKFVDNNPYAVLEEEERALQSAIKASLLLNSPVDLDSKQQNVSQQKQQQEQQPTTTTNSVSSSKSKSVATTDKNRTTSTAVAPTTSSNKKANKSNKTSTANTTATTTTTASSKKNKSNSNKSSNVSNTTTTTSTTENSASEGSFIKNAVIFIFILLLMVVGFKYTQTLNQ
Protein: Asp1 (Q3S2Y6)
Organism: Streptococcus agalactiae
Interaction partners:
Sequence:
MFYFIPSWYNSDQKWHNEAPIWYRVLENMTFDDTVSQVRMFQNADEEVRLLLFSYNPQLRYMLHEESMLAVSYWSFFDDIQNIQQKEIKLINFKELNWPKGTYFVYTPFLVLAKHGGEIIARIQFAENGNLLLIELLIDGVLDKIMIFDDRGFVSSIKYFKQNRLIYQDYLNQNGVWQIREYASKFPRIVVNPMSDKVFNFTEYDDWDTLIRERILVLKKLEVTPDDYIIVAVNDIHNNLVRKSFPDQKKIFSFFGERYSFDNRLDFNELLDEGELFIAESEKIERLLITSLQEKNYSSNYVENHISRIPPFDTRLRLGQSQNIEELIAYLLVDDLSQTYLSEVLDQLLAKMEVNPSLELKIVSYKNDYDMTSLKEQVKDKILSSKNPDYFFTSLSLEDENHFKEEQKTKIRGISFDIYTNENQIIDALDTARLVIDLRDDPDLYTQIAALSSGIPQINKVHTNYVEHQKNGWIISDSTELNNAIDYYFDGLMNWNKSLVYSVKKMGDYTSGKILQRWRKLLEKE
Protein: Protein unc-13 homolog B (Munc13-2) (Q62769)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-depending refilling of readily releasable vesicle pool (RRP) (By similarity). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). In collaboration with UNC13A, facilitates neuronal dense core vesicles fusion as well as controls the location and efficiency of their synaptic release (By similarity).
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Cell membrane. Synapse. Note=Localized to synapses. Translocated to the plasma membrane in response to phorbol ester binding.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 1
- Protein unc-13 homolog C
- Regulating synaptic membrane exocytosis protein 2
- Ras-related protein Rab-3A
- Syntaxin-1A
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Protein bassoon
- Peripheral-type benzodiazepine receptor-associated protein 1
- Syntaxin-binding protein 1
Sequence:
MSLLCVRVKRAKFQGSPDKFNTYVTLKVQNVKSTTVAVRGDQPSWEQDFMFEISRLDLGLSVEVWNKGLIWDTMVGTVWIALKTIRQSDEEGPGEWSTLEAETLMKNDEICGTKNPTPHKILLGTRFELPFDIPEEEARYWTYKLEQINALADDNEYSSQEESQRKLLPTAAAQCRHWTYLGWGEHQTFEDPDSAVDDRDSDYRSETSNSAPPPYHTTTQPNASAHQFPMPVPLPQQLFLQGSSRDSCNDSMQSYDLDYPERRALSPTSSSRYGSSCNVSRGSSLLSELDQYHEQDDDGRERDSIHSSHSYGSLSRDGQAGLGEQEKALEVACESQKEKTGESKERDDATVCPPSDLMLHKDLTLGPQESFPEEKASSPFTQARAHWFRAVTKVRLQLQEISDDGDPSLPQWLPEGPAGGLYGIDSMPDLRRKKPLPLVSDLAMSLVQSRKAGITSAMATRTSLKDEDLKSHVYKKTLQALIYPISCTTPHNFEVWSATTPTYCYECEGLLWGLARQGMRCSECGVKCHEKCQDLLNADCLQRAAEKSSKHGAEDRTQNIIMAMKDRMKIRERNKPEIFEVIRDVFTVSKVAHVQQMKTVKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLQINVEIKGEEKVAPYHVQYTCLHENLFHYLTDIQGSGGVWIPDARGDDAWKVYFDETAQEIVDEFAMRYGIESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSTYRNNFPAGSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHDLYSHQYQLQEQPLEEPGPSIRNLDFWPKLITLIVSIIEEDKNSYTPVLNQFPQELNVGKVSAEVMWHLFAQDMKYALEEHEKDRLCKSADYMNLHFKVKWLHNEYVRELPALQGQVPEYPAWFEQFVLQWLDENEDVSLEFLRGGLERDKRDGFQQTSEHALFSCSVVDVFTQLNQSFEIIRKLECPDPSILAHYMRRFAKTIGKVLIQYADILSKNFPAYCTKERLPCILMNNMQQLRVQLEKMFEAMGGKELDSEAADSLKELQVKLNTVLDELSMVFGNSFQVRIDECVRQMADILGQVRGTGNASPNARASVAQDADSVLRPLMDFLDGNLTLFATVCEKTVLKRVLKELWRVVMNTMERVIVLPPLIDQTGTQLILTAAKELSQLSKLKDHMVREETRNLTPKQCAVLDLALDTVKQYFHAGGNGLKKTFLEKSPDLQSLRYALSLYTQTTDTLIKTFVRSQTAQVHDGKGIRFTANEDIRPEKGAGVDDPVGEVSIQVDLFTHPGTGEHKVTVKVVAANDLKWQTAGMFRPFVEVTMVGPHQSDKKRKFTTKSKSNSWTPKYNETFHFLLGNEEGPEAYELQICVKDYCFAREDRVIGLAVMPLRDVAAKGSCACWCPLGRKIHMDETGMTILRILSQRSNDEVAREFVKLKSESRSIEEGS
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (Chaperonin containing T-complex polypeptide 1 subunit 7) (HIV-1 Nef-interacting protein) [Cleaved into: T-complex protein 1 subunit eta, N-terminally processed] (Q99832)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P80313}.
Interaction partners:
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta-2
- Cell division cycle protein 20 homolog
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Sequence:
MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDAPTAAGRGRGRGRPH
Protein: Chlorophyll a-b binding protein 1, chloroplastic (Chlorophyll a-b protein 140) (CAB-140) (LHCII type I CAB-1) (P04778)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Interaction partners:
- Chlorophyll a-b binding protein CP26, chloroplastic
- Chlorophyll a-b binding protein CP29.1, chloroplastic
- Photosystem II CP43 reaction center protein
- Chlorophyll a-b binding protein
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Photosystem II reaction center W protein, chloroplastic
- Chlorophyll a-b binding protein 3, chloroplastic
- Photosystem II protein D1
- Expressed protein
- Photosystem II CP47 reaction center protein
Sequence:
MAASTMALSSPAFAGKAVKLSPAASEVLGSGRVTMRKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK
Protein: Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (E7E2N8)
Organism: Carassius auratus (Goldfish)
Function: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing.
Subcellular location: Secreted {ECO:0000305|PubMed:25447639}. Lysosome {ECO:0000269|PubMed:25447639}.
Interaction partners:
Sequence:
MFGFRLSVLLFAVCSLSACSCMFVNSCKYPPSQWCDSRDIAAQCGVLEQCMKFNASPVTVSLYYESLCPGCREFLVSQLVPTFIMLSDIMNIELVPYGNAQEKDDQGNYTFICQHGEDECRGNMIETCLLKALGPKAIPVIFCMESGADVLKAAQPCLGVYFPDTTWDSVMKCVTGDEGNKLMHQNALKTNALKPPHEYVPWITINGEHTDDLQDKATNSLFNLVCSLYKGEKPAACGQGLKKRTNSYCMN
Protein: RNA-binding protein, putative (Q387K0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSQQPQYYTTQQQPPQQQQQQAPPPSMGAMNQDLDLLRNLMVNYIPTTVDEVQLRQLFERFGPIESVKIVCDRETRQSRGYGFVKFQSASSAQQAIASLNGFVILNKRLKVALAASGHQRGRNMNNGFNAYGGYGGYGGYGAYPPVANPYAQQQMMAMQQHYMMAASPMPPISRQ
Protein: Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Protein AR1) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein) (Q9UGU0)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.
Subcellular location: Nucleus {ECO:0000269|PubMed:10995766}.
Interaction partners:
- Androgen receptor
- Albumin
Sequence:
MQSFREQSSYHGNQQSYPQEVHGSSRLEEFSPRQAQMFQNFGGTGGSSGSSGSGSGGGRRGAAAAAAAMASETSGHQGYQGFRKEAGDFYYMAGNKDPVTTGTPQPPQRRPSGPVQSYGPPQGSSFGNQYGSEGHVGQFQAQHSGLGGVSHYQQDYTGPFSPGSAQYQQQASSQQQQQQVQQLRQQLYQSHQPLPQATGQPASSSSHLQPMQRPSTLPSSAAGYQLRVGQFGQHYQSSASSSSSSSFPSPQRFSQSGQSYDGSYNVNAGSQYEGHNVGSNAQAYGTQSNYSYQPQSMKNFEQAKIPQGTQQGQQQQQPQQQQHPSQHVMQYTNAATKLPLQSQVGQYNQPEVPVRSPMQFHQNFSPISNPSPAASVVQSPSCSSTPSPLMQTGENLQCGQGSVPMGSRNRILQLMPQLSPTPSMMPSPNSHAAGFKGFGLEGVPEKRLTDPGLSSLSALSTQVANLPNTVQHMLLSDALTPQKKTSKRPSSSKKADSCTNSEGSSQPEEQLKSPMAESLDGGCSSSSEDQGERVRQLSGQSTSSDTTYKGGASEKAGSSPAQGAQNEPPRLNASPAAREEATSPGAKDMPLSSDGNPKVNEKTVGVIVSREAMTGRVEKPGGQDKGSQEDDPAATQRPPSNGGAKETSHASLPQPEPPGGGGSKGNKNGDNNSNHNGEGNGQSGHSAAGPGFTSRTEPSKSPGSLRYSYKDSFGSAVPRNVSGFPQYPTGQEKGDFTGHGERKGRNEKFPSLLQEVLQGYHHHPDRRYSRSTQEHQGMAGSLEGTTRPNVLVSQTNELASRGLLNKSIGSLLENPHWGPWERKSSSTAPEMKQINLTDYPIPRKFEIEPQSSAHEPGGSLSERRSVICDISPLRQIVRDPGAHSLGHMSADTRIGRNDRLNPTLSQSVILPGGLVSMETKLKSQSGQIKEEDFEQSKSQASFNNKKSGDHCHPPSIKHESYRGNASPGAATHDSLSDYGPQDSRPTPMRRVPGRVGGREGMRGRSPSQYHDFAEKLKMSPGRSRGPGGDPHHMNPHMTFSERANRSSLHTPFSPNSETLASAYHANTRAHAYGDPNAGLNSQLHYKRQMYQQQPEEYKDWSSGSAQGVIAAAQHRQEGPRKSPRQQQFLDRVRSPLKNDKDGMMYGPPVGTYHDPSAQEAGRCLMSSDGLPNKGMELKHGSQKLQESCWDLSRQTSPAKSSGPPGMSSQKRYGPPHETDGHGLAEATQSSKPGSVMLRLPGQEDHSSQNPLIMRRRVRSFISPIPSKRQSQDVKNSSTEDKGRLLHSSKEGADKAFNSYAHLSHSQDIKSIPKRDSSKDLPSPDSRNCPAVTLTSPAKTKILPPRKGRGLKLEAIVQKITSPNIRRSASSNSAEAGGDTVTLDDILSLKSGPPEGGSVAVQDADIEKRKGEVASDLVSPANQELHVEKPLPRSSEEWRGSVDDKVKTETHAETVTAGKEPPGAMTSTTSQKPGSNQGRPDGSLGGTAPLIFPDSKNVPPVGILAPEANPKAEEKENDTVTISPKQEGFPPKGYFPSGKKKGRPIGSVNKQKKQQQPPPPPPQPPQIPEGSADGEPKPKKQRQRRERRKPGAQPRKRKTKQAVPIVEPQEPEIKLKYATQPLDKTDAKNKSFYPYIHVVNKCELGAVCTIINAEEEEQTKLVRGRKGQRSLTPPPSSTESKALPASSFMLQGPVVTESSVMGHLVCCLCGKWASYRNMGDLFGPFYPQDYAATLPKNPPPKRATEMQSKVKVRHKSASNGSKTDTEEEEEQQQQQKEQRSLAAHPRFKRRHRSEDCGGGPRSLSRGLPCKKAATEGSSEKTVLDSKPSVPTTSEGGPELELQIPELPLDSNEFWVHEGCILWANGIYLVCGRLYGLQEALEIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLHEENFSVRCPKHKPPLPCPLPPLQNKTAKGSLSTEQSERG
Protein: GLABROUS1 enhancer-binding protein-like 1 (Protein GPL1) (Storekeeper-like protein At2g25650) (Q8VYD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. May play redundant roles with GEBP and GPL2 in cytokinin responses by regulating the transcript levels of type-A ARR response genes. Involved in stress responses. Plays a repressive role in cell expansion by counteracting the positive role of CPR5 in this process, but does not regulate cell proliferation or endoreduplication.
Subcellular location: Nucleus {ECO:0000269|PubMed:18162594}.
Interaction partners:
- F-box/kelch-repeat protein At1g67480
- E3 ubiquitin-protein ligase ATL59
- Pectin acetylesterase 3
- Secretory carrier-associated membrane protein 1
- Lysine-rich arabinogalactan protein 18
- F-box protein VBF
- Protein NRT1/ PTR FAMILY 8.1
- Protein CPR-5
Sequence:
MVTPKQIDFSSCGGGDNSDDTLSHRESPRNPSSKRAAASFAAEAGEETMKKKKKKKKKNLGPPLIVRIWNEEDELSILKGLVDYRAKTGFNPKIDWDAFYSFLGSSIVAKFSKEQVLSKIRKLKRRFHVHWEKISEGNDPKFTRSSDSEAFGFSSMIWGQGEFGNDDGMDKEMVKEHDVNGNGAAENGTARIAQENESGEEMLKEHEETLNENGAEEIRDNDETARKAQQLESESEEEMLKEHEEPFNENGAENIRDNNGTTQIAQQSESESEEMLKEHEEVANTELVNENGAAKTTENGTTGGKERHDDDDDDELCAVQDAFEAVMSQGLSGYQKKLQLEKLMNLGTGKRRELSDEWKALCVEERRLNIKKLRFSAKLAEAANDS
Protein: Transforming acidic coiled-coil containing protein 1 (E5RJU4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEA
Protein: Oligodendrocyte-myelin glycoprotein (Q63912)
Organism: Mus musculus (Mouse)
Function: Cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Paired immunoglobulin-like receptor B
- Reticulon-4 receptor
- Myelin-associated glycoprotein
- Reticulon-4
- Tumor necrosis factor receptor superfamily member 16
- Tumor necrosis factor receptor superfamily member 19
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- Transforming protein RhoA
- Receptor-type tyrosine-protein phosphatase S
Sequence:
MEYQILKMSSCLFILLFLTPGILCICPLQCTCTERHRHVDCSGRNLTTLPPGLQENIIHLNLSYNHFTDLHNQLTPYTNLRTLDISNNRLESLPAQLPRSLWNMSAANNNIKLLDKSDTAYQWNLKYLDVSKNMLEKVVLIKNTLRSLEVLNLSSNKLWTVPTNMPSKLHIVDLSNNSLTQILPGTLINLTNLTHLYLHNNKFTFIPEQSFDQLLQLQEITLHNNRWSCDHKQNITYLLKWVMETKAHVIGTPCSKQVSSLKEQSMYPTPPGFTSSLFTMSEMQTVDTINSLSMVTQPKVTKTPKQYRGKETTFGVTLSKDTTFSSTDRAVVAYPEDTPTEMTNSHEAAAATLTIHLQDGMSSNASLTSATKSPPSPVTLSIARGMPNNFSEMPRQSTTLNLRREETTANGNTRPPSAASAWKVNASLLLMLNAVVMLAG
Protein: Urease accessory protein UreG (Q09066)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}.
Interaction partners:
- Urease accessory protein UreH
- Urease accessory protein UreF
- Urease accessory protein UreE
- Urease subunit alpha
- Urease subunit beta
- Acid-activated urea channel
- Phosphoglucosamine mutase
- Hydrogenase/urease maturation factor HypA
- FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
- Hydrogenase expression/formation protein
Sequence:
MVKIGVCGPVGSGKTALIEALTRHMSKDYDMAVITNDIYTKEDAEFMCKNSVMPRERIIGVETGGCPHTAIREDASMNLEAVEEMHGRFPNLELLLIESGGDNLSATFNPELADFTIFVIDVAEGDKIPRKGGPGITRSDLLVINKIDLAPYVGADLKVMERDSKKMRGEKPFIFTNIRAKEGLDDVIAWIKRNALLED
Protein: NAD-capped RNA hydrolase NUDT12 (DeNADding enzyme NUDT12) (EC 3.6.1.-) (NADH pyrophosphatase NUDT12) (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 12) (Nudix motif 12) (Q9DCN1)
Organism: Mus musculus (Mouse)
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to nutrient stress. Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP (By similarity). May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BQG2}. Peroxisome {ECO:0000250|UniProtKB:Q9BQG2}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9BQG2}. Note=Localizes to cytoplasmic granules in the presence of BLMH. {ECO:0000250|UniProtKB:Q9BQG2}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- Nicotinamide riboside kinase 1
- Cytosolic purine 5'-nucleotidase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Glutamine-dependent NAD
- NAD kinase 2, mitochondrial
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MSSVKRNPKKEMISELHSSAAEGNVAKLAGILSHSPSLLNETSENGWTALMYAARNGHPDVVQFLLEKGCDRSLVNKARQTALDIAAFWGYRHIANLLANAKGGKKPWFLTNEVDECENYFSRTLLDRRSDKRNNSDWLQAKESHPTTVYLLFSDLNPLVTLGGNKESSQQPEVRLCQLNYPDVKGYLAQPEKITLVFLGVELEMRKGSPAQAGGVPEEEEDGLVAWFALGIEPGAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGSATKIEEGGYKRVCVRETCPSLQGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVSCQPWPMPSSLMIGCLAVAVSTEIKVDKNEIEDARWFTREQVVDVLTKGKQQAFFVPPSRAIAHQLIKHWVGMNPNL
Protein: Phthiocerol dimycocerosate exporter MmpL7 (P9WJU7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for export of phthiocerol dimycocerosate (PDIM) to the cell wall. Essential for normal replication during the active-growth phase of the murine tuberculosis model.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:10573420}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative phthiocerol dimycocerosate transporter LppX
- Long-chain-fatty-acid--AMP ligase FadD28
- Phenolphthiocerol/phthiocerol polyketide synthase subunit E
- Trehalose-2-sulfate acyltransferase PapA2
- Probable doxorubicin resistance ABC transporter permease protein DrrC
- Uncharacterized PPE family protein PPE42
- Uncharacterized PPE family protein PPE54
- PPE family protein PPE34
- 2'-acyl-2-O-sulfo-trehalose
- PPE family protein PPE8
Sequence:
MPSPAGRLHRIRYIRLKKSSPDCRATITSGSADGQRRSPRLTNLLVVAAWVAAAVIANLLLTFTQAEPHDTSPALLPQDAKTAAATSRIAQAFPGTGSNAIAYLVVEGGSTLEPQDQPYYDAAVGALRADTRHVGSVLDWWSDPVTAPLGTSPDGRSATAMVWLRGEAGTTQAAESLDAVRSVLRQLPPSEGLRASIVVPAITNDMPMQITAWQSATIVTVAAVIAVLLLLRARLSVRAAAIVLLTADLSLAVAWPLAAVVRGHDWGTDSVFSWTLAAVLTIGTITAATMLAARLGSDAGHSAAPTYRDSLPAFALPGACVAIFTGPLLLARTPALHGVGTAGLGVFVALAASLTVLPALIALAGASRQLPAPTTGAGWTGRLSLPVSSASALGTAAVLAICMLPIIGMRWGVAENPTRQGGAQVLPGNALPDVVVIKSARDLRDPAALIAINQVSHRLVEVPGVRKVESAAWPAGVPWTDASLSSAAGRLADQLGQQAGSFVPAVTAIKSMKSIIEQMSGAVDQLDSTVNVTLAGARQAQQYLDPMLAAARNLKNKTTELSEYLETIHTWIVGFTNCPDDVLCTAMRKVIEPYDIVVTGMNELSTGADRISAISTQTMSALSSAPRMVAQMRSALAQVRSFVPKLETTIQDAMPQIAQASAMLKNLSADFADTGEGGFHLSRKDLADPSYRHVRESMFSSDGTATRLFLYSDGQLDLAAAARAQQLEIAAGKAMKYGSLVDSQVTVGGAAQIAAAVRDALIHDAVLLAVILLTVVALASMWRGAVHGAAVGVGVLASYLAALGVSIALWQHLLDRELNALVPLVSFAVLASCGVPYLVAGIKAGRIADEATGARSKGAVSGRGAVAPLAALGGVFGAGLVLVSGGSFSVLSQIGTVVVLGLGVLITVQRAWLPTTPGRR
Protein: G-rich sequence factor 1 (GRSF-1) (Q12849)
Organism: Homo sapiens (Human)
Function: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences. Involved in the degradosome-mediated decay of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. Acts by unwinding G-quadruplex RNA structures in MT-ncRNA, thus facilitating their degradation by the degradosome. G-quadruplexes (G4) are non-canonical 4 stranded structures formed by transcripts from the light strand of mtDNA.
Subcellular location: [Isoform 1]: Mitochondrion matrix {ECO:0000269|PubMed:23473033, ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:25683715, ECO:0000269|PubMed:29967381}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000269|PubMed:23473033, ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:25683715}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:23473034}.
Interaction partners:
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- ATP-dependent RNA helicase DHX30
- FAST kinase domain-containing protein 2
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
- Probable ATP-dependent RNA helicase DDX28
- tRNA methyltransferase 10 homolog C
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Poly
- rRNA methyltransferase 3, mitochondrial
- FAST kinase domain-containing protein 5
Sequence:
MAGTRWVLGALLRGCGCNCSSCRRTGAACLPFYSAAGSIPSGVSGRRRLLLLLGAAAAAASQTRGLQTGPVPPGRLAGPPAVATSAAAAAAASYSALRASLLPQSLAAAAAVPTRSYSQESKTTYLEDLPPPPEYELAPSKLEEEVDDVFLIRAQGLPWSCTMEDVLNFFSDCRIRNGENGIHFLLNRDGKRRGDALIEMESEQDVQKALEKHRMYMGQRYVEVYEINNEDVDALMKSLQVKSSPVVNDGVVRLRGLPYSCNEKDIVDFFAGLNIVDITFVMDYRGRRKTGEAYVQFEEPEMANQALLKHREEIGNRYIEIFPSRRNEVRTHVGSYKGKKIASFPTAKYITEPEMVFEEHEVNEDIQPMTAFESEKEIELPKEVPEKLPEAADFGTTSSLHFVHMRGLPFQANAQDIINFFAPLKPVRITMEYSSSGKATGEADVHFETHEDAVAAMLKDRSHVHHRYIELFLNSCPKGK
Protein: DnaJ homolog subfamily C member 14 (DnaJ protein homolog 3) (Dopamine receptor-interacting protein of 78 kDa) (DRIP78) (Human DnaJ protein 3) (hDj-3) (Q6Y2X3)
Organism: Homo sapiens (Human)
Function: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- D
- SAP domain-containing ribonucleoprotein
- Calnexin
Sequence:
MAQKHPGERGLYGAHHSGGASLRTLGPSVDPEIPSFSGLRDSAGTAPNGTRCLTEHSGPKHTQHPNPAHWLDPSHGPPGGPGPPRDAEDPDQSETSSEEESGVDQELSKENETGNQKDGNSFLSIPSACNCQGTPGIPEGPYSEGGNGSSSNFCHHCTSPALGEDELEEEYDDEESLKFPSDFSRVSSGKKPPSRRQRHRFPTKEDTREGGRRDPRSPGRHRLGRKRSQADKRKGLGLWGAEELCQLGQAGFWWLIELLVLVGEYVETCGHLIYACRQLKSSDLDLFRVWMGVWTGRLGGWAQVMFQFLSQGFYCGVGLFTRFLKLLGALLLLALALFLGFLQLGWRFLVGLGDRLGWRDKATWLFSWLDSPALQRCLTLLRDSRPWQRLVRIVQWGWLELPWVKQNINRQGNAPVASGRYCQPEEEVARLLTMAGVPEDELNPFHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENELSRSVNEFLSKLQDDLKEAMNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQRVGISPDTHRVPYHISFGSRIPGTRGRQRATPDAPPADLQDFLSRIFQVPPGQMPNGNFFAAPQPAPGAAAASKPNSTVPKGEAKPKRRKKVRRPFQR