wanglab/gogpt-training-data huggingface dataset:
Protein: U3 small nucleolar ribonucleoprotein protein IMP3 (U3 snoRNP protein IMP3) (BRMS2) (Q9NV31)
Organism: Homo sapiens (Human)
Function: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:34516797}.
Interaction partners:
- KRR1 small subunit processome component homolog
- Something about silencing protein 10
- U3 small nucleolar ribonucleoprotein protein MPP10
- U3 small nucleolar ribonucleoprotein protein IMP4
- U3 small nucleolar RNA-associated protein 6 homolog
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS6
- WD repeat-containing protein 46
- Neuroguidin
- U3 small nucleolar RNA-interacting protein 2
Sequence:
MVRKLKFHEQKLLKQVDFLNWEVTDHNLHELRVLRRYRLQRREDYTRYNQLSRAVRELARRLRDLPERDQFRVRASAALLDKLYALGLVPTRGSLELCDFVTASSFCRRRLPTVLLKLRMAQHLQAAVAFVEQGHVRVGPDVVTDPAFLVTRSMEDFVTWVDSSKIKRHVLEYNEERDDFDLEA
Protein: Protein O-mannosyl-transferase 1 (EC 2.4.1.109) (F1QF89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6A1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Fukutin.
- Ribitol-5-phosphate transferase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannosyl-transferase 2
- Protein O-mannose kinase
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Ribitol-5-phosphate xylosyltransferase 1
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol-phosphate mannosyltransferase subunit 3
Sequence:
MQCVKLPVSVTVEINVLLLAVTALALFTRLYGIHFPKAVVFDEVYYGQFLSLYMKQVFFIDESGPPFGHMILALGAYLGGFDGNFVWNRIGAEYPGNVPVWSLRLIPALAGSFCVPLAYLVVVELGYSHFSALGACALLLMENSLIVQSRFMLLESVLIFFLLLAVLSYLRFHKARNSFFKWFWLVICGVSCAFGIGVKYMGMFTYFLLLSLAAVHTWQLIGDQTLSHGKVMFQVLVRFLALVVLPVIMYLGFFYIHLTLLYRSGPHDQMMSSAFQASLEGGLARITQGQPLDVAFGSQVTLRTVSGKPVPCWLHSHKANYPIRYENGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQSLVVSSPPKPVRHGDIIQLLHGMTTRYLNTHDVAAPMSPHSQEVSGYIDFNVSMPAQNLWRVDIVNRESEKEIWKTILSEVRLVHVNTSAVLKLSGASLPEWGFKQLEVVGDKIYKGYQQTGMWNVEEHRYGRSQEPKERELELKSPTHSDVNKNLTFMAKFLELQWKMLTVKNEESEHKYSSSPLEWITMDTNIAYWLHPSSNAQIHFIGNIVTWTTGNITLVVYCLLFLTYLLRRRRKVEDIPQDSWEQLVLAGVVCLGGWAVNYLPFFLMEKTLFLYHYLPALTFKILQIPIVTEHLYIHVLRSSAQQKAFGGVILAVLCSVYMSYHSLSPLTYGQPALTSDKLAELRWRESWDILLRKR
Protein: Arabinogalactan protein 4 (B1NHU2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MAITKQHLIPLFAISFLLFSQLHCSTTSAQAPAQSPAPPGPPDVAKILQKAGQYSVFVRLLKSTQVSDRLIGELKDTDDGKTIFAPTDKAFSALKSGALNSLNDEQRVQLVLFHVVPDYIPFSQFQTVSNPMRTQAGDSGDGEFPLNVTTSGNTVVLKTGLMKTSVSGTIYTDGQLAVYRVDQVLQPLQVFAARSSALAPAPGMSRKAADVDGNSKASSLAMQNLALFVVSVIAFALSL
Protein: Atlastin-1 (EC 3.6.5.-) (Brain-specific GTP-binding protein) (GTP-binding protein 3) (GBP-3) (hGBP3) (Guanine nucleotide-binding protein 3) (Spastic paraplegia 3 protein A) (Q8WXF7)
Organism: Homo sapiens (Human)
Function: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:19665976}. Golgi apparatus membrane {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum tubular network (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
Interaction partners:
- Spastin
- Receptor expression-enhancing protein 1
- Magnesium transporter NIPA1
- Reticulon-1
- Reticulon-2
- Receptor expression-enhancing protein 5
- Spartin
- Reticulon-4
- Protrudin
- ADP-ribosylation factor-like protein 6-interacting protein 1
Sequence:
MAKNRRDRNSWGGFSEKTYEWSSEEEEPVKKAGPVQVLIVKDDHSFELDETALNRILLSEAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEIFLINKPDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPESLDIKEINGNKITCRGLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEICGGDKPFLAPNDLQTKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLYHQAFPTPKSESTEQSEKKKM
Protein: Isopentenyl-diphosphate Delta-isomerase II, chloroplastic (EC 5.3.3.2) (Isopentenyl pyrophosphate isomerase II) (IPP isomerase II) (Q42553)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Hydroxymethylglutaryl-CoA synthase
- Farnesyl pyrophosphate synthase 2
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Isopentenyl phosphate kinase
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Solanesyl diphosphate synthase 3, chloroplastic/mitochondrial)
- Acetyl-CoA acetyltransferase 1
Sequence:
MSASSLFNLPLIRLRSLALSSSFSSFRFAHRPLSSISPRKLPNFRAFSGTAMTDTKDAGMDAVQRRLMFEDECILVDETDRVVGHDSKYNCHLMENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRESELIQDNALGVRNAAQRKLLDELGIVAEDVPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYVSREELKELVKKADAGEEGLKLSPWFRLVVDNFLMKWWDHVEKGTLVEAIDMKTIHKL
Protein: Pluripotency associated transcript 25 (A0A1Y7VJU7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLETYRNLIAIGFNWDDKNIEEHCQSFGRHTRHERIQSAEKPSEYTQGGKAFALHAHSHAQRHERIHREKKPHGVIQFVEAFAQHSLQLRKRVQTGKKLYEWKQCGKAFEDHSHLKSYEGILMGEKPYECHQWEKAFSSHSNLLQPKGRHTGEKCYECDLCGKAFSQHSRLKRHGRIHTGEKPYKCDQCGKAFSEHCNLQKHKRIHTGEKPYKCHQCDKAFSQHHSLQKHKRIHTGEKPYKCNECDKVFRQSSDLQKHRRIHTGEKPYKCNQCDKAFSQHHSLQIHKRTHTGEKPYKCNQCDKVFSRHSTLQIHIRIHAGEKPFKCNECEKAFSQHSNLQSHRRIHTGKKPYKCNECEKAFSQHSNLQSHRRIHTGKKPYKCNTCEKAFSKHSILHSHRRIHTGEKSYKCNHCEKVFLGHYDLQRHKGIHTG
Protein: Ubiquitin-associated protein 2 (UBAP-2) (RNA polymerase II degradation factor UBAP2) (Q5T6F2)
Organism: Homo sapiens (Human)
Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled nucleotide excision repair (TC-NER) machinery fails to resolve DNA damage. May promote the degradation of ANXA2.
Subcellular location: Nucleus {ECO:0000269|PubMed:35633597}. Chromosome {ECO:0000269|PubMed:35633597}. Cytoplasm {ECO:0000269|PubMed:27121050, ECO:0000269|PubMed:35633597}. Note=Associates with nuclear chromatin. {ECO:0000269|PubMed:35633597}.
Interaction partners:
- Cyclin-dependent kinase 12
Sequence:
MMTSVSSDHCRGAREKPQISAAQSTQPQKQVVQATAEQMRLAQVIFDKNDSDFEAKVKQLMEVTGKNQDECIVALHDCNGDVNKAINILLEGNSDTTSWETVGCKKKNFAKENSENKENREKKSEKESSRGRGNNNRKGRGGNRGREFRGEENGIDCNQVDKPSDRGKRARGRGFGRGRGRGAGRFSTQGMGTFNPADYSDSTSTDVCGTKLVVWEAAQNGADEGTELASNTHNIAQDLSNKSSYGLKGAWKNSVEEWTTEDWTEDLSETKVFTASSAPAENHILPGQSIDLVALLQKPVPHSQASEANSFETSQQQGFGQALVFTNSQHNNQMAPGTGSSTAVNSCSPQSLSSVLGSGFGELAPPKMANITSSQILDQLKAPSLGQFTTTPSTQQNSTSHPTTTTSWDLKPPTSQSSVLSHLDFKSQPEPSPVLSQLSQRQQHQSQAVTVPPPGLESFPSQAKLRESTPGDSPSTVNKLLQLPSTTIENISVSVHQPQPKHIKLAKRRIPPASKIPASAVEMPGSADVTGLNVQFGALEFGSEPSLSEFGSAPSSENSNQIPISLYSKSLSEPLNTSLSMTSAVQNSTYTTSVITSCSLTSSSLNSASPVAMSSSYDQSSVHNRIPYQSPVSSSESAPGTIMNGHGGGRSQQTLDTPKTTGPPSALPSVSSLPSTTSCTALLPSTSQHTGDLTSSPLSQLSSSLSSHQSSLSAHAALSSSTSHTHASVESASSHQSSATFSTAATSVSSSASSGASLSSSMNTANSLCLGGTPASASSSSSRAAPLVTSGKAPPNLPQGVPPLLHNQYLVGPGGLLPAYPIYGYDELQMLQSRLPVDYYGIPFAAPTALASRDGSLANNPYPGDVTKFGRGDSASPAPATTPAQPQQSQSQTHHTAQQPFVNPALPPGYSYTGLPYYTGMPSAFQYGPTMFVPPASAKQHGVNLSTPTPPFQQASGYGQHGYSTGYDDLTQGTAAGDYSKGGYAGSSQAPNKSAGSGPGKGVSVSSSTTGLPDMTGSVYNKTQTFDKQGFHAGTPPPFSLPSVLGSTGPLASGAAPGYAPPPFLHILPAHQQPHSQLLHHHLPQDAQSGSGQRSQPSSLQPKSQASKPAYGNSPYWTN
Protein: Guanylate cyclase soluble subunit alpha-2 (GCS-alpha-2) (EC 4.6.1.2) (P33402)
Organism: Homo sapiens (Human)
Function: Has guanylyl cyclase on binding to the beta-1 subunit.
Subcellular location: Cytoplasm.
Interaction partners:
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit alpha-1
- cGMP-dependent protein kinase 2
- cGMP-dependent protein kinase 1
- Nitric oxide synthase 1
- Inosine triphosphate pyrophosphatase
- Pyruvate kinase PKM
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Bis
Sequence:
MSRRKISSESFSSLGSDYLETSPEEEGECPLSRLCWNGSRSPPGPLEPSPAAAAAAAAPAPTPAASAAAAAATAGARRVQRRRRVNLDSLGESISRLTAPSPQTIQQTLKRTLQYYEHQVIGYRDAEKNFHNISNRCSYADHSNKEEIEDVSGILQCTANILGLKFEEIQKRFGEEFFNICFHENERVLRAVGGTLQDFFNGFDALLEHIRTSFGKQATLESPSFLCKELPEGTLMLHYFHPHHIVGFAMLGMIKAAGKKIYRLDVEVEQVANEKLCSDVSNPGNCSCLTFLIKECENTNIMKNLPQGTSQVPADLRISINTFCRAFPFHLMFDPSMSVLQLGEGLRKQLRCDTHKVLKFEDCFEIVSPKVNATFERVLLRLSTPFVIRTKPEASGSENKDKVMEVKGQMIHVPESNSILFLGSPCVDKLDELMGRGLHLSDIPIHDATRDVILVGEQAKAQDGLKKRMDKLKATLERTHQALEEEKKKTVDLLYSIFPGDVAQQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPMQVISMLNELYTRFDHQCGFLDIYKVETIGDAYCVAAGLHRKSLCHAKPIALMALKMMELSEEVLTPDGRPIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSPTTYQLLKREESFTFIPRSREELPDNFPKEIPGICYFLEVRTGPKPPKPSLSSSRIKKVSYNIGTMFLRETSL
Protein: Myogenic factor 6 (Myf-6) (Muscle-specific regulatory factor 4) (Q6VNZ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Paired box 7a
- Paired box 3a
- Myocyte enhancer factor 2aa
- Growth/differentiation factor 8
- Transcription factor 12
- Myocyte enhancer factor 2ca
- Myosin, light chain 1, alkali; skeletal, fast
- Protein myomaker
- Homeobox protein six1b
- Myogenic factor.
Sequence:
MMDLFETNAYFFNDLRYLEGDHGTLDMPGVSPLYEGNDSPLSPGQDPVPSETGCESSGEEHVLAPPGLQAHCEGQCLMWACKICKRKSAPTDRRKAATLRERRRLKKINEAFDALKKKTVPNPNQRLPKVEILRSAINYIEKLQDLLHSLDEQEQSNDTDPYTYNLKENHVTPSEYHWKKTCQSWQENPDHSSSQMAGHREGAVLESSESSSLRRLSSIVDSISTEEPKARCPSQISEK
Protein: PMS1 homolog 2, mismatch repair system component (C9J167)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWGRRRKLRRLNDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKEFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQLGQGKRQPVVCTGGSPSIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYGLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYHMYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDVNKLNVSQQPLLDVEGNLIKMHAADLEKPMVEKQDQSPSLRTGEEKKDVSISRLREAFSLRHTTENKPHSPKTPEPRRSPLGQKRGMLSSSTSGAISDKGVLRPQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTGCKFRVLPQPTNLATPNTKRFKKEEILSSSDICQKLVNTQDMSASQVDVAVKINKKVVPLDFSMSSLAKRIKQLHHEAQQSEGEQNYRKFRAKICPGENQAAEDELRKEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDENAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHIANLGVISQN
Protein: Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26) (P35508)
Organism: Bos taurus (Bovine)
Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
Interaction partners:
- Cryptochrome-1
- Period circadian protein homolog 2
- PAS domain-containing protein
- Protein LTV1 homolog
- histone acetyltransferase
- Neuronal PAS domain protein 2
- Aryl hydrocarbon receptor nuclear translocator like
- Period circadian regulator 1
- Glycogen synthase kinase-3 beta
- Bystin
Sequence:
MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
Protein: Sodium-coupled neutral amino acid transporter 3 (N-system amino acid transporter 1) (Na(+)-coupled neutral amino acid transporter 3) (Solute carrier family 38 member 3) (System N amino acid transporter 1) (Q99624)
Organism: Homo sapiens (Human)
Function: Symporter that cotransports specific neutral amino acids and sodium ions, coupled to an H(+) antiporter activity. Mainly participates in the glutamate-GABA-glutamine cycle in brain where it transports L-glutamine from astrocytes in the intercellular space for the replenishment of both neurotransmitters glutamate and gamma-aminobutyric acid (GABA) in neurons and also functions as the major influx transporter in ganglion cells mediating the uptake of glutamine (By similarity). The transport activity is specific for L-glutamine, L-histidine and L-asparagine. The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (By similarity). The transport is pH dependent, saturable, Li(+) tolerant and functions in both direction depending on the concentration gradients of its substrates and cotransported ions. Also mediates an amino acid-gated H(+) conductance that is not stoichiometrically coupled to the amino acid transport but which influences the ionic gradients that drive the amino acid transport (By similarity). In addition, may play a role in nitrogen metabolism, amino acid homeostasis, glucose metabolism and renal ammoniagenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9DCP2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9DCP2}. Note=The localization appears to be basolateral in the plasma membrane of hepatocytes surrounding the central vein. Localized at the cerebrospinal fluid (CSF)-facing membrane of the choroid plexus epithelial cells. In astrocytes, the localization at cell membrane is decreased by ammonia through the PKC signaling. Expressed in both luminal and abluminal plasma membranes of larger microvessels and blood brain barrier (BBB) capillaries (By similarity). Restricted to the basolateral membranes of S3 segment cells of the proximal tubules (By similarity). {ECO:0000250|UniProtKB:Q9DCP2, ECO:0000250|UniProtKB:Q9JHZ9}.
Interaction partners:
- Sodium-coupled neutral amino acid transporter 5
- Sodium channel protein type 11 subunit alpha
- Excitatory amino acid transporter 1
- Vesicular inhibitory amino acid transporter
Sequence:
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFTDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKSSGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEEKTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPCPLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCHPEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVDPFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINLLVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFLLMTMSLSFIIIDWASGTSRHGGNH
Protein: Rgs20 protein (B1H233)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRTANGGPRAGASPSASPEDPNLPVESEQTEMRMRQMCSGSETQGSVPSQQQGVGGRGSNACCFCWCCCCSCSCLTVRNQEDQRPQRAAHELRTDIPACEESPMPTLEEVCAWAQSFDNLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKREANKSTIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVDPSQHIFDDAQLQIYTLMHRDSYPRFMNSTVYKDLLESLAEKAVEA
Protein: Bifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT (EC 3.6.1.29) (Adenosine 5'-monophosphoramidase FHIT) (EC 3.9.1.-) (Adenylylsulfatase) (EC 3.6.2.1) (Adenylylsulfate-ammonia adenylyltransferase) (EC 2.7.7.51) (Fragile histidine triad protein) (F4KEV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses dinucleoside triphosphate hydrolase activity. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate. Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate.
Interaction partners:
- Adenylate kinase 3
- GATA transcription factor 6
- Tapetal oleosin GRP-19
- Alkyl transferase
- AT3g53990
- Aspartic proteinase A2
- TATA-box-binding protein 2
- Adenylate kinase 4
Sequence:
MLNLQVTGKTILSSIRCQRKMSSTCSSYAFGPYKIDPREVFYATPLSYAMVNLRPLLPAHVLVCPRRLVPRFTDLTADETSDLWLTAQKVGSKLETFHNASSLTLAIQDGPQAGQTVPHVHIHILPRKGGDFEKNDEIYDALDEKEKELKQKLDLDKDRVDRSIQEMADEASQYRSLFDC
Protein: Protein-export membrane protein SecG (A0A0H2UPV5)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU365087}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU365087}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYNLLLTILLVLSVVIVIAIFMQPTKNQSSNVFDASSGDLFERSKARGFEAVMQRLTGILVFFWLAIALALTVLSSR
Protein: 10 kDa chaperonin, mitochondrial (Chaperonin 10) (CPN10) (Protein groES) (P34893)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seems to function only as a co-chaperone, along with CPN60, and in certain cases is essential for the discharge of biologically active proteins from CPN60.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9011092}.
Interaction partners:
- Chaperonin CPN60, mitochondrial
- Heat shock 70 kDa protein 4
- Chaperonin 60 subunit beta 1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase
- GrpE protein homolog
- Heat shock protein 90-2
- Heat shock 70 kDa protein 14
- Large ribosomal subunit protein uL11z
- Calmodulin-interacting protein 111
- At2g18210
Sequence:
MMKRLIPTFNRILVQRVIQPAKTESGILLPEKSSKLNSGKVIAVGPGSRDKDGKLIPVSVKEGDTVLLPEYGGTQVKLGENEYHLFRDEDVLGTLHED
Protein: Inner membrane protein YgaZ (P76630)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YgaH
- Uncharacterized protein YbaP
Sequence:
MESPTPQPAPGSATFMEGCKDSLPIVISYIPVAFAFGLNATRLGFSPLESVFFSCIIYAGASQFVITAMLAAGSSLWIAALTVMAMDVRHVLYGPSLRSRIIQRLQKSKTALWAFGLTDEVFAAATAKLVRNNRRWSENWMIGIAFSSWSSWVFGTVIGAFSGSGLLQGYPAVEAALGFMLPALFMSFLLASFQRKQSLCVTAALVGALAGVTLFSIPVAILAGIVCGCLTALIQAFWQGAPDEL
Protein: Serine/threonine-protein kinase fray1 (EC 2.7.11.1) (STE20-like kinase fray1) (Q54XL6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- J domain-containing protein
- Protein transport protein Sec61 subunit gamma
- Protein transport protein Sec61 subunit beta
Sequence:
MEINNSNNNNNYVCAQHNRIEHANHHDLPDSDSDSSSREEELMNSSGGGNGKEPIGEKKKLPSHISEVISNERRESIIRELQQIKTISDYPSQANQYNLIEPIGEGTEGRVFKAYCIPLKENVAIKVVELDKMDPQFVKDVIKEVKVMNGNNHPNLIHYHTSFLENNQLWLVMDYLGGGSLADIMKFKYPDGIPEVLAVTVLKSLLKGLEYLHSHQRIHRDLKSDNILIGEDGAIELADFGVSAMFEKNTCCSRKTIVGTPCWMAPEIISERGYNQGVDIWSFGITAIELIRGKPPGYDLPPSKVFMNLLFGNSPSLQEEEDKGVCSHLYKDLVDKCLQKEPSKRPNASKLLEHKVFKQAKKNNYIVSHLLHGLTPCEDRYRESMSPASSNTPSPDSSRPSSPEHYNHGNVVNSPLQKNIKPSSLNKSSSSLELKNKNLSNPDLVNMPRAASHPVELNALELSSGSGPLSQSSDLPHGHLHKIGTPKKKHSPSGSIGDSHGSISPPLSTSPEKERKKGFFNHFRRHSIAKLFGSPKEGDHNHQHHKSEGDHEHHHFHFPWKHHHHSSSNNHVET
Protein: Transcriptional regulator MraZ (P22186)
Organism: Escherichia coli (strain K12)
Function: Negatively regulates its own expression and that of the subsequent genes in the proximal part of the division and cell wall (dcw) gene cluster. Acts by binding directly to DNA. May also regulate the expression of genes outside the dcw cluster.
Subcellular location: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_01008, ECO:0000269|PubMed:24659771}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase H
- Cell division protein FtsL
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Peptidoglycan D,D-transpeptidase FtsI
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Cell division protein FtsA
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Cell division protein FtsQ
Sequence:
MFRGATLVNLDSKGRLSVPTRYREQLLENAAGQMVCTIDIYHPCLLLYPLPEWEIIEQKLSRLSSMNPVERRVQRLLLGHASECQMDGAGRLLIAPVLRQHAGLTKEVMLVGQFNKFELWDETTWHQQVKEDIDAEQLATGDLSERLQDLSL