wanglab/gogpt-training-data huggingface dataset:
Protein: POU domain, class 2, transcription factor 1 (Octamer-binding protein 1) (Oct-1) (XOct1) (Octamer-binding transcription factor 1) (OTF-1) (Xloct1-32) (P16143)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes of some small nuclear RNAs (snRNA) and histone H2B. In vitro does not bind to variant octamer sequences, such as the H2B octamer 5'-GTTTGCAT-3', although binding has been observed in vivo during early embryogenesis, suggesting that interactions between pou2f1 and other factors might be required for octamer-dependent H2B transcription. Acts downstream of Notch signaling during radial glia formation. May be important for gastrulation, possibly through the regulation of an FGF-type signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2017364}. Nucleus {ECO:0000269|PubMed:2017364, ECO:0000269|PubMed:7542467}. Note=Retained in the cytoplasm during early development, then gradually translocates to the nucleus around the mid-blastula transition (MBT).
Interaction partners:
Sequence:
MKLHSSSKIQNHAWLSDARMNNPSETSKSPESGDGNTGTQTNGLDFQKQAVPIGAITSAQAQALLGHLHQVQLAGTSLQAAAHSLNVQTKFKEEPGEPMQVVQPSQQPSLQAAIPQTQLMVAGGQIAGLTLTPAQQQMLLQQAQAQLLAAAVQHSASQQHNAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQYVLVHPTTNLQSAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPVQQLPQSQTTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENITSDSTLTNQSVLNSPGHGMEGLNRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGSSSSPIKSLFSSPNPLVASTPSLVTSSPATTLTVNPVLPLTSAAAITSFHIPGTTGTSSANTATVISTAPPVSSVLTSPSLSSSPSATAASSEASTAGETSTTQTTSTPMTSSLNTGQVMVTASGIHTAAATALQGAAQLPTNASLAAMAAAAGLNPGLMAPSQFAAGGALFSLNPGALGSALSPALMSNSTLATIQALASSGSLPITSLDAAGNLVFANAGGTPNIVTAPLFLNPQNLSLFTSNPVSLISAASAGATGPITSLHATTSSIDSIQNALFTMASASGAASTTTSASKAQ
Protein: F-box protein YDR306C (Q06640)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity).
Interaction partners:
- F-box protein UCC1
- F-box protein HRT3
- F-box protein YLR352W
- Suppressor of kinetochore protein 1
- Cell division control protein 53
Sequence:
MANKSRPKKIKAPYRKYVAGEGFSSTRNDNKAKEFTITIPEDAELIETPQGSYYYDETNDTIVKLTRLSNEKKDKKGRKQSPSSSSTSSSKGEKNGKVIESEEARMHSVSVKMVLPWEIQHRIIHYLDIPEKEEKLNKTANGKKTTTGINMNYLLVCRNWYAMCLPKLYYAPALTSKNFNGFVDTIIINKKKNLGHYVFELNLSTILQSGRNSFVSKLLRRCCSNLTKFIAPQTSFGYAPLISLKSCHDLKFLDLGLVSETVKLKELFSAIKNFTKLTHLSFPRSSIDCQGFQDIQWPQNLRYLKLSGGITNEFVIDTKWPTTITTLEFSYCPQITELSIYSLLSQIGDNLKHLFFHYPMPSLAENSLDHVFTYCANLISLQLMVDYCSKWCFSEFMLSKLVEYDRPLKTLYLECSGSLGLASKIHPDDLTIAILESRLPCLKNICVSPKLGWNMKSDEVADLVVSLEDQDGSLYLNY
Protein: Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme (ATP:glutamine synthetase adenylyltransferase) (ATase) [Includes: Glutamine synthetase adenylyl-L-tyrosine phosphorylase (EC 2.7.7.89) (Adenylyl removase) (AR) (AT-N); Glutamine synthetase adenylyl transferase (EC 2.7.7.42) (Adenylyl transferase) (AT) (AT-C)] (Q2RSQ7)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Interaction partners:
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Glutamine synthetase
- Ammonium transporter
- Nitrogen regulatory protein P-II
- DNA-binding transcriptional regulator NtrC)
- DUF3971 domain-containing protein
- Glutamate synthase large chain
- L-glutamine synthetase
- L-glutamine synthetase
- Glutamine synthetase, catalytic region
Sequence:
MQEFLFPSATARFPLPADQGRLDRGLERWRALARDDSEGIAPSFVKNFLDDPRGNALLAAVFGNSPYLSAALIREPAFVETLALRGPDQVFPDLLEGMARAIAATSEATVVMQVLRVTKRRAALCIALADIARWWSLEQVTAALSALAERSLRAVVAHLLTRRAASGDLVLPHPEDPERDSGFFILGMGKLGGGELNYSSDIDLIVLFDAEKARYQGKRSLKECYVGLTRDLVRMMEERTAEGYVFRTDLRLRPDPGSTAVAISTEAAEIYYETMGQNWERAAMIKARPVAGDLVAGQAFLTHLRPFVWRKYLDFNAIQDIHSIKRQIDAVRGGAEIGVAGHNIKLGRGGIREIEFFAQTQQLIWGGRTPKLRSKSTCEALADLVEVGLVEAPAADELTEAYRYLRTLEHRLQMIDDEQTQTLPLEPDKLRHLALFMGEADAEALGVAVTTRLRRVESHYAGLFEDAPSLSQGGNLVFTGGEDDPETLATLRRMGFSNPEGISATIRGWHHGRYAATRSTRTRERLTELMPDLLKALAATAQPDTALLRFDEFLSKLPTGMQLFTLFQANPGLLGLLAEIMGDAPRLSEHLARNPRLMDIVLTPGFFEGAPSHADMTRSLDALLADAVVFEDTLDLVRRWANDLRFSIGVLALRGLVEAEEAGQSLSDVADVALSRLVPRVEAEFALAHGVVPGGAMAVVALGKLGSREMTATSDLDLIVVYETPEDSEGSQATEAGQRPLPVSAYYTRLTQRIVNAITALTAEGALYEVDMRLRPSGNKGPLATSLTAFRRYQADAAWTWEHMALTRARVITGPEGLRARIDAVIAETLTRPRDAETLARDVADMRARMERDKPAASPWDVKLAPGGLVDIDFLAQFLQLRHAPRTPEVLAADTVGALRRLSEAGYLDPAICRFLCAHHRRNLGIQATLRHSIAGPPRDSDLTPGLKAKLARATGWDDFETLRAHMADDGARVRQIFTEIVDPTRPPPPPPLEKGPPMTEIPVAPGTAAPDFSLPTDGGGTLSLADLRGKKLVLYFYPKDATSGCTTEALGFKEQAEAFAEAGAVIVGVSKDSVKSHDGFKAKQGLPFTLASDAEGAVCQSYGVWVEKSMYGRTYMGIDRSTFLIDGEGIIRKIWRKVKVAGHVAAVLEEARAL
Protein: Carnosine dipeptidase 2 (J3KSV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQK
Protein: Non-specific lipid-transfer protein 5 (LTP 5) (Q9XFS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
Interaction partners:
- Non-specific lipid transfer protein GPI-anchored 2
- Non-specific lipid transfer protein GPI-anchored 1
- Non-specific lipid-transfer protein 9
- Probable pectinesterase/pectinesterase inhibitor 44
- COX assembly mitochondrial protein
- Ribosomal protein L31
- Ribosomal protein L18e/L15 superfamily protein
- Non-specific lipid-transfer protein 15
- Putative lipid-transfer protein DIR1
- AT5g03660/F17C15_80)
Sequence:
MEGLLKLSTLVIVCMLVTAPMASEAAISCGAVTGSLGQCYNYLTRGGFIPRGCCSGVQRLNSLARTTRDRQQACRCIQGAARALGSRLNAGRAARLPGACRVRISYPISARTNCNTVR
Protein: D-psicose 3-epimerase (DPEase) (EC 5.1.3.30) (B8I944)
Organism: Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) (Clostridium cellulolyticum)
Function: Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose.
Interaction partners:
- Oxidoreductase domain protein
Sequence:
MKHGIYYAYWEQEWEADYKYYIEKVAKLGFDILEIAASPLPFYSDIQINELKACAHGNGITLTVGHGPSAEQNLSSPDPDIRKNAKAFYTDLLKRLYKLDVHLIGGALYSYWPIDYTKTIDKKGDWERSVESVREVAKVAEACGVDFCLEVLNRFENYLINTAQEGVDFVKQVDHNNVKVMLDTFHMNIEEDSIGGAIRTAGSYLGHLHTGECNRKVPGRGRIPWVEIGEALADIGYNGSVVMEPFVRMGGTVGSNIKVWRDISNGADEKMLDREAQAALDFSRYVLECHKHS
Protein: Secretin receptor (SCT-R) (SECR) (P47872)
Organism: Homo sapiens (Human)
Function: Receptor for secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5FWI2}; Multi-pass membrane protein {ECO:0000269|PubMed:32811827}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5FWI2}; Multi-pass membrane protein {ECO:0000269|PubMed:32811827}.
Interaction partners:
- Secretin
- Guanine nucleotide-binding protein G
- Anoctamin-6
- VIP peptides
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- Adhesion G protein-coupled receptor A1
- Probable non-functional immunoglobulin heavy variable 3-16
Sequence:
MRPHLSPPLQQLLLPVLLACAAHSTGALPRLCDVLQVLWEEQDQCLQELSREQTGDLGTEQPVPGCEGMWDNISCWPSSVPGRMVEVECPRFLRMLTSRNGSLFRNCTQDGWSETFPRPNLACGVNVNDSSNEKRHSYLLKLKVMYTVGYSSSLVMLLVALGILCAFRRLHCTRNYIHMHLFVSFILRALSNFIKDAVLFSSDDVTYCDAHRAGCKLVMVLFQYCIMANYSWLLVEGLYLHTLLAISFFSERKYLQGFVAFGWGSPAIFVALWAIARHFLEDVGCWDINANASIWWIIRGPVILSILINFILFINILRILMRKLRTQETRGNEVSHYKRLARSTLLLIPLFGIHYIVFAFSPEDAMEIQLFFELALGSFQGLVVAVLYCFLNGEVQLEVQKKWQQWHLREFPLHPVASFSNSTKASHLEQSQGTCRTSII
Protein: Threonine dehydratase (EC 4.3.1.19) (Threonine deaminase) (Q59P56)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Acetolactate synthase regulatory subunit
- Threonine synthase
- Acetolactate synthase
- Tryptophan synthase
- Branched-chain-amino-acid aminotransferase
- SUMO-conjugating enzyme UBC9
- dihydroxy-acid dehydratase
- phosphoserine phosphatase
- low-specificity L-threonine aldolase
- low-specificity L-threonine aldolase
Sequence:
MSITRLSSAKLLLSSTSRKLQVLRLNSTTTKPLTPRQKWPELLDSDFIVNSQGEKQPDYVKLILTSRVYDVVDEAGTPLTNAINLSHRCGANIYLKREDLLPVFSFKLRGAYNMIAHLHSNSPQPISGVIACSAGNHAQGVAFSSSKLNIPATIVMPTPTPSIKYTNVSRLGAQVVLYGDDFDSAKQECERLSTEQNLINIPPFNHPYVIAGQGTIALEIARQLRLDKLNAIFVPVGGGGLIAGVAVYLKHIAPHVKIIGVETYDADALNQSLKNSRSVTLEKVGLFADGTAVKVLGDETWRLAKEYVDEVVLVNTDELCAAIKDIFEDTRSIVEPSGALSVAGLKKYIEEHPEIDHRDKTYVPVLSGANMNFDRLRFVSERAVLGEGKEVSLAVTIPEKPGEFARLQKVINPRAITEFSYRYNGEENADIFVSFNVVDKKKEKSSVIAAMENCGFEVVDISENELAKSHGRYLVGGKSQSTKSSNEKIYQFEFPEKPNALFNFLQALRSDWNISLFNYRNHGHDVGKILCAFTLPEGSEEDFQEFLKNVGYTFVDESDNIFYKKFLRS
Protein: Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (O35253)
Organism: Mus musculus (Mouse)
Function: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Subcellular location: Nucleus {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Cytoplasm {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:15496141). TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:15496141}.
Interaction partners:
- TGF-beta receptor type-1
- E3 ubiquitin-protein ligase SMURF1
- E3 ubiquitin-protein ligase SMURF2
- E3 ubiquitin-protein ligase Arkadia
- Transcriptional coactivator YAP1
- Transforming growth factor beta-1 proprotein
- TGF-beta receptor type-2
- Mothers against decapentaplegic homolog 6
- Mothers against decapentaplegic homolog 3
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
Sequence:
MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGELRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPTSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTAGCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
Protein: Galactofuranosyltransferase GlfT1 (GalTr 1) (EC 2.4.1.287) (Arabinogalactan galactosyltransferase 1) (Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,4/1,5-galactofuranosyltransferase) (UDP-Galf:alpha-3-L-rhamnosyl-alpha-D-GlcNAc-pyrophosphate polyprenol, galactofuranosyl transferase) (P9WMX3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the transfer of the first two galactofuranosyl (Galf) units from UDP-galactofuranose (UDP-Galf) onto the rhamnosyl-GlcNAc-diphospho-decaprenol (Rha-GlcNAc-PP-C50) acceptor, yielding galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50). Thus, GlfT1 is the initiator of galactan synthesis, while GlfT2 continues with the subsequent polymerization events.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16952951}. Secreted, cell wall {ECO:0000269|PubMed:16952951}.
Interaction partners:
- Probable O-antigen/lipopolysaccharide transport integral membrane protein ABC transporter RfbD
- Galactofuranosyltransferase GlfT2
- Probable O-antigen/lipopolysaccharide transport ATP-binding protein ABC transporter RfbE
- N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
- UDP-galactopyranose mutase
- Bacterial proteasome activator
- Probable conserved transmembrane protein alanine and leucine rich
- Decaprenyl-phosphate N-acetylglucosaminephosphotransferase
- Galactan 5-O-arabinofuranosyltransferase
- Conserved protein
Sequence:
MTESVFAVVVTHRRPDELAKSLDVLTAQTRLPDHLIVVDNDGCGDSPVRELVAGQPIATTYLGSRRNLGGAGGFALGMLHALAQGADWVWLADDDGHAQDARVLATLLACAEKYSLAEVSPMVCNIDDPTRLAFPLRRGLVWRRRASELRTEAGQELLPGIASLFNGALFRASTLAAIGVPDLRLFIRGDEVEMHRRLIRSGLPFGTCLDAAYLHPCGSDEFKPILCGRMHAQYPDDPGKRFFTYRNRGYVLSQPGLRKLLAQEWLRFGWFFLVTRRDPKGLWEWIRLRRLGRREKFGKPGGSA
Protein: Endothelin-converting enzyme 2 (ECE-2) (EC 3.4.24.71) (F1N476)
Organism: Bos taurus (Bovine)
Function: Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12054617}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12054617}.
Interaction partners:
- EEF1A lysine methyltransferase 4
- Endothelin-1
Sequence:
MSVALQELGGGGNMVEYKRATLRDEDAPETPVEGGASPDAVEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW
Protein: Uncharacterized protein C1020.05 (O59759)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Kinetochore protein mis13
- Pdp3-interacting factor 1
- Uncharacterized helicase C694.02
- Glycerophosphocholine phosphodiesterase gde1
- Protein Dicer
Sequence:
MMLPKRNIIHFLRKRAIFIVAAFIALLTVDYSLNTIEITDSKSGPFSLNTPIEDIRLVECFSFSPFCRPVLEFWKWARTSRNLYRSRIPWKRAYLYVKRPALYIPGETVLVEQVYVDRQLEKRNKHGIQIRYGTDGDICEFNTLLGEDVVELREGWSAVLNDFIYLGQPVLLTQRPCETPPTPSIEALKRKELSSVTLTYDDEEKKTIKILQLSDLHYSNSDRPCRDPYPYETAEDCMADAKTTAFVNELLQLEEPDFVLLTGDLINGDTSRDARSSLMKAVSPFVDYNVPFAVNFGNHDDLGDLSREELAKILSQIPGSMGLIGNVSGVGNFVLHSPRKFAIYVLDTKGDTSNRRLCPGYDAITEDQLEWLSSKVADFKYEPIQMAVLHIPLKEFCETEDLVGAFREPCSYSICDPNTAKALKSLRIPLAIAGHDHVNDFCGIHPDYNTYFCFAGGAGFGGYGGHGGYVRRARVFELDPVERAVRTWKRLEWPPEDRKLMLDVQTILV
Protein: Alpha/beta-Hydrolases superfamily protein (Lipase, putative) (Q9C8G6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
- Probable lysophospholipase BODYGUARD 4
- Protein kinase family protein
- ACD11 homolog protein
- Alpha/beta-Hydrolases superfamily protein
- Protein BONZAI 3
Sequence:
MENALVKTPLRKLRRRRTKRVWRLKQKLKLAWKSIKIRVKSHLPGFLSTKKHLFHIKSRKEEQDLSQVAQRICKISNDSTKSLAFLLQLPKYSADDFLDRGDLMTPAASPREKISKMWRELHGSNNWENLLDPLHPWLRREVTKYGEFVESVYDSLDFDPLSEFCGSSRYNRNKLFEELGLTRHGYKVTKYIYAMSRVDVPQWFLSSALGETWSKDSNWMGFVAVSGDRESLRIGRRDIVVAWRGTVTPTEWFMDLRTSMEPFDCEGKHGKTVVKVQSGFLSIYNSKSELTRYNKESASEQTMDEVKRLVNFFKDRGEEVSLTITGHSLGGALALMNAYEAARDVPALSGNISVISFGAPRVGNLAFKEKLNSLGVKVLRVVNKQDIVPKLPGIVFNKVLNKLNPITSRLNWVYRHVGTQLKLDVFSSPYVKRDSDLGRAHNLEVYLHVLDGFHRKKSGFRVNARRDVASVNKSTDMLLDHLRIPEFWYQVAHKGLILNKQTGRWVKPVRAPEDIPSPLPTGPKPIYSL
Protein: Probable portal protein (Gene product 4) (gp4) (D3WAC3)
Organism: Lactococcus phage p2 (Lactococcus lactis bacteriophage p2)
Function: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine. Necessary to ensure correct procapsid size during capsid assembly. Once the capsid is packaged with the DNA, the terminase complex is substituted by the connector proteins gp15.
Subcellular location: Virion {ECO:0000269|PubMed:24027307}. Note=Occupies the twelfth vertex of the capsid. {ECO:0000305|PubMed:24027307}.
Interaction partners:
Sequence:
MNLFGKVVSFSRGKLNNDTQRVTAWQNEAVEYTSAFVTNIHNKIANEITKVEFNHVKYKKSDVGSDTLISMAGSDLDEVLNWSPKGERNSMDFWRKVIKKLLRAPYVDLYAVFDDNTGELLDLLFADDKKEYKPEELVRLTSPFYINEDTSILDNALASIQTKLEQGKLRGLLKINAFLDIDNTQEYREKALTTIKNMQEGSSYNGLTPVDNKTEIVELKKDYSVLNKDEIDLIKSELLTGYFMNENILLGTASQEQQIYFYNSTIIPLLIQLEKELTYKLISTNRRRVVKGNLYYERIIVDNQLFKFATLKELIDLYHENINGPIFTQNQLLVKMGEQPIEGGDVYIANLNAVAVKNLSDLQGSRKDVTSTDETNNQ
Protein: Transcriptional regulator prz1 (Pbp1-responsive zinc finger protein 1) (Q09838)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the regulation of calcium ion homeostasis. Binds to the calcineurin-dependent response element. Transcriptionally regulates pmc1.
Subcellular location: Nucleus {ECO:0000269|PubMed:12637524}. Cytoplasm {ECO:0000269|PubMed:12637524}.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calmodulin
- Calcineurin subunit B
- Calcium-transporting ATPase 1
- Calcium-channel protein cch1
- Stretch-activated cation channel yam8
- Calcium/calmodulin-dependent protein kinase type I
- Myosin 1 light chain cam2
- Calcium-binding protein NCS-1
Sequence:
MERQRSEEANRRFKDLNPSSLYDNLSKPDLGGSSELHTYMNDTSLADIPLFEDTLASEVSSSLISNPSKNNIQHLHPNTSEPFKTSSKSDEYDSYPRTGNVPTFSFTELNDTSVSGFGSQAVFENSVSPLSNPSNSPQAFDLTQGSSSTHNANDFTVNNVGSRRQSIYEFNIGIPSSNIDSSQFLPVSRAIAASEISPSSSPQLLTSFLPSGSVSNPSSPYLQGSVGALYEADAFNFVDVMSQASGTEVDSERFPSVDFEDPSLLMENQQNITGTGSFADYLQPPSSGSLGAFTNASPGESNTGIDFDTDNTNLNPSVDLLSNHSTPSFIFENSPSAEFSHQSSPYLVPNSGRTLNSENARESTIRSVNSPFSEDHADASLTTHVFDPISPTALSNSVLNYDSNNFSGTPQINVVPSSPSKSQSGPSLPANPLLQTDISITYSQSASPVSGQPAMNENSYDLQNANLCAPEMSPTYTARHRSNSAGSRFDAYEPIPQLYTHFSHSSECLSVNQDTELLGKIENDNSKSNDYLSVRNTRPRSRSLNSLVGNKSENSSSSKAKSESKSQGNYVCTFAGCNKRFTRAYNLKSHMNTHTNYRPFQCSICKKSFARQHDKRRHEQLHTGIKAFACVTCNQRFARMDALNRHYKSEVGQNCLRTATERGIQVPPSRKTAVASTSKQK
Protein: A-kinase anchor protein 6 (Q3UHR2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MLTMSVTLSPLRSQDPDPMATDASPMAINMTPTVEQEEGEGEEAVKDVGAEQQYGKPPPLHTAADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLGGLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGAANEDSSQVILSEDHRGGHEEDGALEPGEQLGSTLETSSLGDTLTNAAEHPPETANQDSTSSPQLGAKKSQPGPCEMMTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETLKNERRGSDGKGRVVDLKPELSRSTPSLVEPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGIGNLENIVRSHIKEISSSLGRLTDCHKEKPRLKKPHKTLAEVSLCKIPKRGTGSGKQSENTRSSVVPTMVSPGAPKATARPATDSASTTSGDTCHQRNRGGKLPAQSKASSSSPCSHSSESSLGSDNIKSPLPLLSKSQKGSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCMPLSGMKKFTDEKSERPSSSEKNESHSATKSALIQKLMKDIQHQDNYEAIWERIEGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLKMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEAQLCYLEAQRDAVEQMSLKLYSEQYTSGSKRKEEFADMSKAHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDSINEKWELLGKTLREKIQDTMAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLRKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDLEPMVPTVKLEETHHKDSGYEEEAGDCGGSQYTSNITAPSSPHIYQVYSLHNVEFHEDSHTQFLKSSPKFTGTVQPTVLTKSLSKDSSFSSTKSLPDLLGGSSLVRPYSCQSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETQHLDPQMGDAANVLEQKFKDEGECIKLSSVSQASVSPVGCVNGKAGDLNSITKHTTDCLGDELQGKHEVFTFYDYSYLQGSKLKFPMIMKQPQSEKAHLEDPLLRGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLHLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKGENKKNTYDVTKDPHVADMENGNVESTPEREKEKPEIPEASANLASNVKKISESKHDEYEALMDGSDDSSVTGKEFGPPNDRHPPQIGADPQHPERGDCTSVQNSCSGLLLETGGGSRQDSDGLKSLSNDAPSVARNAAGCCLLEQNETEESASISSSTSCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGGFYSYLSLSSHDSDCGEVTNYIDEKSNTPLPPDTVDSGLDDKEDVDCFFEACVEDEPADEEARLSSALPNESEVQDEAAKPEQMTASSSVFRDETDTVPLSGLSPQKGADDAKEGDGASHTSQGCVESAEPTTPPGKAKREGSSRKQSVSGTPEENAASAKPKIQAFSLNAKQPKGKAALYPSPQTLTCKEKLVSFHEDRHSNMHR
Protein: GTP-binding nuclear protein GSP1/Ran (Q6FR65)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Nucleoporin NSP1
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Exportin-T
- Candida glabrata strain CBS138 chromosome C complete sequence
- Importin-95
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MSAEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLAFHTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCGIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL