wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphate system positive regulatory protein PHO81 (CDK inhibitor PHO81) (P17442)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85 and PCL7-PHO85 under low-phosphate conditions.
Subcellular location: Cytoplasm. Nucleus. Note=Localizes predominantly to the nucleus in both high- and low-phosphate conditions.
Interaction partners:
- PHO85 cyclin PHO80
- Cyclin-dependent protein kinase PHO85
- Phosphate system positive regulatory protein PHO4
- Inorganic phosphate transporter PHO84
- Vacuolar transporter chaperone 3 complex subunit 3
- Vacuolar transporter chaperone complex subunit 4
- Protein SYG1
- Inorganic phosphate transporter PHO87
- Vacuolar transporter chaperone complex subunit 2
- Low-affinity phosphate transporter PHO90
Sequence:
MKFGKYLEARQLELAEYNSHFIDYKALKKLIKQLAIPTLKASSDLDLHLTLDDIDEKIIHQRLQENKAAFFFKLERELEKVNGYYLARESDLRIKFNILHSKYKDYKINGKLNSNQATSFKNLYAAFKKFQKDLRNLEQYVELNKTGFSKALKKWDKRSQSHDKDFYLATVVSIQPIFTRDGPLKLNDETLHILLELNDIDNNNRRADIQSSTFTNDDDDDNNTSNNNKHNNNNNNNNNNNNNNNNNNILHNNYELTTSKISENQLEHLFQASSSSLDMEMEIENWYKEILNIATVKDVQRKHALLRNFRETKIFTYLLQNSSESFHKNVFSLLKECLTTLFLLLVASPLDDNSLHIFYKSNQDHIDLSYCDEDDQVFSRKNVFHEAASCPEKSRLFILDEALTTSKLSKETVQKLLNAQDIHSRVPLHYAAELGKLEFVHSLLITNLLEDVDPIDSDSKTPLVLAITNNHIDVVRDLLTIGGANASPIEKPILDYSKNVISSTKVQFDPLNVACKFNNHDAAKLLLEIRSKQNADNAKNKSSQHLCQPLFKKNSTGLCTLHIVAKIGGDPQLIQLLIRYGADPNEIDGFNKWTPIFYAVRSGHSEVITELLKHNARLDIEDDNGHSPLFYALWESHVDVLNALLQRPLNLPSAPLNEINSQSSTQRLNTIDLTPNDDKFDLDIQDSIPDFALPPPIIPLRKYGHNFLEKKIFIKLKLRPGLESIKLTQDNGIIMSSSPGRITLSSNLPEIIPRNVILPVRSGEINNFCKDISETNDEEDDDEISEDHDDGEIIFQVDSIDDFSMDFEIFPSFGTRIIAKTTAMPFLFKKVAINSIATMNLPLFDTRLNNIGSLTLDYQIIFPYPGNPLKIINYEPYWKSTGSDLMTSSKDGNFVTSSSLNGSFISVLVCALNDETIVAAPKPYVEFKGTKILLNDLTKEQLEKVVDYDFGKIDGSFDEVTLKQYLSSRVVPLRSLLEVIPGSAQLVIRVYFPTDKEIDTIPIKISPFININQFIDKLLLIIFEHERFLRHSGSGSMRQIVFSSCNWEACSILNWKQPNFPVLLQMKNLLRDSTTGKFVGDTPNCLKELAVNPQKMSYLNTELINIHTMVQFAMNNNLLGVTLPYEVLKICPSLARIIKQNGLLLIASVGENDQIPADGGYSGIYYACELLFENNIDM
Protein: Threonine--tRNA ligase, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P87144)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Putative leucine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, mitochondrial
- Histidine--tRNA ligase, mitochondrial
- Probable threonine--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Putative glycine--tRNA ligase
- Putative proline--tRNA ligase C19C7.06
- Probable cysteine--tRNA ligase
- Probable glutamate--tRNA ligase, cytoplasmic
- Monothiol glutaredoxin-5
Sequence:
MSAAAVKGVQASLDNLSLEIPFIQHRLDLFDKLQKEYKESLATKPREEIDITLPDGKVIKGTSWETTPISIAASISKGLADRVTVAIVNGEPWDLTRPLEASCTLKLCDFNDPEGKRVFWHSSAHILGEATELSFHCHLCIGPPTDEGFFYEMGIDNGRVITNDDYSSIESYAKQAIKQKQPFERLVISKEGLLEMFRYNKYKQYIIQTKIPDGASTTVYRCGPLIDLCTGPHVPHTGRIKSFAVTKNSSSYFLGDAKNDSLQRVYGISFPDNKQMQEYKTFLAEAAKRDHRKIGRDQELFFFNEISPGSCFFLPHGARIYNTLLKYMRYQYSKRGYQEVITPNMYNVNLWKTSGHWNNYSENMFSFDIEKEKYALKPMNCPGHCVMFKSRDRSYRDLPWRVADFGVLHRNEFSGALSGLTRVRRFQQDDAHIFCTPDQVRSEIEGCFDFLKEVYGTFGFTFHLELSTRPEEKYLGDLATWDKAEAQLKAALDASGYKWELNAGDGAFYGPKIDITVFDALKRQHQCATIQLDFQLPERFQLEFHAPASAEEAKESGNNNKYTRPVMVHRAILGSLERMIAILTEHYAGKWPFWMSPRQVCIIPVSAAAYNYADKVHNILSEADIFVDTDKSDNTLPKKIRNAQLAQYNFIFVVGAEEESTNSVNVRNRDDPKKQSKGSTVAVEEVVKKLLKLKESKSLINDL
Protein: Cysteine-rich protein 3 (CRP-3) (Thymus LIM protein) (m17TLP) (Q6Q6R3)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11713292}.
Interaction partners:
Sequence:
MSWTCPRCQQPVYFAEKVSSLGKNWHRFCLKCERCHSILSPGGHAEHNGRPYCHKPCYGALFGPRGVNIGGVGCYLYNLPTPPPASRISLSPSNFSPPRPRTGLSRAKKGPPYLKTFTGETSLCPGCGDPVFFAEKVMSLGRNWHRPCLRCQRCRKTLTAGSHAEHDGMPYCHIPCYGYLFGPKGVNIGDVGCYIYDPVDIRSK
Protein: DNA repair protein RecO (Recombination protein O) (P0A7H3)
Organism: Escherichia coli (strain K12)
Function: Involved in DNA repair and RecF pathway recombination.
Interaction partners:
- Recombination protein RecR
- DNA replication and repair protein RecF
- GTPase Era
- Pyridoxine 5'-phosphate synthase
- Single-stranded-DNA-specific exonuclease RecJ
- Protein RecA
- ATP-dependent DNA helicase RecG
- Single-stranded DNA-binding protein
- Regulatory protein RecX
- Holo-[acyl-carrier-protein] synthase
Sequence:
MEGWQRAFVLHSRPWSETSLMLDVFTEESGRVRLVAKGARSKRSTLKGALQPFTPLLLRFGGRGEVKTLRSAEAVSLALPLSGITLYSGLYINELLSRVLEYETRFSELFFDYLHCIQSLAGVTGTPEPALRRFELALLGHLGYGVNFTHCAGSGEPVDDTMTYRYREEKGFIASVVIDNKTFTGRQLKALNAREFPDADTLRAAKRFTRMALKPYLGGKPLKSRELFRQFMPKRTVKTHYE
Protein: GTP-binding protein (Q7SY56)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Rho guanine nucleotide exchange factor
- Rho/rac guanine nucleotide exchange factor
Sequence:
MTLNKGDKLRNMDKRRGSMPFPLHLQTLHRRSMPVDDRELRSMPAAQPSELPGLMRFNADRNSCVSDSSDSVISSGSDSDGQVYKVVLLGEHGVGKSSLARIFGGVEDSNDCEETGNTYDRSLVVDDEETSILLYDIWEQDNSQWLQDQCMRMGDAYIIVYSVTDKSSFEKASELRIQLRRARQSENIPIILVGNKSDLVRSREVSMDEGSACAVVFDCKFIETSASLHHNVRDLFEGIVRQIRLRKDSKEENARRMANCKRRESISKKAKRFLGRMVARKNKKMAFRQKSKSCHDLSVL
Protein: RE70685p (Q86P57)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELCIATKSKIETAQSSMPQSSQCSSSSNCRNYQKKCHQNQTNTQVQSTQRSNCSSHSDRDHLTNQQKQQNQRTNSATAASAAAATLSESTRCNIIISSSSSSSSSTKSSKNIREPSSSSSTQLNTLYSLLVLLIVGLATATASPSPSPSHAPFGRESRRDALLAYYKRAHLPQSSSSGISLGHKYHLLHDANGLDFDELTPTASSVSALSRAERFRLRKRSATPTTPATAAGVTSLDVATAAAAATDAAAKDAGSGKKPEEKCEPKVLETLPDEPFYDYTDIAEDAARQFIEFLSGKFPNANTPIAIDEPTRAEVSRRANGIASYALNEDDNLLAFAIAAPSIHTVVVKFRDNVTIPPDQVHNKAYLGSYWRELGAAWNSTDGTQEWGAPFRDCNLLTRRWLWPSHILQRAQDQSCGGCLHCRRRGCVQRWPGGSFRSPSWLRSEYDLLPAHREQTRRHPGCVHLSVPGILLPAQFHAPGIPWRSSGTVRGLRQLLVHSVSRRMH
Protein: Protein Vpr (R ORF protein) (Viral protein R) (Q72500)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147, ECO:0000256|HAMAP-Rule:MF_04080}. Virion {ECO:0000256|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000256|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. {ECO:0000256|HAMAP-Rule:MF_04080}.
Interaction partners:
Sequence:
MEQAPEDQGPQREPYNEWTLELLEELKSEAVRHFPRIWLHNLGRHIYETYGDTWAGVEAIIRILQQLPFIHFRIGCRHSRIGVTRQRRARNGASRS
Protein: Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (GAD-65) (Glutamate decarboxylase 65 kDa isoform) (Q05329)
Organism: Homo sapiens (Human)
Function: Catalyzes the production of GABA.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12356867}. Cytoplasmic vesicle {ECO:0000269|PubMed:12356867}. Presynaptic cell membrane {ECO:0000269|PubMed:12356867}; Lipid-anchor {ECO:0000269|PubMed:12356867}. Golgi apparatus membrane {ECO:0000269|PubMed:12356867}; Peripheral membrane protein {ECO:0000269|PubMed:12356867}; Cytoplasmic side {ECO:0000269|PubMed:12356867}. Note=Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- 4-aminobutyrate aminotransferase, mitochondrial
- Receptor-type tyrosine-protein phosphatase-like N
- Glutamate decarboxylase 1
- Glutamine synthetase
- Glutamate dehydrogenase 1, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Cysteine dioxygenase type 1
Sequence:
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Protein: Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)] (P00748)
Organism: Homo sapiens (Human)
Function: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.
Subcellular location: Secreted.
Interaction partners:
- Kininogen-1
- Plasma protease C1 inhibitor
- Plasma kallikrein
- Antithrombin-III
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Plasminogen
- Coagulation factor XI
- Tissue factor
- Prothrombin
- WD repeat-containing protein 90
Sequence:
MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS
Protein: Na-K-Cl cotransporter (Q9QX10)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEPGPAAPSSGAPRPARDGDAPLTAAGVDLPGTAVLSGREDATAGSQAGGGVRGEGTPAAGDGLGKPLGPTPSQSRFQVDPVSENAGRAAAAAAAAAAAAAAGAAGKETPAAGKAGTESGVAKGSEEAKGRFRVNFVDPAASSSADDSLSDAAGVGGDGPNVSSQNGGDTVLSEGSSLHSGGGSGHHQQYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRHTAAQLGEKLLRPSLGEFHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLSVLVIAMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFPNAVAVAMYVVGFAETVVELLKEHSILMIDEINDIRIIGAITVVVLLGISVAGMEWEAKAQIVLLVILLLAIADFVIGTFISLDSKKPKGFFGYKSEIFSENFGPDFREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTVVYIGIAVSVGSCVVRDATGNVNDTITTELTNCTSAACKLNFDFSYCESNTCSYGLMNNFQVMSMVSGFAPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQMFAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWISLTGAILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLSALQHSIRLSGVEDHVKNFRPQCLVMTGSPNSRPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGLGRMKPNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVNVDYSKKSDQDAFKASGEKPITQKDEEEDGKTSTQPLLKKESKGPVAPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIPYLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIVAFDDMIEPYRLHEDDKEQDIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPPILLVRGNHQSVLTFYS
Protein: BTB/POZ domain and ankyrin repeat-containing protein NPR2 (OsNPR2) (NPR1 homolog 2) (OsNH2) (Q0JJ01)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Does not seem to be involved in defense response against the bacterial blight disease caused by Xanthomonas oryzae pv. oryzae (Xoo). Over-expression of NPR2/NH2 does not confer disease resistance to Xoo.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5ICL9}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- BTB/POZ domain and ankyrin repeat-containing protein NPR3
- Os12g0138800 protein
- Transcription factor TGA2.3
- Transcription factor TGA2.2
- Os11g0142300 protein
- Transcription factor TGAL1
- Transcription factor TGA2.1
- Os05g0492000 protein
- Transcription factor TGAL6
Sequence:
MPARSAVVVIAMEPSSSITIASSSSYLSNGSSPCSVSLAPPGAGAVAAQAAPVAAGEGGGGGGGGGGGGSSSVEVVSLNRLSANLERLLLDSDLDCSDADVDVADGGPPVPVHRCILAARSTFFYNLFAARGRGGDGAAGGGGGGGGGGGERTGGRPRYKMEELVPGGRVGRDAFLSLLGYLYTGKLRPAPDDVVSCADPMCPHDSCPPAIRFNVEQMYAAWAFKITELISLFQRRLLNFVDKTLVEDVLPILQVAFHSELTPVLEKCIRRIARSNLDNVSLDKELPPEVAVQIKEIRQKSQPNEGDTVISDPVHEKRVRRIHRALDSDDVELVKLLLNESEITLDDANALHYAAAYCDSKVVSELLDLRLANLNLKNSRGYTALHLAAMRREPAIIMCLLNKGAAVSQLTADGQSAMSICRRLTRMKDYNTKMEQGQESNKDRLCIDILDREMIRKPMAVEDSVTSPLLADDLHMKLLYLENRVAFARLFFPAEAKVAMQIAQADTTPEFGIVPAASTSGKLKEVDLNETPVTQNKRLRSRVDALMKTVELGRRYFPNCSQVLDKFLEDDLPDSPDALDLQNGTSDEQNVKRMRFCELKEDVRKAFSKDRADNSMFSILSSSSSSSPPPKVAKK
Protein: Spindle pole body assembly component MPS3 (98 kDa nuclear envelope protein) (Monopolar spindle protein 3) (P47069)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the linker nucleocytoskeleton and cytoskeleton (LINC) complex that regulates telomere movement and meiotic recombination during meiosis. Connects the spindle pole body with the nuclear envelope through its interaction with MPS2 and mediates meiotic bouquet formation and rapid chromosome movements in meiotic prophase. Functions as an integral membrane anchor for telomeres and is a nuclear receptor for the SIR4 pathway of telomere tethering and gene inactivation. Essential for nuclear division and fusion and required for the first step of spindle pole body duplication in G1. Functions in sister chromatid cohesion establishment. Recruits double-strand breaks (DSBs) to the nuclear periphery for chromosome healing.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:21518795, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30141044, ECO:0000269|PubMed:30417519, ECO:0000269|PubMed:34586062}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774, ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30141044}. Chromosome, telomere {ECO:0000269|PubMed:32967926}. Note=Localizes to the spindle pole body half bridge throughout the cell cycle (PubMed:15282802). Relocalizes from the spindle pole body to the nuclear envelope in meiosis, via the interaction with HTZ1 (PubMed:21518795, PubMed:22017544). The cohesin component REC8 promotes localization on nuclear envelope in mitotic cells (PubMed:30417519). {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:21518795, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30417519}.
Interaction partners:
- Chromosome segregation in meiosis protein 4
- Non-disjunction protein 1
- Monopolar spindle protein 2
- Regulatory protein SIR4
- Cell division control protein 31
- Histone H2A.Z
- Cell division control protein KAR1
- Nucleoporin POM152
- Inner nuclear membrane protein SRC1
- Spindle pole body component SPC42
Sequence:
MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLDFPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGLFFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLPSNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSALISDVIESPGIGTAGSAESRWEYDLNRYVKEILSNELQYIDKDYFIQEMNRRLQSNKQEIWEEITNRLETQQQQQQQQVQQDYSNVPQQYSSILMKRLIHQIYNSNQHQWEDDLDFATYVQGTKLLNHLTSPTWRQGSGVQPIELLTDSKQSSSTYWQCENEPGCSWAIRFKTPLYLTKISYMHGRFTNNLHIMNSAPRLISLYVKLSQTKEIKALQTLANQYGFGQHHKRDRNYIKIAKFEYRLTDSRIRQQMYLPPWFIQLKPLVRSIVFQVDENYGNKKFISLRKFIINGVTPQDLQIIENNEFPVLLGDTPEYGVTQNTDEGKRKVLLSKPPYASSSTSTKFHPASNVPSFGQDELDQ
Protein: Glycerophosphocholine permease GIT4 (GroPCho permease GIT4) (Glycerophosphodiester transporter GIT4) (A0A1D8PN14)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Glycerophosphodiester transporter that mediates uptake of glycerophosphocholine (GroPCho) with GIT3. Does not possess detectable glycerophosphoinositol (GroPIns) transport activity. The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism. This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids.
Subcellular location: Cell membrane {ECO:0000305|PubMed:24114876}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase GDE1
- Phytanoyl-CoA dioxygenase
- Alpha/beta hydrolase fold-3 domain-containing protein
- Alpha/beta hydrolase fold-3 domain-containing protein
Sequence:
MATRDLPHSVGDFCFGWVDQIRSEITLGKSQDQLIKEDVLEDDETVETKVEIKNLWPAFASGAGLFSDGYVNAGISTVLSCLKKIYGDEFTKSNAMNNIGSIGFVGTVVGQLSFGYISDNFDRKTGMLTANVMLIFFTLMCAVASWGTTVQGFFACLTVWRFFLGIAIGAEYPTSSVIASEFANQLPSGHRNRYFSWFTNAMIDFGFVVSSFVPLVLLWIFTPRHLRAVWRLSIGLGVIPPLILFFIRLKMDNSKSFKKMNMKRVNYSKYPWWLIIKFYWFRLTVVSLIWFIYDFSVYSFGTFNTIIIGEVIPNGTLYENWGWSVVFNLFYMPGAFLGAFIGDYLGPRLTLAIGVGAQGIIGIAMSACLKSLKKHVAGFVVVFGIFSTFGEFGPGNNTGLLASKTCASSIRGQYYGIAAAIGKIGAFVGTWVFPAIQKHYAYSEDLSLQVPFYVSSALCLFSAFLTIFFVPPVGQDAINKEDRLFKEYLEENGVDIRLLGDSGVVTQYQEDEDIGVISDEKDDTVKVQQKNV
Protein: Major histocompatibility complex, class II, DM beta (H0Y7A2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTRPPSVQVAKTTPFNTREPVMLACYVWGFYPAEVTITWRKNGKLVMPHSSAHKTAQPNGDWTYQTLSHLALTPSYGDTYTCVVEHTGAPEPILRDWTPGLSPMQTLKVSVSAVTLGLGLIIFSLGVISWRRAGHSRWHIS
Protein: Uncharacterized protein C106.19 (Q10340)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Pentatricopeptide repeat-containing protein 6
- Uncharacterized protein PB1E7.11c
- Mitochondrial cox1 translation regulator ppr4
- Mitochondrial 15S rRNA processing factor ppr3
- Probable translation initiation factor
- Pentatricopeptide repeat-containing protein 2
- Translation initiation factor IF-2, mitochondrial
- Uncharacterized protein P4H10.18c
- Large ribosomal subunit protein uL4m
- Pentatricopeptide repeat-containing protein 8
Sequence:
MFLRPWSRNFLCSCRGFSVCTPYASIKSASELALKNISELQALQKIQNHTEKLKFFSSKLHNKGEPFTLQLGDLITEHTSVPELNEILDKFSQSNELFTMRFLEKASIIAHKNRSAELARRLRTYAANAMIDLSRVAFVNIFWTLLKTRDKEGIVETIEGQPIAFKVARRIFRRLLVYTSEAGENIEICFFLTNSLFKRLLNNREALSKDEKSELQNLYYDLLLCFSYSYYVPGVKLLLPMLYNGSFKEINRTAIDRSLLALLSTGELEAALELLVYLKNNNIPINDAYLRMMVINFCLANKPTLAVRFCQAWFKQSKMLSSTENLLLIAESLSRASNDFAAISKQMQPFSIESSSFYLPSHRLLMLVALMMKNSSGILHSYAVLKKANAITNKELRIMMQHAMDLRSTEFAEAVLKESEFTLQSNRSQLLMDFVAILFLNKEYTKAFATLEKTFASKIKPSHNIISFSLSLVKRFGTKNDLFFLRRSFKNMGIETLDEIEKNLPPKVVYRCFNY
Protein: Cis-3-hydroxy-L-proline dehydratase (c3LHyp dehydratase) (c3LHypD) (EC 4.2.1.171) (Aconitase X) (AcnX) (PaLhpI) (Q9I485)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Has also activity with (2S,3S,4R)-3,4-dihydroxyproline as substrate, albeit at about 300-fold lower rate. No activity with L-proline, trans-4-hydroxy-L-proline (t4LHyp), cis-4-hydroxy-L-proline (c4LHyp), trans-3-hydroxy-L-proline (t3LHyp), D-proline, cis-4-hydroxy-D-proline (c4DHyp), trans-4-hydroxy-D-proline (t4DHyp) or L-serine as substrates. No hydro-lyase activity with citrate or cis-acotinate. Does not catalyze 2-epimerization of c3LHyp to trans-3-hydroxy-D-proline (t3DHyp). Involved in a degradation pathway that converts c3LHyp to L-proline, which would allow P.aeruginosa to grow on c3LHyp as a sole carbon source.
Interaction partners:
- Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase
- Delta
- Amino acid ABC transporter ATP binding protein
- Probable permease of ABC transporter
- Amino acid ABC transporter membrane protein
- Amino acid ABC transporter periplasmic binding protein
Sequence:
MKHAHLIVPRTLVAGSASGELLYAPTGLSFWGGVDPRSAEVIDRHHPLSGRHLHGRLLAIPGGRGSCTGSSVLLELILGGRAPAAILLREPDEILALGAIVAEELFGRSLPIACLGERFDELAAYPWARLADGRLELHRDAPPPLEARPAEALATDAGPRLDAFDQALLAGEHGEAARLAMRIVLRMAALQGAQRLIDIQRAHIDACIYTGPAGLRFAETLRDLGARVRVPTTLNAISVDQRRWREQGVPAALGEPAAALARAYLDMGAQPSFTCAPYLLDDSARAGEQIVWAESNAVLFANSVLGARTNKYADFMDICCALTGRAPLAGCHLDEQRQARVLIEVEDLGSVDDAFYPTLGYLCGLLCDGQIPAIDGLRQRQPDHDALKAFGAALGTSSSVPMFHVIGVTPEAPDLASAFGGRAPRRTLRVGRERLRDAWRELDSAGETRIDLVALGNPHFSASEFAQLAALCHGRRRHPEVALVITSSRQVVAQAEAAGHLATLQAFGARLVTDTCWCMLDEPLVPPGARTLMTNSAKYAHYAPGLVGRQVRFAGLAGCVEAAVGGRSPAGLPAWLSEDC
Protein: IS1535, resolvase (O05913)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MNLADWAESVGVNRHTAYRWFREGTLPVPAERVGRLILVKTAASASAAAAGVVLYARVSSHDRRSDLDRQVARLTAWATERDLGVGQVVCEVGSGLNGKRPKLRRILSDPDARVIVVEHRDRLARFGVEHLEAALSAQGRRIVVADPGETTDDLVCDMIEVLTGMCARLYGRRGARNRAMRAVTEAKREPGAG
Protein: NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.90) (Glyceraldehyde phosphate dehydrogenase (NAD(P))) (GAPN) (O57693)
Organism: Thermoproteus tenax
Function: Catalyzes the irreversible NAD(P)-dependent non-phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3PG). It is highly specific for D-GAP.
Interaction partners:
Sequence:
MRAGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTLVEAPADRVKDMVLYKREVFAPVASAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE
Protein: Dihydrofolate reductase (EC 1.5.1.3) (B4DM58)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKIPRCSL
Protein: Ankyrin repeat-containing protein C105.02c (Q9P7I0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative fatty acid elongase 2
Sequence:
MSTEGAKPSEMLIAACRSNNVDMLEEVVHQQEGDGVSFINNARDSLGNDCVHVCTKYGSLECLDWLLDISGVNLNNRCRMTGDTPLHFAVMFIKKDQETALRMVEMLMEVGADPLLTNNDGFRPIDLVPGDFHDVFASALEGPAPALQYSADVVADDDDEEEGSGESDEE
Protein: Uncharacterized protein (A0A1D8PIK8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- Fgr39p
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MEKKRSPIQITRSLNQIMITRKPYRIRSFINRSYSITRNPSKINRNISTHDRSTTNVLKRNQRRLKEFENNIQLAEQFKTHRQNVVEILKDEKNIDALFEKEVPIIVNDYEKLTEEMGALSFNDIEMRNTIMLVCHSLVESMYIELTLSKLEDKRIKPYLEEIKSSHWFESLAEYRFRFYNFKSSQFLSSTESDMSTQVNGNNFVRFNSCQKNSHEYIKKFERSFEKYKKAQNEPMSHIQLATNLVQDLLCTHEYIPTTEIWHYLLRNLGTLKLYNYQQIIYLSLFQYKHQPTILATPKEQDRLTAPLMADHFSHLIEDFPEILSTLCQYQEVRKDKRTFIELLSFLKLDKLAGEVMAIKSPLLSKAKYKLPAICPGIELECKDLFISRDCLYSIMKSAINLELYEYVDLLYDKIVLDSIDPYRIQLNYEEKRLVEGSIFTPELFLIMLEACKKSKDLGRVLWLMPFLDEYVGKNSVPVTLKNSILEVLKTFNLEGKLVSYQKIM
Protein: Protein kinase STUNTED (EC 2.7.11.-) (B5X4Z9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes cell proliferation in the gibberellic acid (GA) signaling pathway, acting downstream of RGA, and possibly through a negative regulation of two cyclin-dependent kinase inhibitors SIM and SMR1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22492352}.
Interaction partners:
Sequence:
MAVDKVIVKQRNIILVGIPIDESGVEVLKWALEEVAKHGDCVVVVHVCFTYYRALKSKSSLDRYLKPYIEFCSTKKIELKGEVLKGNSVLGVLVKEAKRYNAMSVVVGVKQQSKLSLKIAKGCAKELPSTTDILAIHRGNIVFRRSNHYQLPLAQKISSRPSSELSEGFSDKDLAKTTGQEKRKISGRSLSLPSVEVVDQTPGWPLLRTSTLATPMVQHQTRKISVVNWVMSLPERFPHHPNQTCQQSFCDKQLKDILKDINRWFSYDVLKTATSDFSLENLIGKGGCNEVYKGFLEDGKGVAVKILKPSVKEAVKEFVHEVSIVSSLSHSNISPLIGVCVHYNDLISVYNLSSKGSLEETLQGKHVLRWEERLKIAIGLGEALDYLHNQCSNPVIHRDVKSSNVLLSDEFEPQLSDFGLSMWGSKSCRYTIQRDVVGTFGYLAPEYFMYGKVSDKVDVYAFGVVLLELISGRTSISSDSPRGQESLVMWAKPMIEKGNAKELLDPNIAGTFDEDQFHKMVLAATHCLTRAATYRPNIKEILKLLRGEDDVSKWVKIEEDDEDGFDDEVYPNSNTELHLSLAMVDVEDNDSVSNSSLERSNNSLFSSSSSSSQELQS