wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-like-specific protease 1 (EC 3.4.22.-) (O42957)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: A cysteine protease that proteolytically removes the C-terminus of pmt3.
Interaction partners:
- Ubiquitin-like protein pmt3/smt3
- SUMO-conjugating enzyme ubc9
- Ubiquitin-activating enzyme E1-like
- Importin subunit beta-3
- E3 SUMO-protein ligase pli1
- Ubiquitin-like-specific protease 2
- Ran GTPase-activating protein 1
- Pre-rRNA-processing protein las1
- Polynucleotide 5'-hydroxyl-kinase grc3
- Importin subunit alpha-1
Sequence:
MIGKRNASKRTRQDDCITYEEYQRKRKKTFLNTFVNICSRTVTYAKLFLTKTPISELDRIAGEAIPSNSNSTNSKLEPSTKAPESRFSHINSKTERGYVTVESDMSSHNTLDRNSKPTVSHSYTNSSKDEKFLDPIALQNLFSPASDTHSQNIHDEALSPSSFRVSRSRYFPRPHRSSKNLSVSNRLQLAVFKETTSSTLSHGNSVEADEINSFNPTPFSSSPLHFTNSSPNPNSDIVTPDKQLDVVSEHARYKHLPFTATLRKKSPHDSTSRKASFRFVQSDQQPARNIVTSDIQNEKSLLLLIRDLKEKQTESFQDWNEVDFLQLKGLEISPPPTRPKFIPELEFPDNARKRALKYLNQSNSVSSSEPIITKFNIPITLKDLHTLRNRQWLNDEVINFYMNLISERSKIDSSLPRVHGFNTFFYTSLQRRGYAGVRRWAKKARVNIADMDAVFIPVHLDVHWCMAVINKSKKRFEYWDSLAGSPGKVFDLLRDYYIAETKGAVDVSDWENFMDDNSPRQRNGHDCGVFACKTAECVSRNVPVQFSQNDMPELRIKMAASIIDAQIY
Protein: L-arabinose-binding periplasmic protein (ABP) (P02924)
Organism: Escherichia coli (strain K12)
Function: Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
Subcellular location: Periplasm.
Interaction partners:
- Arabinose import ATP-binding protein AraG
- L-arabinose transport system permease protein AraH
- Arabinose-proton symporter
- D-xylose-binding periplasmic protein
- Galactofuranose-binding protein YtfQ
- Autoinducer 2 import system permease protein LsrD
- Arabinose operon regulatory protein
- Inner membrane ABC transporter permease protein YjfF
- Sensor protein EvgS
- Ribose import ATP-binding protein RbsA
Sequence:
MHKFTKALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMDALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDVVLITRDNFKEELEKKGLGGK
Protein: Ubiquitin carboxyl-terminal hydrolase 33 (EC 3.4.19.12) (Deubiquitinating enzyme 33) (Ubiquitin thioesterase 33) (Ubiquitin-specific-processing protease 33) (VHL-interacting deubiquitinating enzyme 1) (Q8R5K2)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Beta-2 adrenergic receptor
- Roundabout homolog 1
- von Hippel-Lindau disease tumor suppressor
- Beta-arrestin-2
- WD repeat and SOCS box-containing protein 1
Sequence:
MTTFRNHCPHLDSVGEITKEDLIQKSLGACQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTPPSLPHVRQPQQTQENSVQDFKIPSNPALKTPMVAVSEDLDIEVEEEDELKARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEMEEEPQTLTSEETVEEEKSQSDVDFQSCESCSSSEKAENESGSKGFPEDSNETTMLIQDEDDLEMAKDWQKEKVCNKINKANADVELDKDRDTVCETVDLNSQETVKVQIHGRASESITDVHLNDLATSQILPSNESVSPRLSASPPKLGSLWPGLSPPHKKAQSTSAKRKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAKLHSSSHPTIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIELEKIEKRRKTELEIFIRLNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGSVMLKQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDVLQAEEKIEVETRSL
Protein: RE26469p (Q8IGU8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
LRFNRRWSQTCPKCQKYLPRFSENSALWNEIRMDPDNDIYAFYDIRGYKGKCRPGRPNSERILQPRMSLLGKPLNYNRGTRRDVRYRRLQSRLYNFLERPRGLHAIFYHVMVFLMVFTCLALSVFSTIKEYEEDAVYILFRMEILVVIWFTMEFGARLWSSGCRSRYQGCLGRLKFVKRPFCIIDIVTILASIVVLGMGTSGQVFATSALRGLRFFQILRMVRMDRRGGTWKLLGSVVYAHRQELITTMYIGFLGLIFASFLVYMWEKDVNDKFSNFAQALWWGVITLCTVGYGDMVPITWQGKLIASCCALLGISFFALPAGILGSGFALKVQQQQRQKHMIRRRQPAATLIQAVWRCYAADEHSVSVATWNIHRVALPSPPASRASSSFKHNTSFVARLPTIRRHKSQTIQTPGGGDGGGVSKPPGSSRASTRYTRTIRDINASVENLDEEDEPRCTQLTNRHKTAIRFIRKLKYFVARRKFKEALKPYDVKDVMEQYAAGHVDLLGRVKMLHLRLDQILGKQGSKAKDVYASKISLASRVVKVERQVADIEEKLDILIKAYMEDRDRFLALPLPAKPKIHSISPSHKPLHHAHNLAMIDVWKRTAALSVHPEQVTTTPLLNPSAPDSSELRSLTATQTPTTTTDAIATQTPMPPHVQHTATNTKSSVLNSYQLGSEKQQHNDVFMTELENRTKKRVTLSLHRSTSEPYSKQEQRIIIPDEGADSLDSSAKPTPPDSSIILIDEYEDFEEEDLNCEGEMDHFPTWEIDSDIGVEVDVDADADGDCDESTEDTALLQCATRTAIVITPISPVSSAHNLQQLNDQTTTLNKSNLLPPDSG
Protein: Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Nuclear cytoplasmic O-GlcNAcase and acetyltransferase) (NCOAT) (O60502)
Organism: Homo sapiens (Human)
Function: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.
Subcellular location: [Isoform 3]: Nucleus {ECO:0000269|PubMed:11341771}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771, ECO:0000269|PubMed:11788610}.
Interaction partners:
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Aurora kinase B
- Ganglioside GM2 activator
- Beta-glucuronidase
- Beta-hexosaminidase subunit beta
- Beta-2-microglobulin
- Hepatitis A virus cellular receptor 1
- Arylsulfatase B
- Glutamine--fructose-6-phosphate aminotransferase 2
- Glutamine--fructose-6-phosphate aminotransferase 1
Sequence:
MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL
Protein: Allatostatin C/drostatin C receptor 1 (Q8MU51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTADSEANATNWYNTNESLYTTELNHRWISGSSTIQPEESLYGTDLPTYQHCIATRNSFADLFTVVLYGFVCIIGLFGNTLVIYVVLRFSKMQTVTNIYILNLAVADECFLIGIPFLLYTMRICSWRFGEFMCKAYMVSTSITSFTSSIFLLIMSADRYIAVCHPISSPRYRTLHIAKVVSAIAWSTSAVLMLPVILYASTVEQEDGINYSCNIMWPDAYKKHSGTTFILYTFFLGFATPLCFILSFYYLVIRKLRSVGPKPGTKSKEKRRAHRKVTRLVLTVISVYILCWLPHWISQVALIHSNPAQRDLSRLEILIFLLLGALVYSNSAVNPILYAFLSENFRKSFFKAFTCMNKQDINAQLQLEPSVFTKQGSKKRGGSKRLLTSNPQIPPLLPLNAGNNNSSTTTSSTTTAEKTGTTGTQKSCNSNGKVTAPPENLIICLSEQQEAFCTTARRGSGAVQQTDL
Protein: Mediator of RNA polymerase II transcription subunit 11 (Mediator complex subunit 11) (dMED21) (Q9VVS4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
Sequence:
MNPLDKIHALDEIEKEIILCMQSAGQALQELGKEKSSQKNAETQSQQFLKSLSSVESKLSEQINYLTQVSTGQPHEGSGYASAKVLQMAWHRIQHARSRVRELEETKAKHSHAARQQLKRQQEHAAAQQQQQQQQQQQQQQQQMQQAAQQQQQQTGGGNAGSGDHPMGGDSSMSTN
Protein: Mitochondrial outer membrane protein OM14 C-terminal domain-containing protein (Q5A8Z9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Uncharacterized protein
- tRNA threonylcarbamoyladenosine dehydratase
- Prn4p
- Tea1p
- SNAP receptor
Sequence:
MSSKAPSNEQIKKDVKKDADNIAKKGKEESEHLKKQGKEAVDEASEKGKEFIDQANKKGKELLDEANDKSKEFLKEARKELNHLEEEGQNLLSQFVAYVKSTANSIGQSLNKAGAELQSATSAAVSRTSVELQNPVVIAQIAVAAGGAAAGYLAYLERYRINTDNKYVVGIHASIITGLVVLDGYLFSTYYPKYDKKVAK
Protein: Triacylglycerol lipase SDP1 (EC 3.1.1.3) (Protein SUGAR-DEPENDENT 1) (Q9LZA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the release of fatty acids from the oil body in germinating seedlings. Can hydrolyze triacylglycerols and diacylglycerols but not monoacylglycerols, phospholipids, galactolipids or cholesterol esters. SDP1 lipase activity is required to limit triacylglycerol accumulation in roots, leaves and stems, which are vegetative tissues. Functions synergistically with PDAT1 in regulating fatty acid flow from membrane lipid synthesis toward peroxisomal beta-oxidation through a transient triacylglycerol pool.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:25775518}. Membrane {ECO:0000269|PubMed:16473965}; Peripheral membrane protein {ECO:0000305}. Peroxisome {ECO:0000269|PubMed:25775518}. Note=Associates with the oil body membrane (PubMed:16473965). Migrates from peroxisomes to the oil body surface through peroxisomal tubulation (PubMed:25775518). {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:25775518}.
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase 1
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Triacylglycerol lipase 1
- Diacylglycerol O-acyltransferase 3
- Phosphatidate phosphatase PAH1
- Putative phospholipid:diacylglycerol acyltransferase 2
- Phosphatidate phosphatase PAH2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 3
Sequence:
MDISNEASVDPFSIGPSSIMGRTIAFRVLFCRSMSQLRRDLFRFLLHWFLRFKLTVSPFVSWFHPRNPQGILAVVTIIAFVLKRYTNVKIKAEMAYRRKFWRNMMRTALTYEEWAHAAKMLEKETPKMNESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHSLQFFDQLGGVFSIVKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVPYHPPFNLDPEVGTKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKDLVRAYGGRFAAKLAHLVEMEVKHRCNQVLELGFPLGGLAKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIELALDDSVAILNHMRRLKKSAERAATATSSSHHGLASTTRFNASRRIPSWNVLARENSTGSLDDLVTDNNLHASSGRNLSDSETESVELSSWTRTGGPLMRTASANKFIDFVQSLDIDIALVRGFSSSPNSPAVPPGGSFTPSPRSIAAHSDIESNSNSNNLGTSTSSITVTEGDLLQPERTSNGFVLNVVKRENLGMPSIGNQNTELPESVQLDIPEKEMDCSSVSEHEEDDNDNEEEHNGSSLVTVSSEDSGLQEPVSGSVIDA
Protein: NifU-like protein 1, chloroplastic (AtCNfu1) (AtCnfU-IVb) (Q93W77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular scaffold for [Fe-S] cluster assembly of chloroplastic iron-sulfur proteins.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12553879, ECO:0000269|PubMed:15031412}.
Interaction partners:
- Iron-sulfur cluster assembly protein 1
- Cysteine desulfurase, mitochondrial
- Monothiol glutaredoxin-S14, chloroplastic
- Lipoyl synthase, chloroplastic
- Lipoyl synthase, mitochondrial
- Protein BOLA1
- Fe-S cluster assembly factor HCF101, chloroplastic
- Frataxin, mitochondrial
- Dihydroxy-acid dehydratase, chloroplastic
- Iron-sulfur cluster co-chaperone protein HscB homolog
Sequence:
MMASLATSISGSFRILVKSSSTRNGFPVISDQNPSFVLFANKRRHISRTAIFHRSAISGSSQGEKISPLASGVSSGLYSAQTFDLTPQNVDLVLEDVRPFLISDGGNVDVVSVEDGVVSLKLQGACTSCPSSSTTMTMGIERVLKEKFGDALKDIRQVFDEEVKQITVEAVNAHLDILRPAIKNYGGSVEVLSVEGEDCVVKYVGPESIGMGIQAAIKEKFKDISNVTFTS
Protein: C-type lectin domain family 4 member C (Blood dendritic cell antigen 2) (BDCA-2) (C-type lectin superfamily member 7) (Dendritic lectin) (CD antigen CD303) (Q8WTT0)
Organism: Homo sapiens (Human)
Function: Lectin-type cell surface receptor which may play a role in antigen capturing by dendritic cells. Specifically recognizes non-sialylated galactose-terminated biantennary glycans containing the trisaccharide epitope Gal(beta1-3/4)GlcNAc(beta1-2)Man. Binds to serum IgG. Efficiently targets ligand into antigen-processing and peptide-loading compartments for presentation to T-cells. May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells. May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11748283, ECO:0000269|PubMed:21880719}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Interleukin-3 receptor subunit alpha
- T-cell surface glycoprotein CD1c
- High affinity immunoglobulin epsilon receptor subunit gamma
- Thrombomodulin
- Neuropilin-1
- Integrin alpha-X
- Leukocyte immunoglobulin-like receptor subfamily A member 4
- Inter-alpha-trypsin inhibitor heavy chain H4
- T-cell surface antigen CD2
- High affinity immunoglobulin epsilon receptor subunit alpha
Sequence:
MVPEEEPQDREKGLWWFQLKVWSMAVVSILLLSVCFTVSSVVPHNFMYSKTVKRLSKLREYQQYHPSLTCVMEGKDIEDWSCCPTPWTSFQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICKMKKIYI
Protein: Protein JASON (F4IDQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. Acts as positive regulator of PS1 in male sporogenesis. Not involved in female meiosis.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Protein GIGAS CELL1
- Formin-like protein 14
- Kinesin-like protein KIN-7B
- Protein DYAD
- Protein POLLENLESS 3
- FHA domain-containing protein PS1
- MADS-box transcription factor PHERES 1
- Mitogen-activated protein kinase kinase 6
- Cyclin-A1-2
Sequence:
MRRLLMNRNLSPLCRSVLRFIDLSVCRAMACFLDCFRARDNRSTSNLVSHSSLANSRKAQDSQNDLSALFLSEEKSASSPCLDKERFDLDSIHIDKGLRDEARFLKACGTIPETPIEIRKASQKLSPQHSGSSHFHSWISSSSSMGSRLAESSTPMKACEEVGRPSFTSEQTASSCVIDVRDNARISSASSDGTEVESVGTAIKGELDRTARPTFTAGKNKSVRFECDLDQSNSSNSSENGSSRKPEMGGKICFTVSSPNPTPLKLSDEMQTPGTIYPANMESGGRGRPRIRSQFVHSVSNIMENASLYKVYKDSHEGLDYEEQIEAETPSSETYGEKVEESSDEKLSKFEASFSPWLNQINENIAALNERTPGVGVITPGDRPIIGLVAAQWIENEQTEISPKMWDGNGIPNSTTKYKEDQKVSWHATPFEVRLEKALSEEGGQSLFPQRKLEVMMEEVEGDTDISQLHHSVQPNSVVSF
Protein: Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (EC 1.2.1.13) (NADP-dependent glyceraldehydephosphate dehydrogenase subunit A) (P50362)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
Sequence:
MAAMMQKSAFTGSAVSSKSGVRAKAARAVVDVRAEKKIRVAINGFGRIGRNFLRCWHGRQNTLLDVVAINDSGGVKQASHLLKYDSTLGTFAADVKIVDDSHISVDGKQIKIVSSRDPLQLPWKEMNIDLVIEGTGVFIDKVGAGKHIQAGASKVLITAPAKDKDIPTFVVGVNEGDYKHEYPIISNASCTTNCLAPFVKVLEQKFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTTTGAAKAVSLVLPSLKGKLNGIALRVPTPTVSVVDLVVQVEKKTFAEEVNAAFREAANGPMKGVLHVEDAPLVSIDFKCTDQSTSIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAEVTAKKWVA
Protein: Protein RPN4 (Nuclear protein SON1) (Ubiquitin fusion degradation protein 5) (Q03465)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a transcriptional activator of a number of genes encoding proteasomal subunits. Binds to a PACE (proteasome-associated control element) DNA sequence 5'-GGTGGCAAA-3'. Its expression is in turn regulated by the 26S proteasome, thereby providing a negative feedback control mechanism. Required for normal growth at low temperatures.
Subcellular location: Nucleus.
Interaction partners:
- E3 ubiquitin-protein ligase UBR2
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit RPN10
- AP-1-like transcription factor YAP1
- 26S proteasome regulatory subunit RPN2
- 26S proteasome complex subunit SEM1
- Transcription factor PDR3
- Transcription factor PDR1
- 26S proteasome regulatory subunit 7 homolog
- Transcriptional activator HAC1
Sequence:
MASTELSLKRTLTDILEDELYHTNPGHSQFTSHYQNYHPNASITPYKLVNKNKENNTFTWNHSLQHQNESSAASIPPQQTYHFPIFNKYADPTLTTTTSFTTSEATANDRQINNVHLIPNEIKGASETPLQKTVNLKNIMKVSDPYVPTRNTFNYDVKISNDFFDNGDNLYGNDEEVLFYEDNYNPKMQWSLQDNSAAINNEDARAIFNNEFDSDDDDISDDEEDEIEENCLQQEQHQEEPLLSLDVTPISMFGSDQKTGRAKSSSHLFNEYSYVDSNMDSISSVVSEDLLDERGHEKIEDEDEDNDLDEDDIYDISLLKNRRKQSFVLNKNTIDFERFPSPSTSANVPSTATTGKRKPAKSSSNRSCVSNSNENGTLERIKKPTSAVVSSNASRRKLINYTKKHLSSHSSTNSNSKPSTASPSAHTSSSDGNNEIFTCQIMNLITNEPCGAQFSRSYDLTRHQNTIHAKRKIVFRCSECIKILGSEGYQKTFSRLDALTRHIKSKHEDLSLEQRQEVTKFAKANIGYVMG
Protein: Hypoxia-inducible factor 1-alpha (Q6EHI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Egl-9 family hypoxia-inducible factor 3.
- Hypoxia-inducible factor 1-alpha inhibitor
- Hypoxia-inducible factor 1 subunit alpha,-like
- Hypoxia-inducible factor 1-alpha
- hypoxia-inducible factor-proline dioxygenase
- Catenin beta-1
- Cellular tumor antigen p53
- Aryl hydrocarbon receptor nuclear translocator.
- Von Hippel-Lindau tumor suppressor.
- Cullin 2
Sequence:
MDTGVVTEKKRVSSERRKEKSRDAARSRRGKESEVFYELAHQLPLPHNVTSHLDKASIMRLTISYLRMRKLLNSDEKEEKEENELESQLNGFYLKALEGFLMVLSEDGDMVYLSENVSKSMGLTQFDLTGHSIFEFSHPCDHEELREMLVHRTGSKKTKEQNTERSFFLRMKCTLTSRGRTVNIKSATWKVLHCAGHVRVHEGSEASEDSGFKEPPVTYLVLICEPIPHPSNIEVPLDSKTFLSRHTLDMKFSYCDERITELMGYEPDDLLNRSVYEYYHALDSDHLTKTHHNLFAKGQATTGQYRMLAKKGGFVWVETQATVIYNPKNSQPQCIVCVNYVLSGIVEGDVVLSLQQTVTEPKAVEKESEETEEKTSELDILKLFKPESLNCSLESSTLYNKLKEEPEALTVLAPAAGDAIISLDFNNSDSDIQLLKEVPLYNDVMLPSSSEKLPLSLSPLTPSDSIPALTKLETGGEDFPFSSASDRVPDPTNTPSTSGLGSSGPNSPMDYGFPVEPDISSEFKLDLVEKLFAIDTEAKTPFSTQPMEDLDLEMLAPYIPMDDDFQLRIPSPLDPLPSATHSVSAMSSLFQPLPSSPASPASSTSSTVKQEASSRAPSPLHLLQEVCSAPVSPFSGSRDASPVRSSTPQSSSQLNNREMSPKMLAFQNIQRKRKLNEVTSLSEAVGLGALLHSVDSAIDPGKRAKVLEVKGSSVLGGNKTILILPSDVASRLLSSSLEGSGGLPQLTRYDCEVNAPVQDRHHLLQGEELLRALDQVN
Protein: Spn43Ac (Q6V6U7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPASVLL
Protein: Calmodulin-binding transcription activator, isoform H (A0A0B4LF06)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFYGAQNKLQLQLTRPKPTTIPTTTDMPSYLVFFDGEPIKLPDNLESLPRADSFPSQRHRWNTNEEIAAILISFDKHGEWQSKEVRTRPKSGSLLLYSRKKVRYRRDGYCWKKRKDGKTTREDHMKLKVQGTECIYGCYVHSAILPTFHRRCYWLLQNPDIVLVHYLNVPYPDDNKMAVIAPSITLWGDKKEWTKEELVSQLKPMLSTINSDDDSDSGNDIEISTAETVESIVCQLMEKQRLSRQAALVKQLDCGCGDGGCVDGKTCTHPVMRRSAAMLKSSVQEKRLGEPFNGNTPNVVVASKLYSRWAERPRQHVDNHGQFHNVTQQLPQESAIKFQIIPPQQQQQQDGNYQQQQYRGGSQMLAARSNLVMQQQQQHQQQQQYHQQQQQQQQQQQQHQQQQQHLSLQRFVASQGQNSVHLNQQHRLQIANTTITATASDPATTLAAAAAVAAASGATPVALNIMDTELIENQNHMTANKITNSGSSNSSSSNASKQLAGQTNNKLNVVNNNDPGNNNFMYNQQQQLNASSNSNNSSQQQQQQQQQHYYKLQQTTATPTSGQPPPLAQVQPHSLAQPPVEAMCMSPEHRSSSQPTPATSSAGSIPSSVSVSISVSTSTPTPAPTSISTPTSGTSSTSSSLQSIIDGNQQQQITTTSTAATCDNLMSANALSEDSHTVNNQATEAPNRSQLQSQSQSLSLNQNGCATYSASSDNSSQISDESSSFGGNNQNSSNSSTSEEEPQVEALSFFNETLDLSQEDIQRTLIANMPYNTTAAGATAPSTTITTGNTKLELSQQETKEKPAMGTETATEIEDDETDDVFANLDAFDMLVEFPELDLDDKQALNNTALEQSSFLGESAPSQPRKVHNICDFSPEWSYTEGGVKVLVAGPWTSSNGGAYTVLFDAQPVPTQLVQEGVLRCYCPAHEAGFVTLQVACGGFLVSNSVMFEYKLSLLADAPFDATSSNDCLYKFTLLNRLSTIDEKLQVKTEHELTTDNTALYLEPNFEEKLVAYCHKLIKHAWSMPSTAASWTVGLRGMTLLHLAAALGYAKLVGAMLNWRSENPHIILETELDALSQDVYGFTPLAWACVRGHVECSLLLYKWNHNALKIKTQAQQTPLDLASMRGHKVLLAQMYRLEKERCRKPQLRGGLANLSMNMGVEAEAEEQHQSFSAFDLELQRKHDGVFLRPVAVHSNQSPPNGSSRYSKRSSIDSGINMDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALCEVSTGESSPVHDKDCDDNSTSATDVTIGNDLVLPDAVVGDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRIKLQKERAEKEKLVHQRRAEYLQNLQFQGQQEMLVYHENNISAPSSGNTNASNNNNLHQIQSNQ