wanglab/gogpt-training-data huggingface dataset:
Protein: Thioredoxin-1 (Q09433)
Organism: Caenorhabditis elegans
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Shown to facilitate the reduction of insulin disulfide bonds. Might play a role in the reversible nitrosylation of cysteine residues in target proteins, and thereby contributing to the response to intracellular nitric oxide. Shapes the ASJ sensory neuron biphasic response to nitric oxide (NO) exposure; trans-nitrosylation activity might inhibit calcium flux to the cytoplasm in ASJ neurons when exposed to a NO stimulus, whereas de-nitrosylation activity might promote calcium flux when NO is diminished. By regulating the NO-induced ASJ sensory neuron activity, mediates the avoidance response to NO-producing organisms like P.aeruginosa. Positively regulates life span extension under normal and caloric restriction conditions, dauer formation and the oxidative stress response. Contributes to the down-regulation of expression of the insulin-like neuropeptide daf-28 in the ASJ neurons in a redox-independent fashion, thereby promoting dauer formation. Negatively regulates the nuclear localization of the intestinal skn-1 transcription factor in a p38 MAPK pathway-dependent and redox-independent fashion.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase nsy-1
- Thioredoxin reductase 1
- Serpentine receptor class gamma-8
- Specificity protein transcription factor 1
Sequence:
MLKRCNFKNQVKYFQSDFEQLIRQHPEKIIILDFYATWCGPCKAIAPLYKELATTHKGIIFCKVDVDEAEDLCSKYDVKMMPTFIFTKNGDAIEALEGCVEDELRQKVLEHVSAQ
Protein: Casein kinase I isoform gamma-3 (CKI-gamma 3) (EC 2.7.11.1) (Q9Y6M4)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Protein smoothened
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
- G protein-coupled receptor kinase 3
- Beta-adrenergic receptor kinase 1
- Casein kinase I isoform gamma-1
- Casein kinase I isoform gamma-2
Sequence:
MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSKNQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAPTEVEVMDETKCCCFFKRRKRKTIQRHK
Protein: Cuticle collagen dpy-13 (Protein dumpy-13) (P17657)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Mutations in dpy-13 affects the body shape.
Interaction partners:
- COLlagen
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- Cuticle collagen dpy-5
Sequence:
MDIDTKIKAYRFVAYSAVVFSVIAVLSVCITLPIVYNYVHTVRRQLHNEALTCKGSMKDVWADVHHLRVDAASNRTARAVRYGRDDAAAGNGPNFDSGCEGCCQPGPQGAPGAPGKPGRPGKPGAPGFPGNPGKAPQKPCEEITPPPCKPCPQGPPGAPGLPGDQGDKGEAGQPGQPGSDAAPGEQGPKGPNGAPGKPGAPGAPGDEGLPAVCEPVQKGEPGSTGEPGPVGPPGPSGQPGNDGTPGQPGPKGPPGPDGKPGADGNPGQPGPVGPPGTPGERGICPKYCAIDGGIFFEDGTRR
Protein: Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-) (P35558)
Organism: Homo sapiens (Human)
Function: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis. Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle. At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor. The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:32322062}. Endoplasmic reticulum {ECO:0000269|PubMed:32322062}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000269|PubMed:32322062}.
Interaction partners:
- Pyruvate carboxylase, mitochondrial
- Pyruvate kinase PKLR
- Alpha-enolase
- ATP-citrate synthase
- Beta-enolase
- Enolase 4
- Malate dehydrogenase, mitochondrial
- Gamma-enolase
- Citrate synthase, mitochondrial
- Pyruvate kinase PKM
Sequence:
MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQMEEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPVLEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSLPGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWMFNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQVNADLPCEIEREILALKQRISQM
Protein: Serine and arginine rich splicing factor 3 (A0A0U1RRV7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRYLREHLLEKDIADLGQMKGNRRPVGKSGVQEITSFDRSMYRKLKFCLRLHKLGAFLRCFSCSNLFCLLEQ
Protein: Pfmc-2TM Maurer's cleft two transmembrane protein (Q8IJ11)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MFHYIYKIYIFTIILCASNLFNNNVVEIGTYKLSYHNGGIQFRMLAQKNDNKKSFGNTLTNILFKDKKKKNLDPQISSLVSLVDNMDITQEKKDKIKNLSLKYINSRDVKEKNESINELQKYSNNEECKEQMDNYLMHLRMQNDIKCLKRKNLWNNIWIVSTTLSLIIICIAFVFYLASTHVSSQLYYFAFSPLIFIIYIVARYFPDMKIGFKKLKTKLNTFFQNKKQITK
Protein: Papp-a2 (Pappalysin 2) (Pappalysin-2 isoform X1) (E9QCK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Insulin-like growth factor-binding protein 5
Sequence:
MMFFRLLAIILAVFHTWPLNSAQSDHIQKYKRTLAQRAERALAGEQCGSVSRKRPPRSTAHHYPLAGVSGRYTRLTDLHLRKTHTVRSCAGDCSSSAVELTNWDANEKETFVQPQEETFIWKKEGKRAQWVTDPASAKSLNPSKRISKGLPLQTEQGADFIDSLSKTRRVARSISEFNNEEVIPEKSYNHHTEYSTENEEYSGEQEGLQSTAGELWKAEVRDVPTKWMTGIYFSGQAEQLKVNPAFAIELPRSRFTIELWVKPEGGQNNPSIIAGVFDNCSHPLSEKGWSVGIQAADPTGRKDGRFFFSLRTDRSLKSTTIIGHQRYQPDSWTHVVASYDGHKMALYVDNFKAGESSEQSGDLYSSYIKACRLFLLGGDQSDHEHSFRGHLGGVALWGYARSHEELLKSHQPHSERQSPLLSQWADFSEVENQWVPYKDRHNPVIVALPVPELQLVSPFLPPPCGVTVCDNFDIALSYNKHWQMRAEKKIRYRVVNICKDNGSDPSVSLQQIQRQHQALEDAFHPYNITLELSIHTVYNSSLQRRFILSNCHIAKVGNRHCDPECDHPLTGHDGGDCLRMGPCYNWKRRDGVCNPECNSIHYDYDDGDCCDPEVTDVAKTCFDPESPQRAYLSVKELKELLHLSSSDMLNVFFANNSAREELAGVATWPWAKEALTHQGGMILNPAYFGTKGHNNTMIHEMGHIFGLYHVFKGVSERESCDDPCQETTASMETGDLCADTAPTPKSKACHDPDPVNDTCGLTQYKNTPYNNYMSYTDDDCTNHFTPNQVARMHCYIDLVYKTWVHERKPTPVPLAPVVVGQKADSVSIHWLNPISGPLAHREGDMNCQLCDENGALHQYAHEATSPHACDSTGYWTPEEAVGAPDVYQPCEPSMQAWSPEVNLYEPNMTTPCPQSEGCVLELHFLQPVLPDSLTVWITYTSANQKAIANIVFITENGELIHTGPQHAFCDIPLTLHVHTSKKVKAIKISTFDKKLEIDAVLLTSRPQNPLCSGCRPLLYRVIREPPIREDQSPAIVRQPSYTDSDVQKDVQYLYRIQVESDGLFSELSPSLLYTHGEHFCGDATLQGTEDCDDGNLLDGDGCSKKCHVEAGFKCHGQPSLCYVFEGDGVCEEFEKGSSIQDCGFFTPQGFNDQWASTALGSHQDQRCPASRVTGEPALTQMCKSQYFDINEIVAHEAWSPCTAHYTQDQSVWLQVGFERPGVAASVIIYLAYDGSWHGENCKKTVTIELCDTNGKRHLLGSYEVSCQRNPLVVNVTHNLSVPFYQTSAVQLNFSSSQVAVVAVALRTSCHFSAFALTGCVRRLCSTESCSPVNIEHASVRCTPALDSKHCSVSCHRGFILTVLHGQSLSSHQKEAELICVHGVWDRVVSCQPVDCGPPPPSHVYFASFSCPWGTTFGKQCTFSCNAPAILQGESDTLVCLEDGLWSYPEAYCKIECADPPFLPNATLLVPHCQGGGHDVGTVCRFKCNPGYYVTGTLNKKPRKKFLRLECLEGGTWQEGSCSPVTCPPLRPMFEGMYSCTNNFDFDSVCTLQCSDPTEKPSIRCTKDGRWTEDFTMCKKIVGSCQAPPEVNLVEYSCDEGFDVGAACYPTCIVPLSDPVVLANGSSADTVEHWMVPTKVQSIVCTGMLKWYPNPEQIHCIQSCEPFGGDGWCDTINNRAYCQYDGGDCCPSTLSSGKVIQFGVDCDQDECTCRDPEAGENKPKEKQQPGAP
Protein: Isoaspartyl peptidase/L-asparaginase (EC 3.4.19.5) (EC 3.5.1.1) (Asparaginase-like protein 1) (Beta-aspartyl-peptidase) (Isoaspartyl dipeptidase) (L-asparagine amidohydrolase) [Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain] (Q8C0M9)
Organism: Mus musculus (Mouse)
Function: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}. Note=Midpiece of sperm tail. In retina localizes in photoreceptor inner segment (PubMed:27106100). {ECO:0000250|UniProtKB:Q7L266, ECO:0000269|PubMed:27106100}.
Interaction partners:
- Asparagine synthetase
- Aspartate aminotransferase, cytoplasmic
- Adenylosuccinate synthetase isozyme 1
- Adenylosuccinate synthetase isozyme 2
- L-amino-acid oxidase
- Aspartate aminotransferase, mitochondrial
- Argininosuccinate synthase
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartoacylase
- Multifunctional protein CAD
Sequence:
MACARGTVAPPVRASIDVSLVVVVHGGGASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETRTRDLPC
Protein: Sterile alpha motif domain-containing protein 5 (SAM domain-containing protein 5) (Q3V1H9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28388653}.
Interaction partners:
- SAM and SH3 domain-containing protein 1
- Ephrin type-A receptor 5
Sequence:
MCTNIVYEWLRALQLPQYAESFVDNGYDDLEVCKQIGDPDLDAIGVLAPAHRRRILEAVHRLREQDAAAAGLYFTLEPQPVPPAPLVEAVPPGRRGEPCGSSAQGTRGDPRGQPGAPCSRELVSYPKLKLKIMIRDKLVRDGIHLSKPPYSRKVPMAGILEYLMNWPKSSQNH
Protein: Nuclear poly(A) polymerase 3 (PAP(III)) (Poly(A) polymerase III) (EC 2.7.7.19) (Polynucleotide adenylyltransferase 3) (Q56XM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:19956626}.
Interaction partners:
- 30-kDa cleavage and polyadenylation specificity factor 30
- FIP1[V]-like protein
- HEAT repeat-containing protein
- Symplekin
- Cleavage stimulation factor subunit 77
- Cleavage stimulating factor 64
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 3-I
- Flowering time control protein FY
Sequence:
MKKGGGRNKGFPQDDESSISLRQLMVNEGLIPSLEDEVKRRGVINQLRKIVVRWVKNVAWQHRLPQNQIDATNATILPYGSYGLGVYGSESDIDALCIGPFFASIAEDFFISLRDMLKSRREVSELHCVKDAKVPLIRFKFDGILVDLPYAQLRVLSIPNNVDVLNPFFLRDIDETSWKILSGVRANKCILQLVPSLELFQSLLRCVKLWAKRRGVYGNLNGFLGGVHMAILAAFVCGYQPNATLSSLLANFFYTFAHWQWPTPVVLLEDTYPSTGAPPGLMPIQLPCGSHQYCNSTITRSTFYKIVAEFLLGHNLTKDYLKLNFSWKDLFELYPYANTYTWFTKIHLSAANQEDLSDWVGWVKSRFRCLLIKIEEVYGICDPNPTEYVETYTKQPNIVFYWGLQLRTINVSDIESVKIDFLKNVNSGSFRGTVGRIQLTLVKASQLPKNGECGSNNRSKKVTKTCWRIREDKQCNNVPVYSKHLPGYVVGYQKMVNREADGMEVKC
Protein: Nanos homolog 3 (NOS-3) (P60323)
Organism: Homo sapiens (Human)
Function: Plays a role in the maintenance of the undifferentiated state of germ cells regulating the spermatogonia cell cycle and inducing a prolonged transit in G1 phase. Affects cell proliferation probably by repressing translation of specific mRNAs. Maintains the germ cell lineage by suppressing both Bax-dependent and -independent apoptotic pathways. Essential in the early stage embryo to protect the migrating primordial germ cells (PGCs) from apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:21421998}. Cytoplasm {ECO:0000269|PubMed:21421998}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P60324}. Cytoplasm, P-body {ECO:0000250|UniProtKB:P60324}. Note=Co-localizes with PUM2, EIF2S1 and TIAL1 in the stress granules. Co-localizes with DCP1A in the P-body. {ECO:0000250|UniProtKB:P60324}.
Interaction partners:
- Deleted in azoospermia-like
- Pumilio homolog 2
- Dead end protein homolog 1
- PR domain zinc finger protein 14
- Pumilio homolog 1
Sequence:
MGTFDLWTDYLGLAHLVRALSGKEGPETRLSPQPEPEPMLEPDQKRSLESSPAPERLCSFCKHNGESRAIYQSHVLKDEAGRVLCPILRDYVCPQCGATRERAHTRRFCPLTGQGYTSVYSHTTRNSAGKKLVRPDKAKTQDTGHRRGGGGGAGFRGAGKSEPSPSCSPSMST
Protein: Uncharacterized protein (Q5ARM6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MRSSIALVLAVGTAALADFTFDELWALQNTLWDNFLYPANLQQINATDTSVFAENVQGRVDITRTFDGRELNNEYIFGLFSDPSHLSLVGIPISYNITQFAANQNITSATTVFTFNATSFNILVPITIDTWILYNADGKILQYDATFRWFGWLLDTLLEAAGTGIFNTTDPAETQRALGNLLATTICQTHGQHCVDDNQQYNSNEDCVRFLTEDIRFGSAYELGRNTLLCREVHEHMVQYRPTEHCPHIGPDGGGYCVDDKDYAEVVTERYFREPFVPYGYGDTNLWVAA
Protein: Ceruloplasmin (Cuproxidase ceruloplasmin) (EC 1.16.3.4) (Ferroxidase ceruloplasmin) (EC 1.16.3.1) (Glutathione peroxidase ceruloplasmin) (EC 1.11.1.9) (Glutathione-dependent peroxiredoxin ceruloplasmin) (EC 1.11.1.27) (P00450)
Organism: Homo sapiens (Human)
Function: Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16150804}. Note=Colocalizes with GCP1 in secretory intracellular compartments. {ECO:0000250|UniProtKB:P13635}.
Interaction partners:
- Ferroportin
- Copper-transporting ATPase 2
- Lactotransferrin
- Myeloperoxidase
- Haptoglobin
- Frataxin, mitochondrial
- Alpha-1-antitrypsin
- Heme oxygenase 1
- Copper-transporting ATPase 1
- Albumin
Sequence:
MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVEPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
Protein: Diacylglycerol O-acyltransferase 2D (GmDGAT2D) (EC 2.3.1.20) (K7K424)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Involved in triacylglycerol (TAG) synthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Can use oleoyl-CoA and linoleoyl-CoA as substrates. May play a role in TAG biosynthesis in different tissues in responses to environmental and hormonal cues.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27345221}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q9ASU1}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1B
- Diacylglycerol O-acyltransferase 1A
- diacylglycerol O-acyltransferase
- Diacylglycerol O-acyltransferase 1C
- Diacylglycerol O-acyltransferase 3-2
- Diacylglycerol O-acyltransferase 3-1
- Acyltransferase
- Acyltransferase
- Acyltransferase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
Sequence:
MAAEPVSDGGAAAEKLISGREEFGDSSNLFSAILAMVLWLGAIHFNIALILLAVFFLPLSKSLLVFGFLFGFMVLPINEKSRFGRRLSRFICKHACNYFPITLHVEDMKAFDPNRAYVFGYEPHSVLPIGIVALADHTGFMPLPKVKVLASSTVFYTPFLRHLWTWLGLTPATKKNFISLLASGHSCILIPGGVQEAFHMQHGTEIAFLKARRGFVRVAMVKGKPLVPVFCFGQSNVYKWWKPGGKLFLKFARAIKFTPICFWGIFGSPLPFRHPMHVVVGRPIEVDKNREPTTEEVAKIHGLFVEALQDLFERHKARAGYPNLELRIV
Protein: Cell division cycle 20.2, cofactor of APC complex (AtCDC20.2) (Q9S7I8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:21687678}.
Interaction partners:
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 8
- Mitotic spindle checkpoint protein MAD2
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 5
- Mitotic checkpoint protein BUB3.1
- Anaphase-promoting complex subunit 1
- Cell division cycle protein 27 homolog B
Sequence:
MDAGLNRCPLQEHFLPRKNSKENLDRFIPNRSAMNFDYAHFALTEERKGKDQSATVSSPSKEAYRKQLAETMNLNHTRILAFRNKPQAPVELLPSNHSASLHQQPKSVKPRRYIPQTSERTLDAPDIVDDFYLNLLDWGSANVLAIALDHTVYLWDASTGSTSELVTIDEEKGPVTSINWAPDGRHVAVGLNNSEVQLWDSASNRQLRTLKGGHQSRVGSLAWNNHILTTGGMDGLIINNDVRIRSPIVETYRGHTQEVCGLKWSGSGQQLASGGNDNVVHIWDRSVASSNSTTQWLHRLEEHTSAVKALAWCPFQANLLATGGGGGDRTIKFWNTHTGACLNSVDTGSQVCSLLWSKNERELLSSHGFTQNQLTLWKYPSMVKMAELTGHTSRVLYMAQSPDGCTVASAAGDETLRFWNVFGVPETAKKAAPKAVAEPFSHVNRIR
Protein: LD07615p (Q8SZI4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSLIVLCVHIYVYVYVSKIYLVCILTKRYAKTALPAGEQNRQTTAKTNEIIPLSIESDLANPRRLVTNSTNPSMVSRWSQRTLSRLISTAPPLEFCFPFILDLEIFQL
Protein: hydroxyacylglutathione hydrolase (EC 3.1.2.6) (Glyoxalase II) (C0H490)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Glyoxalase I-like protein GILP
- Lactoylglutathione lyase
- hydroxyacylglutathione hydrolase
- GDP-L-fucose synthase
Sequence:
MKPCAQVLVVPVLNDNFSYVIIDEKTKKAASIDPVEPDKVLKRIETANVELEYVLCTHHHYDHSGGNIRMRELKQNIKVVGSAYEPTPGVNEKVYDGQIIRLGELNIKAIHAPCHTKGHILYYVYKTDEAKQEDHKYKPILFTGDTLFIAGCGRFFEGSAKDMFKNIEKVKNMRKETLIYCGHEYTLNNLRFALSIENDNEYMKNKLNEVTEKLKNKEHSVPSTIEEENLINPFFRTHCYVNKFNMNDEIKILDKLRQLKNNF
Protein: Phosphate regulon transcriptional regulatory protein PhoB (Q3K4G1)
Organism: Pseudomonas fluorescens (strain Pf0-1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVGRSILIVDDEAPIREMIAVALEMAGYDCLEAENSQQAHAIIVDRKPDLILLDWMLPGTSGIELARRLKRDELTGDIPIIMLTAKGEEDNKIQGLEVGADDYITKPFSPRELVARLKAVLRRAGPTDGEAPIEVGGLLLDPISHRVTIDGRPAEMGPTEYRLLQFFMTHQERAYTRGQLLDQVWGGNVYVEERTVDVHIRRLRKALGDAYENLVQTVRGTGYRFSTKA
Protein: Magnetosome protein MamA (P0DO20)
Organism: Paramagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
Function: Probably forms a large homooligomer on which other magnetosome subunits assemble. Required for formation of functional magnetosomes from pre-existing vesicles.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:16707673}; Peripheral membrane protein {ECO:0000269|PubMed:16707673}. Note=Reversibly binds to magnetosomes (PubMed:16707673). Forms oligomers that cover the surface of the magnetosome (By similarity). {ECO:0000250|UniProtKB:Q2W8Q0, ECO:0000269|PubMed:16707673}.
Interaction partners:
Sequence:
MSSKPSDILDEVTLYAHYGLSVAKKLGMNMVDAFRAAFSVNDDIRQVYYRDKGISHAKAGRYSQAVMLLEQVYDADAFDVDVALHLGIAYVKTGAVDRGTELLERSLADAPDNVKVATVLGLTYVQVQKYDLAVPLLIKVAEANPINFNVRFRLGVALDNLGRFDEAIDSFKIALGLRPNEGKVHRAIAFSYEQMGRHEEALPHFKKANELDEGASV
Protein: Protein FAM228A (Q86W67)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAATKTASYDEHFRPEKLREWPEPESVSLMEVLAREDIDEAVCAILFKENSIVKVTVPPFVDPLFQRQQEVDEERRTGLQCETGKRHSIKELEEIEKARLHASSPYFTFTSHCVIPKEWHKASARARSKTYKYSPEKLIYADKKQKRKEKKTADLSQAAFERQFLSSKLSQKNKVGERKGLVSRGLGRGWHAGLCSTHEQHILVPE