wanglab/gogpt-training-data huggingface dataset:
Protein: Adhesin pMGA1.2 (Q9KH15)
Organism: Mycoplasmoides gallisepticum (Mycoplasma gallisepticum)
Interaction partners:
Sequence:
MKRKNILKFVSLLGIGSFVMLAAASCTSATTPTPNPEPKPTPNPEPKPDPMPNPPSGGMNGGDINPGGGQNMMDSAAQELTAARTALTSLLASKNANVEMYSDYAKIQNTLIAAYTTAEQTSQNSSATLEQVKNATSALQTAINTANSNKQKFDQDHSNLLMSYKNLMATLAKKETAVMTLKDPKYSAILDQINGVSSKGEELVQHTLDPVSGIVPAANTITEEITKIEEVISEKTLQDQKNNADQFANYQSFTLDKTKLENVEDAKKMGQPANYSFVGYSVDVTGTSGQETTIPNWNFAQRAIFTSGNQPTKVTATTTGEDQSTAKPLSDVSWIYSLAGTGAKYTLEFTYYGPSTGWLYFPYKLVKANDDVGLQYKLNSNETLTPIIFGEGTTTNGPAATVENINVAKVRLTGLAFGKNTIEFSVPMSKVAPMIGNMYITSSDTETNKQNIENSIFGNSVTTKNNITKISVDTLSAYSLASDWSTFIGQYSSDSLTLNGNRISDQKYYLIGYVGGNTGQRNITMVANTNQQRLPTASNQNTRSYTFYVNAPKAGAYYIKGVFTSEVRRDLKFSTGDMSSNNVTIQQLTTGNLTTLKTFDTSATEGPTRVTTVDTNRKTLTLVKGLNKIVVSGATANNGNAPNFGYLEFILNETQS
Protein: Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) (O15144)
Organism: Homo sapiens (Human)
Function: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 1B
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
Sequence:
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR
Protein: snRNA-activating protein complex subunit (SNAPc subunit) (Protein SHOOT REDIFFERENTIATION DEFECTIVE 2) (Q8L627)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator of small-nuclear RNA genes (snRNA), which have essential roles in pre-mRNA splicing and rRNA processing. Essential protein involved in the establishment of apical meristems and organ primordia, embryogenesis, cell differentiation and cell proliferation, probably by modulating the establishment of auxin gradients. Participates in the control of competence in cell proliferation; required for the reinitiation of the progression of the cell cycle and subsequent cell proliferation during cell redifferentiation leading to callus formation, especially during the first day of dedifferentiation (e.g. callus, root and shoot formation from root and hypocotyl explants).
Subcellular location: Nucleus {ECO:0000269|PubMed:16098103}.
Interaction partners:
- Transcription initiation factor IIA subunit 2
- Transcription initiation factor IIF subunit alpha
- TATA-box-binding protein 2
- TATA-box-binding protein 1
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase II subunit 4
- At1g75700
- Transcription initiation factor IIF, beta subunit
- Transcription initiation factor TFIID subunit 13
- DNA-directed RNA polymerases II, IV and V subunit 8B
Sequence:
MAMKEAFPEDYLSQEELEPSLNVSHHENPLAGRAKRKRTVKNTEVKKRTLKNTEVMKMTEKKTEEAYLVKVEQLAKLKQKQEEDKAAVTLHCFSKTSETGKDVVAPPEGFEQMQSLRFIDNNYTKLKPSDIQGQVDPLFPEVILCVEIYNSRKVKTQEFLVLGRQMLTELKDNIHCATDQVMQKAGKYDPSGYFLIEDVFHNDLRNPSAKDYSYPILDWLWNSKDEALKKWECVLTGELQKKQKLVLGEAKSVDLPRYRTADMQSTHFCDIRFRVGASYVYCHQGDCKHTIVIRDMRMSHPEDVQNRAAYPIMFWPKRRIQKCGVCKIKRASKVAVDDKWASENSSYFCDVCFELLHSEEGPLNCDFPVFDYVHE
Protein: Protein/nucleic acid deglycase 1 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Glyoxalase III) (EC 4.2.1.130) (Holding molecular chaperone) (Hsp31) (Maillard deglycase) (P31658)
Organism: Escherichia coli (strain K12)
Function: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities. However, these apparently disparate activities are all recruited to execute its protein deglycase primary function. Plays an important role in protecting cells from carbonyl stress, severe heat shock and starvation, as well as in acid resistance of stationary-phase cells.
Subcellular location: Cytoplasm.
Interaction partners:
- Hydroxyacylglutathione hydrolase GloB
- Lactoylglutathione lyase
- Hydroxyacylglutathione hydrolase GloC
- D-lactate dehydrogenase
- Glyoxylate/hydroxypyruvate reductase B
- Lactaldehyde dehydrogenase
- Quinone-dependent D-lactate dehydrogenase
- Glyoxylate/hydroxypyruvate reductase A
- Protein/nucleic acid deglycase 2
- Protein/nucleic acid deglycase 3
Sequence:
MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG
Protein: Lipoxygenase (EC 1.13.11.-) (A1XCI5)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MMNLNLKQPLVLPAHHSNVVGSRLSSSSPSAAAASRRTGGGVSSRSGSRRHVRLPRISCSATEEVSGAVSSVTVERMLTVTASVEASPAIGQMYFQRAVDDIGDLLGKTLLLELVSSELDAKSGVEKTRVTAYAHKTLREGHYEAEFKVPASFGPVGAVLVENEHHKEVFIKEIKLVTGGDSSTAVTFDCNSWVHSKFDNPEKRIFFTLKSYLPSDTPKGLEDLRKKDLQALRGDGHGERKVFERVYDYDVYNDLGDPDKNPAHQRPVLGGNKQYPYPRRCRTGRPRTKKDPETEMREGHNYVPRDEQFSEVKQLTFGATTLRSGLHALLPALRPLLINKKDLRFPHFPAIDDLFSDGIPLPAQTGFDAFRTVVPRMVKLVEDTTDHVLRFEVPEMIERDRFSWFKDEEFARQTIAGLNPLCIQLLTEFPIKSKLDPEVYGPAESAITKEILEKQMNGALTVEQALAAKRLFILDYHDVFLPYVHKVRELQDATLYASRTIFFLTDLGTLMPLAIELTRPKSPTRPQWKRAFTHGPDATDAWLWKLAKAHVLTHDTGYHQLVSHWLRTHCCVEPYIIAANRQLSRLHPVYRLLHPHFRYTMEINALAREALINADGIIEESFWPGKYAVELSSVAYGATWQFDTEALPNDLIKRGLAVRGEDGELELTIKDYPYAHDGLLVWDSIRQWASEYVNVYYKSDEAVAADPELRAFWDEVRNVGHGDKKDEPWWPVLDTRDSLVETLTTIMWVTSGHHSAVNFGQYHFAGYFPNRPTTIRKNMPVEEGGPGEEMEKFLKQPETTLLDMLPTQMQAIKVMTTLDILSSHSPDEEYMGEFAEPSWLAEPMVKAAFEKFGGRMKEIEGFIDECNNNLDLKNRCGAGIVPYELLKPFSKPGVTGRGIPSSISI
Protein: Transcriptional regulator np20 (Q9HT74)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Zinc import ATP-binding protein ZnuC
- High-affinity zinc uptake system membrane protein ZnuB
- High-affinity zinc uptake system protein ZnuA
- Probable transcriptional regulator
- Zinc finger/thioredoxin putative domain-containing protein
- Lipoprotein
- DUF2796 domain-containing protein
Sequence:
MYKIAPKTPLACQPHDHSQCVSTALAEADALCARQGVRLTELRRRVLELVWQSHKPLGAYDILAVLSETDGRRAAPPTVYRALDFLQENGLVHRIASLNAFVGCNNPEHSHQGQFLICRTCHTAIELEQPDISRAIVAGANSVGFAVESQTVEVVGLCGTCRDQKDA
Protein: Integral membrane protein TmpA (G5EB10)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSQPEEVIVTRPPTAVCVPESPSETSFVNIEKCIIKDVSELMLPDEPSFDLEAQSTARRLISPIRYTFLNIYRRLFTLVFLANIGVFVYVMVADRKLLALVNAAAANLLACGLARQPLVVNTIFFTVCSIPRSAPLWLRRIASKVYHYGGVHSGCGVASLIWYLGFIGEFSRQYWSGSSSPFSAAPIVLAYIILVLLLAIIIVAYPTFRFKRHDYFELTHRFSGWLIVALFVILLMVFVDEASAAEGKPMGRFLIELPAFWFLMLVVLAIIHPWLLLRKVKVTPEYLSPHAVRLHFSHTTTTFGKGIQLSKHPLQDWHGFATFPDVDRDGKSFSSLVSKAGDWTAATIKDQPTHLWKRGVLIYGFAYAMRVYKRVVVVTTGSGIGPCLSFLGDENRPSLRVIWQTRAPKRTYGKEVLNLVGRMDPNPVIIDTNSSGRLDMVPVIRQIAREHDAEAICVISNPFVTKKVVYELESMGIPAYGPIFDS
Protein: 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase BtrO (EC 1.14.14.13) (Butirosin biosynthesis protein O) (Q4H4E5)
Organism: Niallia circulans (Bacillus circulans)
Function: Monooxygenase component of a two-component system involved in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Together with BtrV, mediates hydroxylation of gamma-L-Glu-GABA-S-BtrI. Not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory. Octanoyl-S-[BtrI acyl-carrier protein] is also accepted as substrate.
Interaction partners:
Sequence:
MIALDTIQYYGQIPGVNHYNGKKEFMENAVKIAQLSDAYGIVGSLSFFNHSVLDPWAVSSVIMRHTERHVPLIALQPYMYPPYTAAKLIQSFTYLYDRRIDLNMITGAVTGELQQTGGYIDHSSRYKKLHEYVQVLRLLLESDSAVSFKGDYYELNNLEFKPLLPDKRLFPRIFMSGSSEEGLETGLKAADFVVTHPGPLEHFKRHFSEKVQGSAVQSAIRIEIIARESAEQAWKIAHARYPGNRQGKIQLRMKTNSESSWQRMLAELALASETYDEVFWMGGYMNGGIYSPVLVGDYEQVAAYLNEYYKLGVKAVLLGSMYSEEDFIHFSRVKEGISNPV
Protein: GTPase activating protein Gyp51 (Q10496)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase-activating protein involved in ER to Golgi trafficking and polarized exocytosis.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MAFTEANEREVQSSYEKENVKIIREEEAKDQESTDDIAVEDGTGTSPDLNFFSTQNVMQMNFEDEYSEFSNEDDEAEIDNSFADSIPNEPEIPDMQDEYSRDSHSQQSVEEQNNTTNTDEDASVNEFSVAADISDVNTLGKDNSESTEEPVNEVNETATLGNEDVGERSGFPSEGLDNEPESQRDLDETGNLAPEDLKDEVKSVHEFNEPNDLRQQEESYSDDDDTNVNEFEDVNEIENEHQLSVADEDQTSRLVKGKMIFVGKEDFGEEADISNSVFIEQNGPNSDTVSGFKETSSIVNSSSTTEKPGVALDSQNDTSIFNEEQTNSLTETFNDLTLDHLPENVESEPVAGKENETAKNESGASDNDHKANVHVFVLKSSEDAITLNEEKIATQDDPLEAPTPIVASSSTIFLNSNQRNDELSASGSQEPHPKDGTNSTSSLPLDTNNLSNSEPPSHVLDASSETIEVIQTIKKLQNQVPETIKDEVGKKNTAFSPGTSLSTNHVKTKSRSAHNNSTSPFSTAVSSWLNPLRYPSDKSPRVISSYLESVFISKPRSIGDAQKLEILEYLQSQSSTVSNQVFTLLSNFIQNPLFVLDECFDEFRNLILMHNSHTVHTVVWKTISSWTSYDYEMQYSSLSIKNCDSDKAIRKDLDRTFAPEILSHFFSNRQQLEPTDNIAESTANLHRVLRSLAIVLPQVGYTQGMSWIAGALLMHLPAPQAFALLVFLFKNYHLQNIFSSEMRGLSRVLHQFTRLVEDYMPSLAIHFKRQDIKTCSYASEWFLTLFAYKFPLEVVAHLYDILFLYGPGILFNFGLALLSHSQESLLKLNMDRLISYLKEDIFLAFKETQEGENYDTSLFVKTAFSFEIQPDVLDRYGNEYDILLKSEHELDSSLEEMRNRHKSLNEHFIMLSDSMANLQVEHENMSALLLKEKMYLKNQTVEQASLKSEIASLNSQLAKQKSEIEQAFQGDMEAIIAENLEIMVESQSLEDEIFRKEKQLAETKVNLAVLDEDHMMALQKWSQLMNRIKTK
Protein: DNA repair protein RAD51 homolog 3 (Q8SZ30)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- FI03211p
- X-ray repair cross complementing 2
- Rad51 recombinase D
- Breast cancer type 2 susceptibility protein homolog
- DNA repair protein Rad51 homolog
- DNA repair and recombination protein RAD54-like
- Fanconi anemia group D2 protein homolog
- Meiotic recombination protein W68
- Fanconi anemia group I protein homolog
- Mlh1, isoform A
Sequence:
MNHRFVRVWEPSQPEAIERRPSVSHENFRIFDKSCWDISQSASNKILTGKKALDTHFGGGISLGHLVELIGNSGTGKTQMCLQLCLNVQIPKAAGGLEGSALFIDTRQDFHPDRLMGLALKLERQYAHRVPEFKAHKMLQKIHYVRCPKLDQLMATVLSCHRHLVDHPDIKLIVIDSLAFTLRMLEDGAHRYEMLLELHESMRRLQRQHELTWVFTNVLTHRYVKQKFQVEPALGDLHSHLINERIWFSGSSELHLGKSWRTSRLIKESE
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (F1NQU9)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MGCVQCKDKEATKLTDERDGSLTQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHATGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSEKADGLCFNLTVIATNNTPQTVGLAKDAWEVARDSLFLEQKLGQGCFAEVWRGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGDNL
Protein: G-protein coupled receptors family 1 profile domain-containing protein (A0A060YJS0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ig-like domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Endothelin-3
- Neuropeptide Y
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
MDSFNSSGVDTFPVVNLNSSSESPYSSATIASLAALVSFLILFTVVGNVLVVIAVLTSRAMKAPQNLFLVSLATADILVATLVMPFSLANELMGYWYFGRVWCGIYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPKRVKCIIVIVWLISAMISSPPLISIDKNNDNSQYPGCELNNDTWYILSSSIASFFAPCLIMILVYIRIYQVAKTRTRGMSEKKHGPAALCKINGDRETGHCQASNKSMDLRSSVSMKKVSQAREKRFTFVLAVVMGVFVVCWFPFFFSYCLHGVCGDPCKIPDPLFKFFFWIGYCNSSLNPAIYTIFNQDFRRAFQKILCKSWKKSF
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (Q09816)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03155, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Spermidine synthase
- Adenine phosphoribosyltransferase
- Methylthioribose-1-phosphate isomerase
- Nucleolar protein 58
- AB hydrolase superfamily protein C1039.03
- 13 kDa ribonucleoprotein-associated protein
- Large ribosomal subunit protein eL22
- Silenced mating-type M-specific polypeptide Mc
- Inosine-5'-monophosphate dehydrogenase
- Telomerase reverse transcriptase
Sequence:
MNKQAEPILLGVIGGSGFYDLPGFDIVESVNPITPWGYPASPISIARTTSGFLIAFLARHGVGHIYTPTEVPSRANIAALKSLGVLAIVSFSAVGSLREDIPPEDFVLPTQIIDRTLCARPNTFFESGCVAHVSFGDPFDQDLYEILSSCGSNLKNGSKLHTKRKGDDLTVVCMEGPAFSTRAESNLYRSWGASIINMSVIPEAKLAREAEIAYQMVCMATDYDCWRMNEEPVTVETVMEHISNNKDNAKIFLLEAVKKLEAPLLQGFLGRNLRESVQNGIQTNHKHRNPDAIRRLQFLFPNLTIPH
Protein: Protein YobA (P0AA57)
Organism: Escherichia coli (strain K12)
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- Inner membrane protein YebZ
- Uncharacterized protein YebY
Sequence:
MASTARSLRYALAILTTSLVTPSVWAHAHLTHQYPAANAQVTAAPQAITLNFSEGVETGFSGAKITGPKNENIKTLPAKRNEQDQKQLIVPLADSLKPGTYTVDWHVVSVDGHKTKGHYTFSVK
Protein: Photosystem I reaction center subunit II, chloroplastic (Photosystem I 20 kDa subunit) (PSI-D) (Q39615)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side {ECO:0000250}.
Interaction partners:
Sequence:
MAVMMRTQAPAATRASSRVAVAARPAARRAVVVRAEAEAAPAAAKKAAEKPAWTVPTLNPDTPSPIFGGSTGGLLRKAQTEEFYVITWEAKKEQIFEMPTGGAAIMRQGPNLLKFGKKEQCLALTTQLRNKFKLTPCFYRVFPDGKVQYLHPADGVYPEKVNAGRVGANQNMRRIGQNVNPIKVKFSGRMMSPAEI
Protein: von Hippel-Lindau-like protein (VHL-like protein) (VLP) (Q6RSH7)
Organism: Homo sapiens (Human)
Function: Functions as a dominant-negative VHL to serve as a protector of HIFalpha.
Interaction partners:
Sequence:
MPWRAGNGVGLEAQAGTQEAGPEEYCQEELGAEEEMAARAAWPVLRSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNVNGQPVFANITLQCIP
Protein: Echinoderm microtubule-associated protein-like 1 (EMAP-1) (HuEMAP-1) (O00423)
Organism: Homo sapiens (Human)
Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules (PubMed:24859200, PubMed:25740311). Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity). {ECO:0000250|UniProtKB:Q05BC3, ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}.
Interaction partners:
- Tubulin beta-2A chain
- Echinoderm microtubule-associated protein-like 4
- ALK tyrosine kinase receptor
- Tubulin beta-2B chain
- Tubulin beta-3 chain
Sequence:
MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI
Protein: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHE1-B) (EC 1.2.4.1) (O44451)
Organism: Caenorhabditis elegans
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoacid dehydrogenase acyltransferase catalytic domain-containing protein
- Pyruvate kinase
- Malic enzyme
- Glucose-6-phosphate isomerase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Sequence:
MALRKCGNLFVARLAGTSTRAASTMTVRDALNQAMDEEIKRDDRVFLMGEEVAQYDGAYKISKGLWKKHGDKRVVDTPITEMGFAGIAVGAAFAGLRPICEFMTFNFSMQAIDQIINSAAKTYYMSAGRVPVPIVFRGPNGAAAGVAAQHSQDFSAWYAHCPGLKVVCPYSAEDAKGLLKAAIRDDNPVVFLENEILYGQSFPVGDEVLSDDFVVPIGKAKIERAGDHVTIVSYSRGVEFSLEAAKQLEAIGVSAEVINLRSLRPFDFESIRQSVHKTHHLVSVETGWPFAGIGSEIAAQVMESDVFDQLDAPLLRVTGVDVPMPYTQTLEAAALPTAEHVVKAVKKSLNIA
Protein: Mediator of RNA polymerase II transcription subunit 24 (Mediator complex subunit 24) (Thyroid hormone receptor-associated protein 4) (Thyroid hormone receptor-associated protein complex 100 kDa component) (Trap100) (mTRAP100) (Q99K74)
Organism: Mus musculus (Mouse)
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). Required for basal and activator-dependent transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MKVVNLKQAILQAWKERWSDYQWAINMKKFFPKGATWDILNLAEALLEQAMIGPSPNPLILSYLKYAISSQMVSCSSVLTAISKFDDFSRDLCVQALLDIMDMFCDRLSCHGKAEECIGLCRALLSALHWLLRCTAASAERLQEGLEAGTPAPGEKQLALCLQCLEKTLSSTKNRALLHIAKLEEASSWTAIEHSLLKLGEILANLSNPQLRSQAERCGTLIRSIPSMLSVHSEQLHKTGFPTIHALILLEGTMNLTGEMQPLVEQLMMVKRMQHIPTPLFVLEIWKACFVGLIESPEGTQELKWTAFTYLKIPQVLVKLKKYFHGEKDFTEDVNCAFEFLLKLTPLLDKADQRCNCDCTNFLLQECNKQGLLSEVNFASLVGKRTADRDPQLKSSENANIQPNPGLILRAEPTVTNILKTMDADHSKSPEGLLGVLGHMLSGKSLDLLLAAAAATGKLKSFARKFINLNEFTTHGSGESTKTASVRALLFDISFLMLCHVAQTYGSEVILSESSSGEEVPFFETWMQTCMPEEGKILNPDHPCFRPDSTKVESLVALLNNSSEMKLVQMKWHEACLSISAAILEILNAWENGVLAFESIQKITDNIKGKVCSLAVCAVAWLVAHVRMLGLDEREKSLQMIRQLAGPLYSENTLQFYNERVVIMNSILEHMCADVLQQTATQIKFPSTGVDTMPYWNLLPPKRPIKEVLTDIFAKVLEKGWVDSRSIHILDTLLHMGGVYWFCNNLIKELLKETRKEHTLRAVQLLYSIFCLDMQQVTLVLLGHILPGLLTDSSKWHSLMDPPGTALAKLAVWCALSSYSSHKGQASSRQKKRHREDIEDYVSLFPVEDMQPSKLMRLLSSSDDDANILSSPTDRSMNSSLSASQLHTVNMRDPLNRVLANLFLLISSILGSRTAGPHTQFVQWFMEECVGCLEQDSRGSILQFMPFTTVSELVKVSAMSSPKVVLAITDLSLPLGRQVAAKAIAAL
Protein: Cdc42 guanine nucleotide exchange factor 9 (A0A1B0GVC4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVVDIEDGRDDDFNVSMKNAFKLHNKETEEIHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKVPKQKGVNSARSVPPSYPPPQDPLNHGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRLTPFKK