wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (95 kDa retinoblastoma-associated protein) (RBP95) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B) (O75150)
Organism: Homo sapiens (Human)
Function: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:10944455}.
Interaction partners:
- E3 ubiquitin-protein ligase BRE1A
- Ubiquitin-conjugating enzyme E2 A
- Ubiquitin-conjugating enzyme E2 B
- WW domain-containing adapter protein with coiled-coil
- Ubiquitin-conjugating enzyme E2 N
- Histone H2B type 2-E
- Parafibromin
- RNA polymerase II-associated factor 1 homolog
- Ubiquitin conjugating enzyme E2 V1
- Histone H2B type 1-O
Sequence:
MSGPGNKRAAGDGGSGPPEKKLSREEKTTTTLIEPIRLGGISSTEEMDLKVLQFKNKKLAERLEQRQACEDELRERIEKLEKRQATDDATLLIVNRYWAQLDETVEALLRCHESQGELSSAPEAPGTQEGPTCDGTPLPEPGTSELRDPLLMQLRPPLSEPALAFVVALGASSSEEVELELQGRMEFSKAAVSRVVEASDRLQRRVEELCQRVYSRGDSEPLSEAAQAHTRELGRENRRLQDLATQLQEKHHRISLEYSELQDKVTSAETKVLEMETTVEDLQWDIEKLRKREQKLNKHLAEALEQLNSGYYVSGSSSGFQGGQITLSMQKFEMLNAELEENQELANSRMAELEKLQAELQGAVRTNERLKVALRSLPEEVVRETGEYRMLQAQFSLLYNESLQVKTQLDEARGLLLATKNSHLRHIEHMESDELGLQKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQNLAANEQAGPINREMRHLISSLQNHNHQLKGDAQRYKRKLREVQAEIGKLRAQASGSAHSTPNLGHPEDSGVSAPAPGKEEGGPGPVSTPDNRKEMAPVPGTTTTTTSVKKEELVPSEEDFQGITPGAQGPSSRGREPEARPKRELREREGPSLGPPPVASALSRADREKAKVEETKRKESELLKGLRAELKKAQESQKEMKLLLDMYKSAPKEQRDKVQLMAAERKAKAEVDELRSRIRELEERDRRESKKIADEDALRRIRQAEEQIEHLQRKLGATKQEEEALLSEMDVTGQAFEDMQEQNGRLLQQLREKDDANFKLMSERIKANQIHKLLREEKDELGEQVLGLKSQVDAQLLTVQKLEEKERALQGSLGGVEKELTLRSQALELNKRKAVEAAQLAEDLKVQLEHVQTRLREIQPCLAESRAAREKESFNLKRAQEDISRLRRKLEKQRKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVRGRYEARQRKCPKCNAAFGAHDFHRIYIS
Protein: Tetratricopeptide repeat domain-containing protein PYG7, chloroplastic (Protein PALE YELLOW GREEN 7) (B9DHG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor. Cooperates with PSA3 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16679416}; Multi-pass membrane protein {ECO:0000255}. Note=Copurifies with PSI. {ECO:0000269|PubMed:16679416}.
Interaction partners:
- Photosystem I assembly factor PSA3, chloroplastic
- FAD/NAD
- Ycf3-interacting protein 1, chloroplastic
- At2g23670/F26B6.32
- At5g53080
- Succinate dehydrogenase subunit 3-1
- Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic
- Photosystem I iron-sulfur center
Sequence:
MFESNMVLQTLSSSSPPIHRLYLHHSQILPSSGSPSKISLQIHGRTLAIRSFHDYVFAEISARGLPALNKASLKKLPIKGSTFLLGQSLLMVSAHPQLAAAAEIIKPEPIYEVGELFELSIQLSYLLLLLGLLGVGTFYVIRQVLVRRELDLSAKELQEQVRSGDASATELFELGAVMLRRKFYPAANKFLQQAIQKWDGDDQDLAQVYNALGVSYVREDKLDKGIAQFEMAVKLQPGYVTAWNNLGDAYEKKKELPLALNAFEEVLLFDPNNKVARPRRDALKDRVKLYKGVVAVKSKKR
Protein: V-type proton ATPase subunit e (V-ATPase subunit e) (Vacuolar proton pump subunit e) (Q20591)
Organism: Caenorhabditis elegans
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). During embryonic development, the V-ATPase is required to repress fusion of epidermal cells probably by negatively regulating eff-1-mediated cell fusion.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15866168}; Multi-pass membrane protein {ECO:0000255}. Note=In late stage embryos, localizes to the apical cell membrane and partially to apical junctions of epidermal cells (PubMed:15866168). In the gut of 1.5-fold embryo, localizes to puctate structures (PubMed:15866168). {ECO:0000269|PubMed:15866168}.
Interaction partners:
- V-type proton ATPase subunit
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit C
- Probable V-type proton ATPase subunit G
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit S1
- Probable V-type proton ATPase subunit H 2
- V-type proton ATPase subunit B 1
Sequence:
MGILIPLVSVSAFWAIIGFGGPWIVPKGPNRGIIQLMIIMTAVCCWMFWIMVFLHQLNPLIGPQINVKTIRWISEKWGDAPNVINN
Protein: Fibronectin type III domain-containing protein 3B (Factor for adipocyte differentiation 104) (HCV NS5A-binding protein 37) (Q6NWW9)
Organism: Mus musculus (Mouse)
Function: May be positive regulator of adipogenesis.
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MYVTMMMTDQIPLELPPLLNGEVAMMPHLVNGEAAQQVILVQVNPGETFTIRAEDGTLQCIQGPAEVPMMSPNGSIPPIHVPPGYISQVIEDSTGVRRVVVTPQSPECYPPSYPSAMSPTHHLPPYLTHHPHFIQNSHTAYYPPVTVPGDMPPQFFPQPHLPPTIYSEPEIIPLYGMSSYVTREDQYSKPPHKKLKDRQIDRQNRLNSPPSTIYKNSCATVYNGYGKGHSGGSSGGGGGGSGGGPGIKKTERRARSSPKSSDSDLQEYELEVKRVQDILSGIEKPQVSNIQARAVVLSWAPPVGLSCGPHGGLSFPYSYEVALSDKGRDGKYKIIYSGEELECNLKDLRPATDYHVRVYAVYNSVKGSCSEPVSFTTHSCAPECPFPPKLAHRSKSSLTLQWKAPIDNGSKITSYLLEWDEGKRNSGFRQCFFGSQKHCKLTKLCPAMGYTFRLAARNDIGTSGYSQEVVCYTLGNIPQMPLAPRLVRAGVTWITLQWSRPEGCSPEEVITYTLDIQEDENDSHFHPKYTGEDLTCTVKNLKRSTQYKFRLTASNMEGKSCPSEVLVCTTSPDRPGPPTRPLIKGPVTSHGFSVKWDAPKDNGGSEIPKYLLEITDGTPEAGQWEVAYSGSATEYVFTHLKPGTLYKLRACCISTGGHSQCSESLPVRTLSLAPGQCRPPRVLGRPKHKGVHLEWDVPASESGCEVSEYSVEMTEPENVASEVYHGPELECTVGNLLPGTVYRFRVRALNDGGYGPYSDVSEITTAAGPPGQCRAPRVSFTPDGCVLVGWESPASPGADISEYRLEWGEDEQSLELVYHGPDTCFEMRDLLPAAQYCCRLQAFNPAGAGPYSELVHCQTPASAPDPVSTLCVLEEEPPSAHPDSPSVCLVLNWEEPCNNGSEILAYNIDLGDSCITVGNTTTHVMKNLLPETTYRIRIQAINEIGVGPFSQFIKAKTRPLPPSPPRLECAASGPQSLKLKWGDSNSKTHAAGDMVYTLQLEDRNKRFISIYRGPSHTYKVQRLTEFTCYSFRIQAMSEAGEGPYSETYTFSTTKSVPPTLKAPRVTQLEGNSCEIFWETVPPMRGDPVSYVLQVLVGRDSEYKQVYKGEEATFQISGLQSNTDYRFRVCACRRCVDTSQELSGAFSPSAAFMLQQREVMLTGDLGGMEEAKMKGMMPTDEQFAALIVLGFATLSILFAFILQYFLMK
Protein: Sodium-dependent nutrient amino acid transporter 1 (B4PZQ4)
Organism: Drosophila yakuba (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELKGVQPSNGSANGNGTTNAASTEKADTEKQTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIGFVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGLKYWKVALITSACGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWVYGLQNFCDDIEFMCNRRVSLYWRMCWSFFTPVMMIIIFIYSMATIEPIKYSELYFPEAANIAGWLLFAIGAAQFPLWGLWYASTHPQGTYWKSLKASLKPSDRWGPANPETRREWVIFKNQKAAQRATQKSTSKLGFFWRKLTNFCGSNK
Protein: Cell adhesion molecule 4 (Immunoglobulin superfamily member 4C) (IgSF4C) (Nectin-like protein 4) (NECL-4) (TSLC1-like protein 2) (Q8NFZ8)
Organism: Homo sapiens (Human)
Function: Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor-suppressor activity.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein PALS2
- Cell adhesion molecule 3
- Band 4.1-like protein 2
Sequence:
MGRARRFQWPLLLLWAAAAGPGAGQEVQTENVTVAEGGVAEITCRLHQYDGSIVVIQNPARQTLFFNGTRALKDERFQLEEFSPRRVRIRLSDARLEDEGGYFCQLYTEDTHHQIATLTVLVAPENPVVEVREQAVEGGEVELSCLVPRSRPAATLRWYRDRKELKGVSSSQENGKVWSVASTVRFRVDRKDDGGIIICEAQNQALPSGHSKQTQYVLDVQYSPTARIHASQAVVREGDTLVLTCAVTGNPRPNQIRWNRGNESLPERAEAVGETLTLPGLVSADNGTYTCEASNKHGHARALYVLVVYDPGAVVEAQTSVPYAIVGGILALLVFLIICVLVGMVWCSVRQKGSYLTHEASGLDEQGEAREAFLNGSDGHKRKEEFFI
Protein: Phosphatidylinositol 3-kinase VPS34 (EC 2.7.1.137) (PI3-kinase VPS34) (AtVPS34) (PI3K VPS34) (PtdIns-3-kinase VSP34) (P42339)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the negative regulation of proline, hydrophobic and aromatic amino acids accumulation, especially in response to salt (NaCl), either through inhibition of their synthesis and/or promotion of their catabolism. Triggers defense responses (e.g. pathogenesis related (PR1 and PR5) gene expression and hydrogen peroxide H(2)O(2) burst) to the bacterial pathogen compatible Pseudomonas syringae pv tomato DC3000 (Pst DC3000) and incompatible Pst DC3000 (avrRpt2), by regulating reactive ogygen species (ROS) production and by promoting stomatal closure.
Interaction partners:
- Serine/threonine-protein kinase VPS15
- Beclin-1-like protein
- Autophagy-related protein 101
- Autophagy-related protein 3
- Autophagy-related protein 16
- Autophagy-related protein 9
- Serine/threonine-protein kinase ATG1c
- Autophagy-related protein 11
- Serine/threonine-protein kinase ATG1a
- Serine/threonine-protein kinase ATG1b
Sequence:
MGANEFRFFLSCDINSPVTFRIEKLDGNLPVKKSSDSGVVSIAEEKKPELYIECALYIDGAPFGLPMRTRLKTTGPPYCWNELITLSSKYRDLTAHSQLAITVWDVSCGKTEGLIGGATVLLFNSKMQMKSGKQKLRLWQGKEADGSFPTSTPGKVPRHERGELERLEKLMNKYERGQIQSIDWLDRLMLKSLDTIKEQESTKHGSSHLFVVIDFCSFEHRVVFQESGANLFITAPIGSTNEFVTVWDTELGKTNPSENKQLKLARSLDRGIIDRDLKPSNIERKSIQRVLKYPPTRTLSGDERQLLWKFRFSLMSEKRALTKFLRCVEWSDVQEAKQAIQLMYKWEMIDVCDALELLSPLFESEEVRAYAVSVLERADDEELQCYLLQLVQALRFERSDRSCLSQFLVQRALQNIELASFLRWYVAVELHDHVYAKRFYSTYELLEENIIKLPPGVNGEDGYQLWQSLVRQTELTAQLCSITREVRNVRGNTQKKIEKLRQLLGGLLSELTYFEEPIRSPLTPNVLIKGIVAGESSLFKSALHPLRLTFRTPEEGGSCKLIFKKGDDLRQDQLVVQMVWLMDRLLKLENLDLCLTPYKVLATGHDEGMLEFIPSRSLAQILSEHRSITSYLQKFHPDEHAPFGITATCLDTFIKSCAGYSVITYILGIGDRHLDNLLLTDDGRLFHVDFAFILGRDPKPFPPPMKLCKEMVEAMGGAESQYYTRFKSYCCEAYNILRKSSNLILNLFHLMAGSTIPDIASDPEKGILKLQEKFRLDMDDEACIHFFQDLINESVSALFPQMVETIHRWAQYWR
Protein: Pancreatic secretory granule membrane major glycoprotein GP2 (Pancreatic zymogen granule membrane protein GP-2) (Q9D733)
Organism: Mus musculus (Mouse)
Function: Functions as an intestinal M-cell transcytotic receptor specific of type-I-piliated bacteria that participates in the mucosal immune response toward these bacteria. At the apical membrane of M-cells it binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to elicit a mucosal immune response.
Subcellular location: Zymogen granule membrane {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19218}. Secreted {ECO:0000250|UniProtKB:P19218}. Cell membrane {ECO:0000305|PubMed:19907495}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19218}. Apical cell membrane {ECO:0000269|PubMed:19907495}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19218}. Membrane raft {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19218}. Endosome {ECO:0000305|PubMed:19907495}. Note=Secreted, after cleavage, in the pancreatic juice. {ECO:0000250|UniProtKB:P19218}.
Interaction partners:
- GTP-binding protein 1
- Scavenger receptor cysteine-rich type 1 protein M130
- NPC intracellular cholesterol transporter 1
- Platelet glycoprotein V
- Chymotrypsin-like elastase family member 3B
- Platelet glycoprotein VI
- Protein lifeguard 4
- Pancreatic polypeptide prohormone
- Furin
Sequence:
MVGCDLLWLAAASCVLTLVSPSTIHQGYGRPRNSSNLDLDCGSPDSPSSGICFDPCQNHTVLNDPTRSTENNDSSVAWCDDNLHGWYRFVGDGGVKMPETCVSVFRCHTSAPMWLSGSHPILGDGIVSHTACANWNENCCFWRSEVQVKACSEELGEYHVYKLQGTPECSLRYCTDPSTAPKNCEITCRPEEECVFQNNNWSCVCRQDLHVSDSQSLQPLLDCGDNEIKVKLDKCLLGGMGFKEEIIAYLNDRNCNGTMQDEPNNWVSMTSPVVANYCGNILEKNGTHAIYRNTLSLATDFIIRDFRVNVNFQCAYPLDMSVSLETALQPIVSSLTVDVDGAGEFNVKMALFQDQSYTNPYEGAEVLLPVESILYVGVLLNRGDTSRFKLLLTNCYATPSEDRHDPVKYFIIKNRCPNQRDSTINVRENGVSSESRFSVQMFMFAGNYDLVFLHCEVYLCDSTTEQCQPSCSTNRLRSSRPAIDYNRVLDLGPITKRSAQSSATSKGTPHTTGFLLAWPMFFLPVFLALLF
Protein: Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase) (Q9WUB3)
Organism: Mus musculus (Mouse)
Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Glycogen debranching enzyme
- Phosphoglucomutase-1
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-amylase 1
- Receptor-interacting serine/threonine-protein kinase 3
- Pancreatic alpha-amylase 2a5
- Glycogen [starch] synthase, muscle
- Glucose 1,6-bisphosphate synthase
- Glycogen phosphorylase, liver form
Sequence:
MSRPLSDQDKRKQISVRGLAGVENVSELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGSRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERLDWDKAWDVTVKTCAYTNHTVLPEALERWPVHLMETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFSAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHIITLYNRIKREPNRFMVPRTIMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVERLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYIKCQDKVSELYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEKI
Protein: Biofilm growth-associated repressor (Q9PFB1)
Organism: Xylella fastidiosa (strain 9a5c)
Function: Represses an operon that comprises itself, XF_0764, XF_0765, XF_0766 and blh. Binds to a palindromic AT-rich sequence spanning the -10 region of the blh promoter and blocks transcription of the operon.
Interaction partners:
- Beta-lactamase hydrolase-like protein
- Probable membrane transporter protein XF_0764
- Probable transporter XF_0766
- Probable transporter XF_0765
Sequence:
MVNEMRDDTRPHMTREDMEKRANEVANLLKTLSHPVRLMLVCTLVEGEFSVGELEQQIGIGQPTLSQQLGVLRESGIVETRRNIKQIFYRLTEAKAAQLVNALYTIFCAQEKQA
Protein: Nurim (Nuclear envelope membrane protein) (Nuclear rim protein) (Q8IXM6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}; Multi-pass membrane protein {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}.
Interaction partners:
Sequence:
MAPALLLIPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLMAAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLRYLRAQLQRKLHLLSRPQDGEAE
Protein: ACT domain-containing protein ACR12 (Protein ACT DOMAIN REPEATS 12) (Q9LZ23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in feedback regulation of amino acid metabolism.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21861936}.
Interaction partners:
- ACT domain-containing protein ACR10
- ACT domain-containing protein ACR9
- Uncharacterized protein At4g15545
- At1g70770
- Phosphoglycerate mutase-like protein 1
- ACT domain-containing protein ACR7
- Aspartokinase 2, chloroplastic
- Aspartokinase 3, chloroplastic
- At5g16260 family protein)
- Aspartokinase 1, chloroplastic
Sequence:
MAFSSSIFSVTQFSSSLASRPSSAISRQTRFPAQIASPDLSPALFDDRRKFVGGVMSLLTKSIKNRVYASINSIDSAATPSYPKSEDDDDVVPMPMVMIDQDADPEATIVQLSFGNRLGALIDTMRALKDLGLDVIKGTVSTEGSIKQTKFSITKRDTGRKVEDPDLLEQIRLTIINNLLKYHPECSEQLAMGETFGIKAPEKKIDVDIATHIHVKEDGPKRSLLVIETADRPGLVVEMIKVMADVNIDVESAEIDTEGLVAKDKFHVSYQGQALNRSLSQVLVNCLRYFLRRPETDIDSY
Protein: UDP-glycosyltransferase 76C2 (EC 2.4.1.-) (Cytokinin-N-glucosyltransferase 2) (Q9FIA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the N-glucosylation of cytokinins. Catalyzes the formation of both the 7-N and the 9-N-glucosides.
Interaction partners:
- UDP-glycosyltransferase 76C1
- Histidine kinase 3
- Histidine kinase 2
Sequence:
MEEKRNGLRVILFPLPLQGCINPMLQLANILHVRGFSITVIHTRFNAPKASSHPLFTFLQIPDGLSETEIQDGVMSLLAQINLNAESPFRDCLRKVLLESKESERVTCLIDDCGWLFTQSVSESLKLPRLVLCTFKATFFNAYPSLPLIRTKGYLPVSESEAEDSVPEFPPLQKRDLSKVFGEFGEKLDPFLHAVVETTIRSSGLIYMSCEELEKDSLTLSNEIFKVPVFAIGPFHSYFSASSSSLFTQDETCILWLDDQEDKSVIYVSLGSVVNITETEFLEIACGLSNSKQPFLWVVRPGSVLGAKWIEPLSEGLVSSLEEKGKIVKWAPQQEVLAHRATGGFLTHNGWNSTLESICEGVPMICLPGGWDQMLNSRFVSDIWKIGIHLEGRIEKKEIEKAVRVLMEESEGNKIRERMKVLKDEVEKSVKQGGSSFQSIETLANHILLL
Protein: RE30730p (Q8SYW4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRLLGDVDQGGPAILSPRIHSFPFKLGLPLGLPSTFLGRYGWIQFYCKAALRENNGIIHKNHQVFIVMNPIDLNLEKPILAQPFTCEVEHKLGVVCVGGGQIKCRVSLDRGGYVPGENILVTAFISNYSNVSIKRTKASLTETIEYLARGKVVQTEKRELAVLVRGKIRPGAKDEWHNELYVPPLPPTNLHGCHLIKISYDVFFVIEPKSMEKEIKLQLPIVLATYPFRHSGDAVNANTWPESVLKPDTHTHYPSTLPIFRPWLHEKPIEA
Protein: Linoleate 13S-lipoxygenase 2-1, chloroplastic (EC 1.13.11.12) (Lipoxygenase 2-1) (O24370)
Organism: Solanum tuberosum (Potato)
Function: Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:17210991}. Plastid, chloroplast thylakoid {ECO:0000269|PubMed:17210991}. Note=Associated with the non-appressed part of the thylakoid membrane. {ECO:0000269|PubMed:17210991}.
Interaction partners:
- Fatty acid hydroperoxide lyase
- phospholipase A2
- Sugar-dependent1
- Triacylglycerol lipase SDP1
- Allene oxide synthase 2
- 12-oxophytodienoate reductase
- Alpha-DOX2
- Alpha-DOX2
- Allene oxide synthase
- Alpha-DOX1
Sequence:
MLKPQLQQSSQSTKALIPSWNTNPLFLASFPINILNKNFRLKKKNNFRVHHNYNGASTTKAVLSSTEKATGVKAVVTVQKQVNLNLSRGLDDIGDLLGKSLLLWIVAAELDHKTGIEKPGIRAYAHRGRDVDGDTHYEADFVIPQDFGEVGAILIENEHHKEMYVKNIVIDGFVHGKVEITCNSWVHSKFDNPDKRIFFTNKSYLPSQTPSGVSRLREEELVTLRGDGIGERKVFERIYDYDVYNDLGEADSNNDDAKRPVLGGKELPYPRRCKTGRPRSKKDPLSETRSTFVYVPRDEAFSEVKSVAFSGNTVYSVLHAVVPALESVVTDPNLGFPHFPAIDSLFNVGVDLPGLGDKKSGLFNVVPRLIKAISDTRKDVLLFESPQLVQRDKFSWFRDVEFARQTLAGLNPYSIRLVTEWPLRSKLDPKVYGPPESEITKELIEKEIGNYMTVEQAVQQKKLFILDYHDLLLPYVNKVNELKGSMLYGSRTIFFLTPQGTLKPLAIELTRPPVDDKPQWKEVYSPNDWNATGAWLWKLAKAHVLSHDSGYHQLVSHWLRTHCCTEPYIIASNRQLSAMHPIYRLLHPHFRYTMEINALAREALINANGVIESSFFPGKYAIELSSIAYGAEWRFDQEALPQNLISRGLAVEDPNEPHGLKLAIEDYPFANDGLVLWDILKQWVTNYVNHYYPQTNLIESDKELQAWWSEIKNVGHGDKRDEPWWPELKTPNDLIGIITTIVWVTSGHHAAVNFGQYSYAGYFPNRPTVARSKMPTEDPTAEEWEWFMNKPEEALLRCFPSQIQATKVMAILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEVFSGKLKELEGIIDARNNDSKLSNRNGAGVMPYELLKPYSEPGVTGKGVPYSISI
Protein: Cytochrome c2 (P86317)
Organism: Rhodopseudomonas palustris
Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Subcellular location: Periplasm {ECO:0000269|PubMed:20697695}.
Interaction partners:
Sequence:
QDAAKGEAVFKQCMTCHRADKNMVGPALAGVVGRKAGTAPGFSYSPLNHHSGEAGLVWTQENIITYLADPNAFLKKFLTDKGHADQAVGATKMTFKLANEQQRKDVVAYLATLK
Protein: Uncharacterized protein C10orf120 (Q5SQS8)
Organism: Homo sapiens (Human)
Interaction partners:
- Uncharacterized protein C2orf92
Sequence:
MIREWKNDCQRIEKQRASDTMVQERKNEKPVRIFNTNSSFQDQAPTCCQEDLSSASPLRIWSKFYRSDPRIALGKYSPLEKEILRLGGIHTIAARRLLAYKQEEECRMLKELQLLSPDYKQAMEYKKKHSSPCAICVPLEKIWTAKVIAPLEAFKMPQREQVNVSKHIERMRLARALGNHQPLPYIERFTRSSFLSGVGLGPMAKNKARRKEDNYDTHNCDDANQDKKEEAEGKNTKRREIKMNVVFKSKEPKKCLTYHGNDRKSFLPAKKPERSIAGLTNRNLFCISEFPGDLMLMNQDFISRRDHFSDLVKTYSLEEESIWKERMRKATPYHY
Protein: RING finger protein 141 (Zinc finger protein 230) (Q8WVD5)
Organism: Homo sapiens (Human)
Function: May be involved in spermatogenesis.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MGQQISDQTQLVINKLPEKVAKHVTLVRESGSLTYEEFLGRVAELNDVTAKVASGQEKHLLFEVQPGSDSSAFWKVVVRVVCTKINKSSGIVEASRIMNLYQFIQLYKDITSQAAGVLAQSSTSEEPDENSSSVTSCQASLWMGRVKQLTDEEECCICMDGRADLILPCAHSFCQKCIDKWSDRHRNCPICRLQMTGANESWVVSDAPTEDDMANYILNMADEAGQPHRP
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (K7EID9)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MMINLEARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDT
Protein: NADPH-dependent 3-keto-steroid reductase Hsd3b5 (3 beta-hydroxysteroid dehydrogenase type 5) (3 beta-hydroxysteroid dehydrogenase type V) (3 beta-HSD V) (EC 1.1.1.270) (Dihydrotestosterone 3-ketoreductase) (EC 1.1.1.210) (Q61694)
Organism: Mus musculus (Mouse)
Function: Responsible for the reduction of the oxo group on the C-3 of 5alpha-androstane steroids. Catalyzes the conversion of dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Does not function as an isomerase.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Cytochrome P450 7B1
- Cytochrome P450 7A1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Cholesterol side-chain cleavage enzyme, mitochondrial
- 17-beta-hydroxysteroid dehydrogenase type 6
- Estradiol 17-beta-dehydrogenase 2
- Aldo-keto reductase family 1 member D1
- 11-beta-hydroxysteroid dehydrogenase 1
Sequence:
MPGWSCLVTGAGGFLGQRIVRMLVQEEELQEIRALFRTFGRKHEEELSKLQTKAKVRVLKGDILDAQCLKRACQGMSAVIHTAAAIDPLGAASRQTILDVNLKGTQLLLDACVEASVPTFIYSSSVLVAGPNSYKEIILNAHEEEHRESTWPNPYPYSKRMAEKAVLATNGRLLKNGGTLHTCALRLPFIYGEECQVTSTTVKTALKNNSIIKKNATFSIANPVYVGNAAWAHILAARSLQDPKKSPSIQGQFYYISDNTPHQSYDDLNYTLSKEWGLCLDSGWSLPLSLLYWLAFLLETVSFLLRPVYNYRPPFNRLLITVLNSVFTISYKKAQRDLGYQPLVSWEEAKQKTSEWIGTLVKQHRETLHKKSQ
Protein: RH34413p (Q9VU35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 60 kDa heat shock protein homolog 2, mitochondrial
- 60 kDa heat shock protein homolog 1, mitochondrial
- ATP-dependent Clp protease proteolytic subunit
- Heat shock protein 83
- DnaJ-like-2, isoform A
- GrpE protein homolog, mitochondrial
- Heat shock protein 60A
- GM03767p
- Heat shock 70 kDa protein cognate 5
- AT04835p
Sequence:
MAAAIKKIIPMLDRILIQRAEALTKTKGGIVLPEKAVGKVLEGTVLAVGPGTRNASTGNHIPIGVKEGDRVLLPEFGGTKVNLEGDQKELFLFRESDILAKLE