wanglab/gogpt-training-data huggingface dataset:
Protein: F-box/WD repeat-containing protein sel-10 (Egg laying defective protein 41) (Suppressor/enhancer of lin-12 protein 10) (Q93794)
Organism: Caenorhabditis elegans
Function: Probable substrate recognition component of SCF (SKP1-CUL-F-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates synapse elimination in early development in the motor neuron HSNL. Cell autonomous negative regulator of lin-12/Notch-mediated signaling, with respect to lin-12 activity in cell fate decisions and tumorigenesis. May target the intracellular domains of lin-12/Notch proteins for ubiquitin-dependent degradation. Involved in sex determination by promoting female development. Potential regulator of presenilin. May have a role in egg laying. Regulates zyg-1 levels (possibly redundantly with lin-23) to control centrosome duplication during mitosis. Negatively regulates lin-45 activity and protein stability, probably by targeting it for ubiquitination and proteasomal degradation.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:17626846}. Cytoplasm {ECO:0000269|PubMed:19528325}. Note=Expressed throughout the axon throughout development. {ECO:0000269|PubMed:17626846}.
Interaction partners:
- Skp1-related protein
- RING-box protein 1
- F-box domain-containing protein
- F-box/WD repeat-containing protein lin-23
- Cullin-1
- Presenilin sel-12
- Protein lin-12
- Cell division control protein
- Cullin-3
- RING-box protein 2
Sequence:
MWPRNDVHMDDGSMTPEDQEPVTDNDMEYNDNGEESSYSNGSSSSYNADKLSSSRPLQHKLDLSASPSRNNDLNPRVEHLIALFKDLSSAEQMDAFTRLLQESNMTNIRQLRAIIEPHFQRDFLSCLPVELGMKILHNLTGYDLLKVAQVSKNWKLISEIDKIWKSLGVEEFKHHPDPTDRVTGAWQGTAIAAGVTIPDHIQPCDLNVHRFLKLQKFGDIFERAADKSRYLRADKIEKNWNANPIMGSAVLRGHEDHVITCMQIHDDVLVTGSDDNTLKVWCIDKGEVMYTLVGHTGGVWTSQISQCGRYIVSGSTDRTVKVWSTVDGSLLHTLQGHTSTVRCMAMAGSILVTGSRDTTLRVWDVESGRHLATLHGHHAAVRCVQFDGTTVVSGGYDFTVKIWNAHTGRCIRTLTGHNNRVYSLLFESERSIVCSGSLDTSIRVWDFTRPEGQECVALLQGHTSLTSGMQLRGNILVSCNADSHVRVWDIHEGTCVHMLSGHRSAITSLQWFGRNMVATSSDDGTVKLWDIERGALIRDLVTLDSGGNGGCIWRLCSTSTMLACAVGSRNNTEETKVILLDFDAVYP
Protein: Conserved protein (O05310)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- PASTA domain-containing protein
- Probable DNA-3-methyladenine glycosylase I TagA
- Inactive dihydropteroate synthase 2
- Glucosyl-3-phosphoglycerate synthase
- AP-4-A phosphorylase
- Conserved protein
- Possible conserved membrane protein
- Conserved alanine valine rich protein
- Conserved protein
- Uncharacterized protein Rv2091c
Sequence:
MALVLVYLVVLVLVAIVLFAAASLLFGRGEQLPPLPRATTATTLPAFGVTRADVDAVKFTQVLRGYKTSEVDWVLERLGRELEALRSQLGAIHASSEDAEAESDASNPSRGETVVHYRSDPA
Protein: Rho-related GTP-binding protein Rho6 (Rho family GTPase 1) (Rnd1) (Q8BLR7)
Organism: Mus musculus (Mouse)
Function: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Plexin-B1
- Plexin-A1
- Plexin-A2
- Plexin-B3
- Plexin-B2
- Plexin-A3
- Plexin-A4
- Rho-related GTP-binding protein RhoD
- Rho GTPase-activating protein 35
- Transforming protein RhoA
Sequence:
MKERRAPQPVVVRCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETMDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSETSIHSIFRTASMVCLNKSSPVPPKSPVRSLSKRLLHLPSRSELISTTFKKEKAKSCSIM
Protein: Platelet glycoprotein V (GPV) (Glycoprotein 5) (CD antigen CD42d) (O08742)
Organism: Mus musculus (Mouse)
Function: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein IX
- Platelet glycoprotein Ib beta chain
- Platelet glycoprotein Ib alpha chain
- von Willebrand factor
- Sialoadhesin
- CD151 antigen
- Tyrosine-protein kinase Lyn
- Platelet glycoprotein VI
- Pancreatic secretory granule membrane major glycoprotein GP2
- Integrin alpha-IIb
Sequence:
MLRSALLSAVLPLLRAQPFPCPKTCKCVVRDAAQCSGGSVAHIAELGLPTNLTHILLFRMDQGILRNHSFSGMTVLQRQMLSDSHISAIDPGTFNDLVKLKTLRLTRNKISRLPRAILDKMVLLEQLFLDHNALRDLDQNLFQQLRNLQELGLNQNQLSFLPANLFSSLRELKLLDLSRNNLTHLPKGLLGAQVKLEKLLLYSNQLTSVDSGLLSNLGALTELRLERNHLRSVAPGAFDRLGNLSSLTLSGNLLESLPPALFLHVSSVSRLTLFENPLEELPDVLFGEMAGLRELWLNGTHLSTLPAAAFRNLSGLQTLGLTRNPRLSALPRGVFQGLRELRVLGLHTNALAELRDDALRGLGHLRQVSLRHNRLRALPRTLFRNLSSLESVQLEHNQLETLPGDVFAALPQLTQVLLGHNPWLCDCGLWRFLQWLRHHPDILGRDEPPQCRGPEPRASLSFWELLQGDPWCPDPRSLPLDPPTENALEAPVPSWLPNSWQSQTWAQLVARGESPNNRLYWGLYILLLVAQAIIAAFIVFAMIKIGQLFRTLIREKLLLEAMGKSCN
Protein: tRNA (carboxymethyluridine(34)-5-O)-methyltransferase (EC 2.1.1.229) (tRNA (uracil-5-)-methyltransferase trm9) (tRNA [Um34] methyltransferase) (tRNA methylase 9) (Q10224)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional methyltransferase subunit trm112
- Cytoplasmic tRNA 2-thiolation protein 1
- Putative acyl-CoA-binding protein
- Cytoplasmic tRNA 2-thiolation protein 2
- Elongator complex protein 1
- Elongator complex protein 2
- Uncharacterized protein P8A3.02c
- Elongator complex protein 3
Sequence:
MEIEYENEYVHQVYDKIATHFSDTRYKPWPVVEKFLKSLPLGSVGVDIGCGNGKYQKVNPNVYMIGSDRCVKLVKIASNLGPMVISDGLHVPHPSNRFDFALSIAVIHHFSNENRRLQAVQEVLRPLVKGGKALFFVWALEQKNSRRGFSEDGPQDVYVPWILKRQYEYPNAKPEELKGHDPAENIAYQRYYHLFRKGELNELVETAGGSILEHGYDRDNWWVIAEKN
Protein: At4g12735 (Q8LCC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At5g03100
- Transmembrane protein, putative
- Probable serine/threonine-protein kinase PBL23
- Beta-glucosidase 8
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Serine carboxypeptidase-like 20
- Amine oxidase [copper-containing] zeta, peroxisomal
- Actin-related protein 9
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- RuvB-like protein 1
Sequence:
MSLFTLFFACFVPKSGSRINTTDSNLEVLSLKKPKRKTESIRTPTIVVSYFPVGSNLSRL
Protein: A-kinase anchor protein 2 (AKAP-2) (Q5U301)
Organism: Rattus norvegicus (Rat)
Function: Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:O54931}; Lipid-anchor, GPI-like-anchor {ECO:0000250|UniProtKB:O54931}; Cytoplasmic side {ECO:0000250|UniProtKB:O54931}. Note=Accumulates near the inner, apical surface of highly polarized epithelium in tubules of nephrons. {ECO:0000250|UniProtKB:O54931}.
Interaction partners:
- Paralemmin 2.
- Paralemmin A kinase anchor protein
- Lens fiber major intrinsic protein
Sequence:
MEIGVSVAECKSVPGITSTPHSKDHSSPFYSPSHNGLLTDHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSATKVEPIEKASGRQLPPHIELSRSPSDSMAEGERANGHSTDQPQDMLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEHEKEQFCIRKVRPSEEMIELEKERRELIRSQAVKKNPGIAAKWWNPPQKKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQLQQLQQQQQQQLSTSQLCTAPAAHEHLDSIEHTKEDVVTEQIDFSAARKQFQQMENSRQTLAKGQSTPRLFSIKPFYKPLGSINSDKPPTILRPATIGGTVEDSSTQAAKEQKALCVSESQSAGAGTGNAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPNALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEVHTSKEGSEQQEPGAMVEEAGSQAPGSEKPQGMFAPPQVSSPVQEKRDVLPKILPGEDKTLREKGPSQPPTAVQPSGPVNMKETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAQNAPSLPSRTTCYKTAPGKIEKVKPPPSPTTEGPSLQPDLAPEEAAGAQRPKNLMQTLMEDYETHKSKRRERMDDSSVLEATRVNRRKSALALRWEAGIYANQEEEDNE
Protein: ESX-5 secretion system protein EccA5 (ESX conserved component A5) (Type VII secretion system protein EccA5) (T7SS protein EccA5) (P9WPI1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ESX-5 specialized secretion system, which is responsible for the secretion of EsxN and a number of PE_PGRS and PPE proteins, including PPE41. EccA5 exhibits ATPase activity and may provide energy for the export of ESX-5 substrates (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:B2HSU9}.
Interaction partners:
- Mycosin-5
- ESX-5 secretion system protein EccE5
- ESX-5 secretion system protein EccD5
- ESX-5 secretion system ATPase EccB5
- ESX-2 secretion system ATPase EccB2
- ESX-5 secretion-associated protein EspG5
Sequence:
MTRPQAAAEDARNAMVAGLLASGISVNGLQPSHNPQVAAQMFTTATRLDPKMCDAWLARLLAGDQSIEVLAGAWAAVRTFGWETRRLGVTDLQFRPEVSDGLFLRLAITSVDSLACAYAAVLAEAKRYQEAAELLDATDPRHPFDAELVSYVRGVLYFRTKRWPDVLAQFPEATQWRHPELKAAGAAMATTALASLGVFEEAFRRAQEAIEGDRVPGAANIALYTQGMCLRHVGREEEAVELLRRVYSRDAKFTPAREALDNPNFRLILTDPETIEARTDPWDPDSAPTRAQTEAARHAEMAAKYLAEGDAELNAMLGMEQAKKEIKLIKSTTKVNLARAKMGLPVPVTSRHTLLLGPPGTGKTSVARAFTKQLCGLTVLRKPLVVETSRTKLLGRYMADAEKNTEEMLEGALGGAVFFDEMHTLHEKGYSQGDPYGNAIINTLLLYMENHRDELVVFGAGYAKAMEKMLEVNQGLRRRFSTVIEFFSYTPQELIALTQLMGRENEDVITEEESQVLLPSYTKFYMEQSYSEDGDLIRGIDLLGNAGFVRNVVEKARDHRSFRLDDEDLDAVLASDLTEFSEDQLRRFKELTREDLAEGLRAAVAEKKTK
Protein: Acyl-CoA dehydrogenase FadE28 (ACAD) (EC 1.3.99.-) (3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase alpha subunit) (3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase alpha subunit) (P71857)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. May play an important role for the initial macrophage invasion, possibly in response to the acidification of phagosome. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene-20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2'-propanoyl-CoA)-3a-alpha-H-7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), hexahydroindanone and pregenenone.
Interaction partners:
- Acyl-CoA dehydrogenase FadE29
- 3-oxo-4,17-pregnadiene-20-carboxyl-CoA hydratase beta subunit
- 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA lyase
- Steroid 3-ketoacyl-CoA thiolase
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
- 3-oxo-4,17-pregnadiene-20-carboxyl-CoA hydratase alpha subunit
- Probable acyl-CoA dehydrogenase FadE32
- Acyl-CoA dehydrogenase FadE26
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- Acyl-CoA dehydrogenase IpdE1
Sequence:
MDFDPTAEQQAVADVVTSVLERDISWEALVCGGVTALPVPERLGGDGVGLFEVGALLTEVGRHGAVTPALATLGLGVVPLLELASAEQQDRFLAGVAKGGVLTAALNEPGAALPDRPATSFVGGRLSGTKVGVGYAEQADWMLVTADNAVVVVSPTADGVRMVRTPTSNGSDEYVMTMDGVAVADCDILADVAAHRVNQLALAVMGAYADGLVAGALRLTADYVANRKQFGKPLSTFQTVAAQLAEVYIASRTIDLVAKSVIWRLAEDLDAGDDLGVLGYWVTSQAPPAMQICHHLHGGMGMDVTYPMHRYYSTIKDLTRLLGGPSHRLELLGARCSLT
Protein: Eukaryotic translation initiation factor 3 subunit G (K7EL20)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKVRIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFR
Protein: Increased rDNA silencing protein 4 homolog (O14066)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity).
Interaction partners:
- Sorting nexin C1711.11
Sequence:
MDAIHPVSLRNSKRHPLLHSERNLSRRAVSPSISRSFFQHSNGSFPLFQNHRKSLPSAIYKSVDPYVDANPLDPLAAAKASFADFPEQDDSQSSTSPLSSKYHTKKNKQIFVEDSRRGGAASNAAAIAAKKSGYYERTSTRKRSLTVPTPRTSFPHHPRSRRFSLKNAAIATSYHKFKPLSSNSLSSSGMHFSASKQAFNSPLLQTFSPSPSVSPFSNPAVEKLKTSASKQAAEAQSLREFDFFTPTPEPSDKNLEKLKNGASKQASESQSLKNMESLSLARSSPILTSEKLKNGASKQAIESPPFRASEPLPSSNIIPNPAMERLKNGASKLAIESQPFKSAEPLSSAIPLPNPMSEKMRNGASKQAIMAQSSKINPLPPLTASISDPSFEKLKNTASKQAIESQSLMNSGPELLEPSISDPMLEKMKTDAGKQTVESLSLKSSDATIPKPSVSDLGVEKLKNDASKCAVESQSLMINDPSVSSTSFYNPNMEKLKNGAIKQAIEHQALNAAILNKTQLPYFHQSSSELPISASKRAALSQQTESASKSSSNISEMCDSHPPSNFSISASQQASKDRFSEATSSIDLDLSPGRSLSLASSKLSVKEAGARVYNRSVATPVMTPSNPFEISKSASQLASIAQVPVSEPAKTSEVNLKKSLSLASSKLSFQEAGTSLKEKTANVQHSPEVLNDRSLASLSASRHADAISSKSKQHTEIAQPAFNTTGTVLMKTKSNLSDSALSTPQHSDSVLFDITSKAARLASTCAKTDLHRKPRRKHKSFTLENYFGHNAEDESPQSDEVESQTPPSGYSENDIGGTDIYPFALQGAALAAAKDFSRREASLSDSQSAASMDMLPMKKKLSHSSASSTRSIKSLLTNANQKHIHSSINETDDIPTMAAHIVATGQKNKEKAPSFSNDQALDHLLGSAHKRIPSNKTEWSSSSLHIPSHNSFSDIHHRKIAAHAAAITAASEKLTPSIEETSYSSSKAHDASLSAATLVANKDKLIHAPTPQVLAPVLPKVSLPHRHSVSLGQIRGESEVEGDVFYDAPSDKEDLGSSNAPLDVPHGANRSSMDEVNGSKYDYSDGILDGSGQYTDSDMSDDENSLKDSQSSVLSFSAVPTKVLKFKLRDVLGSEYSPSPQLLASSSDVSGSSSAVRAAMKADKIFPAVHENPPPLKTKQSIAKPSPHTLRVPQKKHKHFYHRDDGKYKSGTNLRKSETVDLPQFFIDENRRKLYEGLWAANKGYLLSKSEYSKPNDLICNIVVRELWSRSGAPTSVLAKIYDLVDRHHTGVLGRDEFIVGMFLIDQYLKGRKLPLKVPDSVWLSSKRMGDMLWRLEKLQKKTDNKKPFFKKKKKKRKHLKKFFDFNTTAKVNEGAMTD
Protein: Acetylcholine receptor subunit alpha-type acr-16 (P48180)
Organism: Caenorhabditis elegans
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane (By similarity). A subunit of the levamisole-insensitive nicotinic receptor.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:15944127}; Multi-pass membrane protein {ECO:0000269|PubMed:15944127}. Cell membrane {ECO:0000269|PubMed:15944127}; Multi-pass membrane protein {ECO:0000269|PubMed:15944127}. Note=The cam-1 protein is required for correct localization.
Interaction partners:
- Resistance to inhibitors of cholinesterase protein 3
- Protein unc-50
- Muscarinic acetylcholine receptor gar-3
Sequence:
MSVCTLLISCAILAAPTLGSLQERRLYEDLMRNYNNLERPVANHSEPVTVHLKVALQQIIDVDEKNQVVYVNAWLDYTWNDYNLVWDKAEYGNITDVRFPAGKIWKPDVLLYNSVDTNFDSTYQTNMIVYSTGLVHWVPPGIFKISCKIDIQWFPFDEQKCFFKFGSWTYDGYKLDLQPATGGFDISEYISNGEWALPLTTVERNEKFYDCCPEPYPDVHFYLHMRRRTLYYGFNLIMPCILTTLMTLLGFTLPPDAGEKITLQITVLLSICFFLSIVSEMSPPTSEAVPLLGIFFTCCMIVVTASTVFTVYVLNLHYRTPETHDMGPWTRNLLLYWIPWILRMKRPGHNLTYASLPSLFSTKPNRHSESLIRNIKDNEHSLSRANSFDADCRLNQYIMTQSVSNGLTSLGSIPSTMISSNGTTTDVSQQATLLILHRIYHELKIVTKRMIEGDKEEQACNNWKFAAMVVDRLCLYVFTIFIIVSTIGIFWSAPYLVA
Protein: Rab11 family-interacting protein 2 (Rab11-FIP2) (G3XA57)
Organism: Mus musculus (Mouse)
Function: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. Plays an essential role in phagocytosis through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for controlling actin-dynamics.
Subcellular location: Cell membrane; Peripheral membrane protein. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-11A
- Unconventional myosin-Vb
- Ras-related protein Rab-11B
- EH domain-containing protein 1
- Rab11 family-interacting protein 5
- Rab11 family-interacting protein 1
- Ras-related protein Rab-25
- Rabenosyn-5
- EH domain-containing protein 3
- Rab11 family-interacting protein 3
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSRQIDSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHSFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSMNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRPDKLNNGGSDSPCDLKSPSAFSENRQDYFEYESTNPFTAKFRASTIMPSSSFHVNPTSSEDLRKIPDNNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFTNS
Protein: Ferritin-like catalase Nec2 (EC 1.11.1.6) (Nectar protein 2) (NmNec2) (P0DO51)
Organism: Nesocodon mauritianus (Blue Mauritius bellflower) (Wahlenbergia mauritiana)
Function: Involved in the production of blood-red nectar containing the alkaloid nesocodin and that serves as a visual attractant for pollinator visitation, including vertebrates such as Phelsuma geckos. The nectar is initially acidic and pale yellow, but slowly becomes alkaline before turning into red within 24 hours. Together with NEC1 and NEC3, facilitates the condensation of sinapaldehyde ((E)-3,5-dimethoxy-4-hydroxycinnamaldehyde) and proline to form nesocodin, a pigment with a stable imine bond. Protects nesocodin from degradation by hydrogen peroxide H(2)O(2) by catalyzing the degradation of H(2)O(2) into water H(2)O and dioxygene O(2).
Interaction partners:
Sequence:
MAFLSNMAMFITMLMFSSMMHPCFSQPSCAPMDTMDTNGVDEADIDMMQFPINLEFLEAEFFLWGALGHGLDVVAPQLAMGGPPPYGAQKANLDPLTQNIITEFAYQEVGHLRALERTVGGFPRPLLNLSASNFANLIEAAFGYHLVPPFNPYRDGLSYMLASYAVPYMGLVGYVGTNPNLKGHQTKRLLAGLLGVESGQDAVIRMYLYERQGHVVAPYRHTVAEFTARISELRNRLAMCGVKDEGVIVPRQLGAENQTMSNVLSANYDSISYRRTPGEILRVVYSTGNESVPGGFYPNGGNGRIARRFLV
Protein: Probable quinone reductase Qor (NADPH:quinone reductase) (Zeta-crystallin homolog protein) (O53146)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Possible transcriptional activator protein
Sequence:
MHAIEVTETGGPGVLRHVDQPQPQPGHGELLIKAEAIGVNFIDTYFRSGQYPRELPFVIGSEVCGTVEAVGPGVTAADTAISVGDRVVSASANGAYAEFCTAPASLTAKVPDDVTSEVAASALLKGLTAHYLLKSVYPVKRGDTVLVHAGAGGVGLILTQWATHLGVRVITTVSTAEKAKLSKDAGADVVLDYPEDAWQFAGRVRELTGGTGVQAVYDGVGATTFDASLASLAVRGTLALFGAASGPVPPVDPQRLNAAGSVYLTRPSLFHFTRTGEEFSWRAAELFDAIGSEAITVAVGGRYPLADALRAHQDLEARKTVGSVVLLP
Protein: Thrombin-like enzyme TLBm (SVTLE TLBm) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (P0DJE9)
Organism: Bothrops marajoensis (Marajo lancehead)
Function: Thrombin-like enzyme that induces the formation of fibrin clot. Cleaves the Aalpha-chain of fibrinogen (FGA) with higher activity than the Bbeta-chain (FGB). Induces platelet aggregation in both platelet-rich plasma and in washed platelet preparations. This aggregation is strongly inhibited by preincubation of the enzyme with PMSF.
Subcellular location: Secreted.
Interaction partners:
Sequence:
VIGGDECNINESPFLAFLYSQLLSSRRYFCGMTLINQEWVLTAAHCNLYPDRKDMNWWLLIKLGKHSGSTRRWVANYDEQVRYWPKEKFIWWYCPNKKKDVINNYVWVWWDKDILLWELWMLIRLNRPVKYSEHIAPLSLPSSPPSAKWWHVGSVCRIMGWGQITETWWNSEDTLPDVPRCANINLFNYEVCRAYNQRWWRGLPAKTLCAGDLEGIIRGGWDTCVGDSGGPLICDGQYQGIAYWGSKPCAEPDEPAAYSKVFDHLDWSQSVIAGGTWWRGDDTCP
Protein: GS homeobox 2 (Genetic-screened homeobox 2) (Homeobox protein GSH-2) (P31316)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds 5'-CNAATTAG-3' DNA sequence and regulates the expression of numerous genes including genes important for brain development. During telencephalic development, causes ventralization of pallial progenitors and, depending on the developmental stage, specifies different neuronal fates. At early stages, necessary and sufficient to correctly specify the ventral lateral ganglionic eminence (LGE) and its major derivatives, the striatal projection neurons. At later stages, may specify LGE progenitors toward dorsal LGE fates, including olfactory bulb interneurons.
Subcellular location: Nucleus.
Interaction partners:
- Achaete-scute homolog 1
Sequence:
MSRSFYVDSLIIKDSSRPAPSLPESHPGPDFFIPLGMPSPLVMSVSGPGCPSRKSGAFCVCPLCVTSHLHSSRPPAGAGGGATGTAGAAVAGGGVAGGTGALPLLKSQFSPAPGDAQFCPRVSHAHHHHHPPQHHHHHHQPQQPGSAAAAAAAAAAAAAAAAALGHPQHHAPVCAATTYNMSDPRRFHCLSMGGSDTSQVPNGKRMRTAFTSTQLLELEREFSSNMYLSRLRRIEIATYLNLSEKQVKIWFQNRRVKHKKEGKGASRNNHTSCKCVGSQAHYARSEDEDSLSPASANEDKEISPL
Protein: Protein yippee-like 4 (Q65Z93)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus, nucleolus.
Interaction partners:
Sequence:
MPSCDPGPAPACLPTKTFRSYLPRCHRTYSCVHCRAHLAKHDELISKSFQGSHGRAYLFNSVVNVGCGPAEQRLLLTGLHSVADIFCESCKTTLGWKYEQAFETSQKYKEGKYIIEMSHMVKDNGWD
Protein: Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH 1) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (PL-insensitive glyceraldehyde-3-phosphate dehydrogenase) (P54226)
Organism: Streptomyces arenae
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTVRIGINGFGRIGRNVFRAAAARSSELEIVAVNDLGDVPTMAHLLAYDSILGRFPEEVTAEPGAIRVGDRTIKVLAERDPGALPWGDLGVDIVIESTGIFTDAAKARSHVDGGAKKVIIAAPASGEDFTVVLGVNDGDYDPERHTIISNASCTTNCLGVLAKVLHDAVGIDSGMMTTVHAYTQDQNLQDAPHKDLRRARAAALNIVPTSSGAAKAIGLVLPELAGRLDAFALRVPVPTGSVTDLTVTTRRGTSVEEVKEAYAAAASGPYKGLLSYVDAPLVSTDIVGDPASLFDAGLTRVCGPQVKVVGWYDNEWGYSNRLIDLATLIGSSL
Protein: Monothiol glutaredoxin-S7 (AtGrxS7) (Protein ROXY 14) (Q6NLU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 1-aminocyclopropane-1-carboxylate oxidase homolog 1
- Monothiol glutaredoxin-S17
Sequence:
MEKLQKMTSEKSLVIFSKNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEQALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLIPMLKRVGALWL
Protein: Transcription factor PAR1 (Basic helix-loop-helix protein 165) (AtbHLH165) (bHLH 165) (Protein HELIX-LOOP-HELIX 1) (Protein PHYTOCHROME RAPIDLY REGULATED 1) (bHLH transcription factor bHLH165) (Q9SJH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical bHLH transcription factor that acts as negative regulator of a variety of shade avoidance syndrome (SAS) responses, including seedling elongation and photosynthetic pigment accumulation. Acts as direct transcriptional repressor of two auxin-responsive genes, SAUR15 and SAUR68. May function in integrating shade and hormone transcriptional networks in response to light and auxin changes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17948056, ECO:0000269|PubMed:21205034}.
Interaction partners:
- Transcription factor PRE1
- Transcription factor PIF4
- Transcription factor HFR1
- Transcription factor PIL1
- Transcription factor BEE 2
- Homeobox-leucine zipper protein HAT4
- Homeobox-leucine zipper protein ATHB-4
- Transcription factor PIF5
- Homeobox-leucine zipper protein HAT3
- Transcription factor BEE 1
Sequence:
MEETLATPDATRRSLSPSCSATVKSRAAGFERRTKRRLSETNASVREDREEAEEEEDEVKEKIEALQRIIPGGAALGVDALFEETAGYILSLQCQIKTIKVLTSFLQRIDQEDMKFGG