wanglab/gogpt-training-data huggingface dataset:
Protein: Sorting nexin-5 (Q9Y5X3)
Organism: Homo sapiens (Human)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin (Probable). Plays a role in the internalization of EGFR after EGF stimulation (Probable). Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C isoform 3 and is retromer-independent. Together with PIP5K1C isoform 3 facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation (Probable). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation. Plays a role in macropinocytosis.
Subcellular location: Endosome {ECO:0000269|PubMed:11485546}. Early endosome {ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:24610942}. Early endosome membrane {ECO:0000269|PubMed:15561769}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000269|PubMed:15561769}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:18854019}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (PubMed:15561769). Detected on macropinosomes (PubMed:16968745, PubMed:21048941). Targeted to membrane ruffles in response to EGFR stimulation. {ECO:0000269|PubMed:15561769, ECO:0000269|PubMed:16968745, ECO:0000269|PubMed:21048941}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-6
- Vacuolar protein sorting-associated protein 26A
- Stromal cell-derived factor 2-like protein 1
- Sorting nexin-32
- TBC1 domain family member 5
- Sorting nexin-3
Sequence:
MAAVPELLQQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN
Protein: Scarecrow-like protein 18 (AtSCL18) (GRAS family protein 7) (AtGRAS-7) (Protein LATERAL SUPPRESSOR) (Q9ZWC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor required for axillary (lateral) shoot meristem formation during vegetative development. Seems to act upstream of REVOLUTA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein PAT1 homolog
- Phosphorylase superfamily protein
- At4g24340
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
Sequence:
MLTSFKSSSSSSEDATATTTENPPPLCIASSSAATSASHHLRRLLFTAANFVSQSNFTAAQNLLSILSLNSSPHGDSTERLVHLFTKALSVRINRQQQDQTAETVATWTTNEMTMSNSTVFTSSVCKEQFLFRTKNNNSDFESCYYLWLNQLTPFIRFGHLTANQAILDATETNDNGALHILDLDISQGLQWPPLMQALAERSSNPSSPPPSLRITGCGRDVTGLNRTGDRLTRFADSLGLQFQFHTLVIVEEDLAGLLLQIRLLALSAVQGETIAVNCVHFLHKIFNDDGDMIGHFLSAIKSLNSRIVTMAEREANHGDHSFLNRFSEAVDHYMAIFDSLEATLPPNSRERLTLEQRWFGKEILDVVAAEETERKQRHRRFEIWEEMMKRFGFVNVPIGSFALSQAKLLLRLHYPSEGYNLQFLNNSLFLGWQNRPLFSVSSWK
Protein: Nicotinamide riboside kinase 1 (NRK 1) (NmR-K 1) (EC 2.7.1.22) (Nicotinic acid riboside kinase 1) (EC 2.7.1.173) (Ribosylnicotinamide kinase 1) (RNK 1) (Ribosylnicotinic acid kinase 1) (Q9NWW6)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). The enzyme also phosphorylates the antitumor drugs tiazofurin and 3-deazaguanosine.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide phosphoribosyltransferase
- Purine nucleoside phosphorylase
- NAD-capped RNA hydrolase NUDT12
- Nicotinamide riboside kinase 2
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MKTFIIGISGVTNSGKTTLAKNLQKHLPNCSVISQDDFFKPESEIETDKNGFLQYDVLEALNMEKMMSAISCWMESARHSVVSTDQESAEEIPILIIEGFLLFNYKPLDTIWNRSYFLTIPYEECKRRRSTRVYQPPDSPGYFDGHVWPMYLKYRQEMQDITWEVVYLDGTKSEEDLFLQVYEDLIQELAKQKCLQVTA
Protein: Homeobox protein Nkx-6.2 (Homeobox protein NK-6 homolog B) (Q9C056)
Organism: Homo sapiens (Human)
Function: Transcription factor with repressor activity involved in the regulation of axon-glial interactions at myelin paranodes in oligodendrocytes. Binds to the consensus DNA sequence 5'-(A/T)TTAATGA-3'. In oligodendrocytes, binds to MBP and PLP1 promoter regions.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:D3Z4R4}.
Interaction partners:
- Neurogenin-3
- Insulin gene enhancer protein ISL-1
- Solute carrier family 2, facilitated glucose transporter member 2
- Hepatocyte nuclear factor 3-beta
- Neurogenic differentiation factor 1
- Oligodendrocyte transcription factor 2
- DNA-binding protein RFX6
- Transducin-like enhancer protein 3
- Pancreas transcription factor 1 subunit alpha
- Slit homolog 1 protein
Sequence:
MDTNRPGAFVLSSAPLAALHNMAEMKTSLFPYALQGPAGFKAPALGGLGAQLPLGTPHGISDILGRPVGAAGGGLLGGLPRLNGLASSAGVYFGPAAAVARGYPKPLAELPGRPPIFWPGVVQGAPWRDPRLAGPAPAGGVLDKDGKKKHSRPTFSGQQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKRHAVEMASAKKKQDSDAEKLKVGGSDAEDDDEYNRPLDPNSDDEKITRLLKKHKPSNLALVSPCGGGAGDAL
Protein: Cathepsin B (EC 3.4.22.1) (Q6PH75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cathepsin D
- Cathepsin Bb
- NACHT domain-containing protein.
- Napsin A aspartic peptidase
- Carboxypeptidase
- Apoptosis regulator Bcl-2
- Legumain.
- Lysosomal-associated membrane protein 1b
- Caspase a
- Bcl-2-like protein 1
Sequence:
MWRLAFLCVISALSVSWARPRLPPLSHEMVNFINKANTTWTAGHNFRDVDYSYVKKLCGTFLKGPKLPVMVQYTEGLKLPKNFDAREQWPNCPTLKEIRDQGSCGSCWAFGAAEAISDRVCIHSDAKVSVEISSQDLLTCCDSCGMGCNGGYPSAAWDFWATEGLVTGGLYNSHIGCRPYTIEPCEHHVNGSRPPCSGEGGDTPNCDMKCEPGYSPSYKQDKHFGKTSYSVPSNQNSIMAELFKNGPVEGAFTVYEDFLLYKSGVYQHMSGSPVGGHAIKILGWGEENGVPYWLAANSWNTDWGDNGYFKILRGEDHCGIESEIVAGIPM
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (P0AGE9)
Organism: Escherichia coli (strain K12)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed.
Interaction partners:
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Succinate--CoA ligase subunit beta
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Fumarate reductase iron-sulfur subunit
- Fumarate reductase flavoprotein subunit
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MSILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK
Protein: Nucleoporin nsp1 (Nuclear pore protein nsp1) (Nucleoskeletal-like protein) (Q10168)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Appears to have a role in the formation of the septum.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15116432}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000250|UniProtKB:P14907}.
Interaction partners:
- Nucleoporin nup146
- Nucleoporin nup44
- Nucleoporin nup186
- Nucleoporin nup45
- Probable nucleoporin C890.06
- Nucleoporin nup107
- Meiotically up-regulated gene 87 protein
- Nucleoporin nup189
- Nucleoporin nup85
- Nucleoporin seh1
Sequence:
MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNSTNASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTNTTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSNTTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFTKPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPSAKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRIDDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISEIVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF
Protein: Homeobox protein OTX1 (Orthodenticle homolog 1) (P32242)
Organism: Homo sapiens (Human)
Function: Probably plays a role in the development of the brain and the sense organs. Can bind to the BCD target sequence (BTS): 5'-TCTAATCCC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box protein Pax-2
Sequence:
MMSYLKQPPYGMNGLGLAGPAMDLLHPSVGYPATPRKQRRERTTFTRSQLDVLEALFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQSGSGTKSRPAKKKSSPVRESSGSESSGQFTPPAVSSSASSSSSASSSSANPAAAAAAGLGGNPVAAASSLSTPAASSIWSPASISPGSAPASVSVPEPLAAPSNTSCMQRSVAAGAATAAASYPMSYGQGGSYGQGYPTPSSSYFGGVDCSSYLAPMHSHHHPHQLSPMAPSSMAGHHHHHPHAHHPLSQSSGHHHHHHHHHHQGYGGSGLAFNSADCLDYKEPGAAAASSAWKLNFNSPDCLDYKDQASWRFQVL
Protein: KH homology domain-containing protein 1A (Nur77 downstream gene 1 protein) (Q3UWR2)
Organism: Mus musculus (Mouse)
Function: Has pro-apoptotic activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14657025}.
Interaction partners:
- KH homology domain-containing protein 1C
Sequence:
MSDLRRKGWWNVPDYFHSPLVFDMEEDKEDYIFGPHDEYLHTLEVHSNTLIQLERWFTPTGQTRVTVVGPLKARLWVMDMIRKVGSKNNLDQIKGKMMLLQIRDHPLRDRDLELHPESGSSLWITTMNDTTFVEVPHFLRFPLTVAWLFCGFVRILGIHNFADLHW
Protein: SPI-1 type 3 secretion system secretin (T3SS-1 secretin) (Protein InvG) (P35672)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000269|PubMed:27974800, ECO:0000269|PubMed:9786184}. Note=Localization to the outer membrane requires InvH/SctG. {ECO:0000269|PubMed:9786184}.
Interaction partners:
- SPI-1 type 3 secretion system needle filament protein
- Lipoprotein PrgK
- Invasion protein InvA
- Surface presentation of antigens protein SpaP
- SPI-1 type 3 secretion system ATPase
- Protein PrgH
- Surface presentation of antigens protein SpaQ
- Surface presentation of antigens protein SpaN
- Surface presentation of antigens protein SpaS
- Surface presentation of antigens protein SpaR
Sequence:
MKTHILLARVLACAALVLVTPGYSSEKIPVTGSGFVAKDDSLRTFFDAMALQLKEPVIVSKMAARKKITGNFEFHDPNALLEKLSLQLGLIWYFDGQAIYIYDASEMRNAVVSLRNVSLNEFNNFLKRSGLYNKNYPLRGDNRKGTFYVSGPPVYVDMVVNAATMMDKQNDGIELGRQKIGVMRLNNTFVGDRTYNLRDQKMVIPGIATAIERLLQGEEQPLGNIVSSEPPAMPAFSANGEKGKAANYAGGMSLQEALKQNAAAGNIKIVAYPDTNSLLVKGTAEQVHFIEMLVKALDVAKRHVELSLWIVDLNKSDLERLGTSWSGSITIGDKLGVSLNQSSISTLDGSRFIAAVNALEEKKQATVVSRPVLLTQENVPAIFDNNRTFYTKLIGERNVALEHVTYGTMIRVLPRFSADGQIEMSLDIEDGNDKTPQSDTTTSVDALPEVGRTLISTIARVPHGKSLLVGGYTRDANTDTVQSIPFLGKLPLIGSLFRYSSKNKSNVVRVFMIEPKEIVDPLTPDASESVNNILKQSGAWSGDDKLQKWVRVYLDRGQEAIK
Protein: Sulfotransferase 1B1 (ST1B1) (EC 2.8.2.1) (DOPA/tyrosine sulfotransferase) (Sulfotransferase family cytosolic 1B member 1) (Q9QWG7)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
Interaction partners:
Sequence:
MSASEDVWRKDLKMIHGYPMIYAFALNWERIEEFQSTPGDIVITTYPKSGTTWLSEIVDMVLNDGNVEKCKRDVITSKVPMLELSVPGIRISGVELLKKTPSPRIIKTHLPIDLLPKSFWENKCKMIYLARNGKDVAVSYYHFDLMNSINPLPGTWEEYLEKFLAGNVAYGSWFDHVKSWWEKREEHPLLYLYYEELKQNPKKEIKKIASFLDKTLDEEALDRIVHHTSFEMMKENPLVNYTHLPTAMMDHSKSPFMRKGIVGDWKNYFTMTQTEQFDAVYKKKMSGTTLEFCTDIQSA
Protein: Guanine nucleotide-binding protein alpha-9 subunit (G alpha-9) (Q54R41)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G alpha-9 antagonizes broad chemotactic response. It functions rapidly following receptor stimulation to negatively regulate PI3K/PTEN, adenylyl cyclase, and guanylyl cyclase pathways.
Interaction partners:
- Latrophilin receptor-like protein A
- Guanine nucleotide-binding protein subunit beta
- Metabotropic glutamate receptor-like protein E
Sequence:
MGCNSSSEAKQSDKIDRTLYDEKKSQEREIKLLLLGSGDSGKSTIAKQMRYIHTKGFSNEEIATFVEIMHSNVLSSIQILIRNVPVEQLGSDLKDKANYYSSINPYELPLTPDIGLEIDRLWKNEAIQKLFSTNRAELNLPEVTAYCLDQVERISSETYTPTQEDVLRCRQRTTGMKETQFNVEDIKFRLIDVGGQKNERRKWMHYFEDVKSIIFCVALGDYDMNLVEDETINRMEDSLKLWNDIVNNPFFKNTSFVLFLNKNDIFREKIKKIPLVDYFPDYQGGYNYEKGIEYIRNKFFSSVPTATTIVAHVTTATDTENITIVFDAVRRNIIQSILKLHY
Protein: Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase) (Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein) (O60185)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:16823372}.
Interaction partners:
- S-methyl-5'-thioadenosine phosphorylase
- Methylthioribulose-1-phosphate dehydratase
- Enolase-phosphatase E1
- Adenine phosphoribosyltransferase
- Pdp3-interacting factor 1
- Putative purine nucleoside phosphorylase
- Methylthioribulose-1-phosphate dehydratase-like protein
- Acireductone dioxygenase-requiring))
- Uncharacterized protein C57A7.07c
Sequence:
MSLQAIIYNEDKLLVLDQLLLPYERKYISVSNVEDAFAVIKKMQVRGAPAIAIVAALSVAVGLKHLSEDADAKEYVINSFEHLKQSRPTAVNLFETAKFMQGIALQEGKNCRNKIIQEAERMLVKDLEDNHNIGTAGRKFLLQHYKDKDKLTVLTHCNTGSLATSGYGTALGIIRSLHESGNLEHAYCTETRPYNQGSRLTAFELVHDKIPATLVTDSTVASIMHKIDAIVVGADRVTRNGDTANKIGTYNLAILAKHFGKPFIVAAPFSSIDTSLASGSQITIEQRPPIEMTTITGPIITDSNSRNLEDPKRVRISIAAPGIDVYSPAFDVTPANLITAIATEKGFYTQQTNNKYDFS
Protein: Corin, serine peptidase (E7EQE7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVSRICFSPQQENGKQLLCGRGENFLCASGICIPGKLQCNGYNDCDDWSDEAHCNCSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNCDCNPTTEHRCGDGRCIAMEWVCDGDHDCVDKSDEVNCSCHSQGLVECRNGQCIPSTFQCDGDEDCKDGSDEENCSVIQTSCQEGDQRCLYNPCLDSCGGSSLCDPNNSLNNCSQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALCEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDEYVEECSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENCGCKERDLWECPSNKQCLKHTVICDGFPDCPDYMDEKNCSFCQDDELECANHACVSRDLWCDGEADCSDSSDEWDCVTLSINVNSSSFLMVHRAATEHHVCADGWQEILSQLACKQMGLGEPSVTKLIQEQEKEPRWLTLHSNWESLNGTTLHELLVNGQSCESRSKISLLCTKQDCGRRPAARMNKRILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRENAAVWKVVLGINNLDHPSVFMQTRFVKTIILHPRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGNKMPFKLQEGEVRIISLEHCQSYFDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEKPGGRWTLFGLTSWGSVCFSKVLGPGVYSNVSYFVEWIKRQIYIQTFLLN
Protein: Zinc finger protein WIP6 (Protein DEFECTIVELY ORGANIZED TRIBUTARIES 5) (WIP-domain protein 6) (AtWIP6) (Q9FX68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcriptional regulator (Probable). Involved in leaf vasculature patterning.
Subcellular location: Nucleus {ECO:0000269|PubMed:20541552}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- At1g60280
- C2H2-like zinc finger protein
- C2H2-like zinc finger protein
- Zinc finger
- Protein C2-DOMAIN ABA-RELATED 1
- NAC domain protein
- At4g35700
- AT5G18310 protein
- LOB domain-containing protein 10
Sequence:
MYNNNQYSFSGDEDSVVLSLGPPGQQYPSHNKPTSTKPSSDHEFNHPLTNPNGVTVALHIGPPSSDKETLSGGNNQEGLTARQGQYWIPSLSQILVGPTQFSCSVCNKTFNRFNNMQMHMWGHGSQYRKGPESLRGTKSSSSILRLPCYCCAEGCKNNIDHPRSKPLKDFRTLQTHYKRKHGAKPFRCRKKCEKTFAVRGDWRTHEKNCGKLWFCVCGSDFKHKRSLKDHVRAFGDGHAAHTVSDRVVGIGDADEDDEEEEEEEEDDVEEEDAHEENVRGEKNYGIRYDHFRRYGQISDDNY
Protein: Probable protein phosphatase 2C 79 (AtPP2C79) (EC 3.1.3.16) (Q9FKX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May dephosphorylate and repress plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness.
Interaction partners:
- Ribosomal L18p/L5e family protein
- Probable inactive leucine-rich repeat receptor-like protein kinase At3g03770
- Probable protein phosphatase 2C 5
- E3 ubiquitin-protein ligase APD4
- E3 ubiquitin-protein ligase APD3
- E3 ubiquitin-protein ligase APD2
- 16 kDa phloem protein 1
- E3 ubiquitin-protein ligase APD1
- Protein SMALL AUXIN UP-REGULATED RNA 9
- Auxin-responsive protein SAUR19
Sequence:
MLSLFFNFLTSCLWPSSSTTSHTYSDSKGKQDGLLWYKDSAHHLFGDFSMAVVQANNLLEDQSQVESGPLTTLSSSGPYGTFVGVYDGHGGPETSRFVNDHLFHHLKRFAAEQDSMSVDVIRKAYEATEEGFLGVVAKQWAVKPHIAAVGSCCLIGVVCDGKLYVANVGDSRAVLGKVIKATGEVNALQLSAEHNVSIESVRQEMHSLHPDDSHIVVLKHNVWRVKGIIQVSRSIGDVYLKKSEFNKEPLYTKYRLREPMKRPILSWEPSITVHDLQPDDQFLIFASDGLWEQLSNQEAVEIVQNHPRNGIARRLVKAALQEAAKKREMRYSDLNKIERGVRRHFHDDITVVVLFLDTNLLSRASSLKTPSVSIRGGGITLPKKL
Protein: Probable beta-1,3-galactosyltransferase 12 (EC 2.4.1.-) (Q66GS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Probable glucuronoxylan glucuronosyltransferase F8H
- Probable beta-1,4-xylosyltransferase IRX14H
- Probable beta-1,4-xylosyltransferase IRX9H
- Xyloglucan 6-xylosyltransferase 2
- Xyloglucan 6-xylosyltransferase 1
Sequence:
MPLFSHRFTTASSSSPASPSYYNKPSSKTHKPNSSSSSYTSSRIHVAIIFFSLVSVFIGVAGTIFALSSTGPASVYRCGGSKDTSRVVSASRKLGGDGGNNGVVVERRKLLGFVGIQTGFDSGDRRTALRSTWFPSDPDSLLRLEQATGLAFRFVIGKSKDAKKMAELEKEIKEYRDFVLLDTEEEYIRLPYKTLAFFKAAFKLFEADYYVKADDDIYLRPDRLATLLANERLHSQTYIGCMKKGPVITDPKLKWYEKQGNLIGNEYFLHAYGPIYVLSAEIVASLAAARNGSLRMFNNEDVTIGSWMLAMDVHHEDNRALCDPHCSPKSIAVWDIPKCSGLCDPESRLKELHKTDMCSKSPTLPPDDIDQ
Protein: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC 2.3.1.168) (52 kDa mitochondrial autoantigen of primary biliary cirrhosis) (Branched chain 2-oxo-acid dehydrogenase complex component E2) (BCOADC-E2) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (BCKAD-E2) (BCKADE2) (BCKDH-E2) (Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide branched chain transacylase) (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase) (P11182)
Organism: Homo sapiens (Human)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P11181}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPILVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVSQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK