wanglab/gogpt-training-data huggingface dataset:
Protein: Arabinogalactan endo-beta-1,4-galactanase A (EC 3.2.1.89) (Endo-1,4-beta-galactanase A) (Galactanase A) (Q8X168)
Organism: Aspergillus niger
Function: Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.
Subcellular location: Secreted {ECO:0000269|PubMed:12383257}.
Interaction partners:
Sequence:
MIYPLLLSALPLLSSAALTYRGADISSLLIEEDAGISYKNLNGETQALEDILVNNGVNSIRQRVWVDPSDGSYDLDYNLKLAKRVQAAGMSIYLDLHLSDTWADPSDQTTPTGWSTTDIDTLTWQLYNYTLDVCNTFAENDIDIEIVSIGNEISSGLLWPLGKTSNYDNIAKLLHSGAWGVKDSNQATTPKIMIHLDNGWDWEEQEYFYKTVLATGSLLSTDFDLMGVSYYPFYNSEATLSALQTSLTNMQSNYDKSVVVVETNWPVSCPDPEYSFPSDLSSIPFSAAGQEEFLEKLAEVVEGVTDGLGIYYWEPAWVDNAALGSSCADNLMVDIDTDEVLESVTVFEDL
Protein: Phosphoadenosine 5'-phosphosulfate reductase (PAPS reductase) (EC 1.8.4.8) (3'-phosphoadenylylsulfate reductase) (PAPS reductase, thioredoxin dependent) (PAPS sulfotransferase) (PAdoPS reductase) (P17854)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305}.
Interaction partners:
- Sulfite reductase hemoprotein beta-component
- Adenylyl-sulfate kinase
- Sulfite reductase flavoprotein alpha-component
- Sulfate adenylyltransferase subunit 1
- Sulfate/thiosulfate import ATP-binding protein CysA
- Siroheme synthase
- Sulfate adenylyltransferase subunit 2
- 3'
- Sulfate transport system permease protein CysW
- Cysteine synthase A
Sequence:
MSKLDLNALNELPKVDRILALAETNAELEKLDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEETRFFGLKRECGLHEG
Protein: Envelope biogenesis factor ElyC (Elevated frequency of lysis) (P0AB01)
Organism: Escherichia coli (strain K12)
Function: Plays a critical role in the metabolism of the essential lipid carrier used for cell wall synthesis.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YgjQ
Sequence:
MLFTLKKVIGNMLLPLPLMLLIIGAGLALLWFSRFQKTGKIFISIGWLALLLLSLQPVADRLLRPIESTYPTWNNSQKVDYIVVLGGGYTWNPQWAPSSNLINNSLPRLNEGIRLWRENPGSKLIFTGGVAKTNTVSTAEVGARVAQSLGVPREQIITLDLPKDTEEEAAAVKQAIGDAPFLLVTSASHLPRAMIFFQQEGLNPLPAPANQLAIDSPLNPWERAIPSPVWLMHSDRVGYETLGRIWQWLKGSSGEPRQE
Protein: M-phase phosphoprotein 10 (U3KQ48)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MAPQVWRRRTLERCLTEVGKATGRPECFLTIQEGLASKFTSLTKVLYDFNKILENGRIHGSPLQKLVIENFDDEQIWQQLELQNEPILQYFQNAVSETINDEDISLLPESEEQEREEDGSEIEADDKEDLEDLEEEEVSDMGNDDPEMGERAENSSKSDLRKSPVFSDEDSDLDFDISKLEQQSKVQNKGQGKPREKSIVDDKFFKLSEMEAYLENIEKEEERKDDNDEEEEDIDFFEDIDSDEDEGGLFGSKKLKSGKSSRNLKYKDFFDPVESDEDITNVHDDELDSNKEDDEIAEEEAEELSISETDEDDDLQENEDNKQHKESLKRVTFALPDDAETEDTGVLNVKKNSDEVKSSFEKRQEKMNEKIASLEKELLEKKPWQLQGEVTAQKRPENSLLEETLHFDHAVRMGMVPSSVVFMSVLFPWFHFIQRFGVVFLFPQLFILKTCKHMAWHGSSHL
Protein: Protein P4 (Protein IV) (Q37958)
Organism: Pseudoalteromonas phage PM2 (Bacteriophage PM2)
Function: May interact with the viral DNA.
Subcellular location: Virion membrane {ECO:0000305|PubMed:12134022, ECO:0000305|PubMed:7408847}; Single-pass membrane protein {ECO:0000305|PubMed:12134022, ECO:0000305|PubMed:7408847}. Note=Part of the capsid inner membrane. Located partially in the inner leaflet of the bilayer. {ECO:0000305}.
Interaction partners:
Sequence:
MQKPSGKGLKYFAYGVAISAAGAILAEYVRDWMRKPKAKS
Protein: Serine:pyruvate aminotransferase (Q24510)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
QIMDEVKEGIKYIFQTLNDATMCISGAGHSGMEAALCNLIEDGDVVLMGITGVWGHRAGDMARRYGAEVHYVEASFGRALSHEEITFAFEGHRPKVFFIAQGDSSTGIIQQNIRELGELCRKYDCFLIVDTVASLGGTEFLMDEWKVDVAYTGSQKSLGGPAGLTPISFSKRA
Protein: Insecticidal protein LA-b (EC 3.2.1.132) (EC 3.2.1.14) (Latex abundant protein b) (P86800)
Organism: Morus alba (White mulberry)
Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:20109180}.
Interaction partners:
Sequence:
SEQQXGRDVGGAL
Protein: Carbohydrate ABC transporter substrate-binding protein (Carbohydrate substrate-binding protein SP0092) (Carbohydrate SBP SP0092) (A0A0H2UMY0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Probably part of an ABC transporter complex involved in carbohydrate transport.
Subcellular location: Cell surface {ECO:0000305|PubMed:28994793}.
Interaction partners:
Sequence:
MKNWKKYAFASASVVALAAGLAACGNLTGNSKKAADSGDKPVIKMYQIGDKPDNLDELLANANKIIEEKVGAKLDIQYLGWGDYGKKMSVITSSGENYDIAFADNYIVNAQKGAYADLTELYKKEGKDLYKALDPAYIKGNTVNGKIYAVPVAANVASSQNFAFNGTLLAKYGIDISGVTSYETLEPVLKQIKEKAPDVVPFAIGKVFIPSDNFDYPVANGLPFVIDLEGDTTKVVNRYEVPRFKEHLKTLHKFYEAGYIPKDVATSDTSFDLQQDTWFVREETVGPADYGNSLLSRVANKDIQIKPITNFIKKNQTTQVANFVISNNSKNKEKSMEILNLLNTNPELLNGLVYGPEGKNWEKIEGKENRVRVLDGYKGNTHMGGWNTGNNWILYINENVTDQQIENSKKELAEAKESPALGFIFNTDNVKSEISAIANTMQQFDTAINTGTVDPDKAIPELMEKLKSEGAYEKVLNEMQKQYDEFLKNKK
Protein: Protein PA-X (Q67020)
Organism: Influenza A virus (A/WSN/1933(H1N1))
Interaction partners:
Sequence:
MEDFVRQCFNPMIVELAEKAMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFNWKDFQLNQENCFLSFRLLGTTWNLGPLILGGYMKQLRSA
Protein: Cyclic di-AMP synthase CdaA (c-di-AMP synthase) (EC 2.7.7.85) (Diadenylate cyclase) (DAC) (Q45589)
Organism: Bacillus subtilis (strain 168)
Function: One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000269|PubMed:26240071}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01499}.
Interaction partners:
- CdaA regulatory protein CdaR
- Phosphoglucosamine mutase
- Cyclic-di-AMP phosphodiesterase PgpH
- Cyclic-di-AMP phosphodiesterase GdpP
- Potassium transporter KimA
- Cyclic di-AMP receptor A
Sequence:
MAFEDIPFLQYLGNAVDILLVWYVIYKLIMVIRGTKAVQLLKGIVVIVLVRMASQYLGLSTLQWLMDQAITWGFLAIIIIFQPELRRALEQLGRGRFFSRSGTPVEEAQQKTIEAITKAINYMAKRRIGALLTIERDTGMGDYIETGIPLNAKVSSELLINIFIPNTPLHDGAVIMKNNEIAAAACYLPLSESPFISKELGTRHRAAVGISEVTDSLTIIVSEETGGVSVAKNGDLHRELTEEALKEMLEAEFKKNTRDTSSNRWYWRGKKNG
Protein: Cytochrome b6-f complex subunit 4 (17 kDa polypeptide) (P0C319)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01344}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01344}.
Interaction partners:
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Cytochrome b6
- Cytochrome b6-f complex subunit 5
- Cytochrome f
- Cytochrome b
- Cytochrome c oxidase subunit 3
- Cytochrome b
- NAD
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 1
Sequence:
MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF
Protein: Nuclear pore complex protein (A1YK61)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
Sequence:
MADSPFPRSSRSGLLRTTLNSSMAPQNLSHSLLILEKSNAEQNERSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQEAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARQRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTLGGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAPVREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRRDIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNGRMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRLAHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYGSVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVKEQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLNWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADEISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
Protein: Inositol oxygenase 1 (EC 1.13.99.1) (Myo-inositol oxygenase 1) (AtMIOX1) (MI oxygenase 1) (Q8L799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable glucuronokinase 2
- Glucuronokinase 1
- Inositol-phosphate phosphatase
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Bifunctional phosphatase IMPL2, chloroplastic
- Phosphatase IMPL1, chloroplastic
- Inositol 3-kinase
- Aldo-keto reductase family 4 member C10
- UDP-glucose 6-dehydrogenase 1
Sequence:
MTILIDRHSDQNDAGDEIVEKNQGNGKEEETELVLDAGFEAPHTNSFGRTFRDYDAESERRRGVEEFYRVNHIGQTVDFVRKMREEYEKLNRTEMSIWECCELLNEFIDESDPDLDEPQIEHLLQTAEAIRKDYPDEDWLHLTGLIHDLGKVLLHSSFGELPQWAVVGDTFPVGCAFDESIVHHKYFKENPDYDNPSYNSKYGIYTEGCGLDNVLMSWGHDDYMYLVAKENQTTLPSAGLFIIRYHSFYALHKSEAYKHLMNNEDRENMKWLKVFNKYDLYSKSKVRVNVEEVKPYYLSLTNKYFPSKLKW
Protein: Ferrichrome outer membrane transporter/phage receptor (Ferric hydroxamate receptor) (Ferric hydroxamate uptake) (Ferrichrome-iron receptor) (P06971)
Organism: Escherichia coli (strain K12)
Function: Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:2066336, ECO:0000269|PubMed:8916906, ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}; Multi-pass membrane protein {ECO:0000269|PubMed:9856937, ECO:0000269|PubMed:9865695}.
Interaction partners:
- Protein TonB
- Biopolymer transport protein ExbD
- Biopolymer transport protein ExbB
- Iron
- Iron
- Iron
- Ferric siderophore reductase
- Ferric enterobactin-binding periplasmic protein FepB
- Maltoporin
- Outer membrane protein A
Sequence:
MARSKTAQPKHSLRKIAVVVATAVSGMSVYAQAAVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF
Protein: Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase) (P12995)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. Complements a bioU deletion in Synechocystis PCC 6803.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- ATP-dependent dethiobiotin synthetase BioD 1
- 8-amino-7-oxononanoate synthase
- Biotin synthase
- ATP-dependent dethiobiotin synthetase BioD 2
- Malonyl-[acyl-carrier protein] O-methyltransferase
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- Bifunctional ligase/repressor BirA
Sequence:
MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQRLTAAVNRAVQDETFFCQ
Protein: Homeobox protein vex1 (Homeodomain transcription factor vex-1) (Ventral homeobox protein) (Xvex-1) (Q9W769)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Acts in a ventral signaling pathway downstream of bmp4 to antagonize the Spemann organizer and ventrally pattern the embryonic mesoderm. Represses transcription of the dorsal genes gsc and otx2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEKRPYSVEWLSESSQRKAVYSNADLLGYKSGNPDKESNISLPSRATGPTLPSVDYREKENYCVRNVQNEERSPPVKDQLHSQPAPQELDTSRRALMVVPACERSTDQGNKVTGTTDTNKKAKPVCDEDAAARARTKFSPEQLEELERSFKENRYIGSSEKRRLSKVLKLSETQIKTWFQNRRMKFKRQTQDARVDAFFSGLYVPYYGYPDLPTPGYSVQPEFSVLAPHTMAAPSLPFGPLQSTVISPGLHPTAIPSANLGSYPYSSMLVHPMLNEPKRQRYSPY
Protein: Ataxin-7 (Spinocerebellar ataxia type 7 protein) (O15265)
Organism: Homo sapiens (Human)
Function: Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation. Necessary for microtubule cytoskeleton stabilization.
Subcellular location: [Isoform a]: Nucleus {ECO:0000269|PubMed:12533095, ECO:0000269|PubMed:16314424, ECO:0000269|PubMed:22100762}. Nucleus, nucleolus {ECO:0000269|PubMed:10441328}. Nucleus matrix {ECO:0000269|PubMed:10441328}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22100762}. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus (PubMed:10441328). It is able to shuttle between the nucleus and cytoplasm (PubMed:16314424). {ECO:0000269|PubMed:10441328, ECO:0000269|PubMed:16314424}.; SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm {ECO:0000269|PubMed:12533095}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Ubiquitin carboxyl-terminal hydrolase 22
- Transcription initiation factor TFIID subunit 9
- Transformation/transcription domain-associated protein
- Transcription and mRNA export factor ENY2
- Ataxin-7-like protein 3
- Transcription factor SPT20 homolog
- Transcription initiation protein SPT3 homolog
- Transcriptional adapter 1
Sequence:
MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEKKPEDNSNNRKFLNKRLSEREFDPDIHCGVIDLDTKKPCTRSLTCKTHSLTQRRAVQGRRKRFDVLLAEHKNKTREKELIRHPDSQQPPQPLRDPHPAPPRTSQEPHQNPHGVIPSESKPFVASKPKPHTPSLPRPPGCPAQQGGSAPIDPPPVHESPHPPLPATEPASRLSSEEGEGDDKEESVEKLDCHYSGHHPQPASFCTFGSRQIGRGYYVFDSRWNRLRCALNLMVEKHLNAQLWKKIPPVPSTTSPISTRIPHRTNSVPTSQCGVSYLAAATVSTSPVLLSSTCISPNSKSVPAHGTTLNAQPAASGAMDPVCSMQSRQVSSSSSSPSTPSGLSSVPSSPMSRKPQKLKSSKSLRPKESSGNSTNCQNASSSTSGGSGKKRKNSSPLLVHSSSSSSSSSSSSHSMESFRKNCVAHSGPPYPSTVTSSHSIGLNCVTNKANAVNVRHDQSGRGPPTGSPAESIKRMSVMVNSSDSTLSLGPFIHQSNELPVNSHGSFSHSHTPLDKLIGKKRKCSPSSSSINNSSSKPTKVAKVPAVNNVHMKHTGTIPGAQGLMNSSLLHQPKARP
Protein: Transcription initiation factor TFIID subunit 9 (TAFII-17) (TAFII20) (TBP-associated factor 17 kDa) (TBP-associated factor 9) (Q05027)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complex SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3, and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- Transcription initiation factor TFIID subunit 11
- SAGA complex subunit ADA2
- SAGA complex subunit SPT7
- SAGA complex subunit NGG1
- SAGA complex subunit SPT20
- Transcription initiation factor TFIID subunit 13
- Histone acetyltransferase GCN5
- SAGA complex subunit SPT3
- Ubiquitin carboxyl-terminal hydrolase 8
Sequence:
MNGGGKNVLNKNSVGSVSEVGPDSTQEETPRDVRLLHLLLASQSIHQYEDQVPLQLMDFAHRYTQGVLKDALVYNDYAGSGNSAGSGLGVEDIRLAIAARTQYQFKPTAPKELMLQLAAERNKKALPQVMGTWGVRLPPEKYCLTAKEWDLEDPKSM
Protein: Microtubule-associated protein 6 (MAP-6) (Stable tubule-only polypeptide) (STOP) (Q7TSJ2)
Organism: Mus musculus (Mouse)
Function: Involved in microtubule stabilization in many cell types, including neuronal cells. Specifically has microtubule cold stabilizing activity. Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated axonal cargo transport (By similarity). Regulates axonal growth during neuron polarization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9600916}. Golgi apparatus {ECO:0000269|PubMed:16837464}. Cell projection, axon {ECO:0000250|UniProtKB:Q63560}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63560}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q63560}; Lipid-anchor {ECO:0000250|UniProtKB:Q63560}; Cytoplasmic side {ECO:0000250|UniProtKB:Q63560}. Note=Isoform 1 and isoform 2 associate with axonal microtubules in neurons (PubMed:16837464). Isoform 3 associates with microtubules in fibroblasts (PubMed:9600916). Localizes predominantly in the proximal part of the axon (By similarity). Preferentially is concentrated on a portion of the microtubule polymer in which tubulin is modified by detyrosination and acetylation and is also resistant to depolymerization induced by both nocodazole and cold (By similarity). In unpolarized neurons, localizes to the Golgi and to secretory vesicles accumulating transiently at the tips of a subset of neurites (By similarity). Following neuronal polarization and during axon outgrowth, accumulates in the axonal growth cone and subsequently localizes throughout the axon. Partially localizes to dendrites in mature neurons (By similarity). {ECO:0000250|UniProtKB:Q63560, ECO:0000269|PubMed:16837464, ECO:0000269|PubMed:9600916}.
Interaction partners:
- Transmembrane protein 106B
Sequence:
MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPAPLQPALAPPSRAVAIETQPAQGESDAVARATGPAPGPSVDRETVAAPGRSGLGLGAASASTSGSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQIPATSQPSQPVLGVPKRRPQSQERGPMQLSADARDPEGAGGAGVLAAGKASGVDQRDTRRKAGPAWMVTRNEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRSEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEETPLPPAQSQTQEGGPAAGKASGADERDTRRKAGPAWMVRRSEGHEQTPAAHAQGTGPEGGKGRAVADALNRQIREEVASTVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEANKPSAADNKAMDRRRIRSLYSEPFKECPKVEKPSVQSSKPKKTSTSHKPPRKAKDKQVVSGQAAKKKTTEGPSATKPDDKEQSKEMNNKLAEAKESRVKPTSDASKNRGPVTKEPHKDQGSVAPGLPKGQEPLKDQGPVVPGLPKDQVPVVPGSLKGQSPTAPGPTKDQGAVLLGPVKDLGPVAPAPIKVQDHIASELLKNKDSVPLAPAKAQSPLLPEPLKNQSPVVPASTKDQSFPTPAPRKDPGPVIPEPEKDRAPTVPERRKDQHVSIMASLKNEAPMVPESVKNQGLAGPELVKDTGTDTTAPRYLKGHDSVFVAPVKNQGPVIPEPVKSQDPIIPALAKDQGPMLPEPPKNQSPVVLGPIKNQDPIIPVPLKGQDPLVPAPTKDQGPTAPDPLKTQGPKGTQLPTVSPSPPVMIPTVPHTEYIEGSP
Protein: DUF21 domain-containing protein At4g33700 (CBS domain-containing protein CBSDUF6) (Q8VZI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAVEYVCCSPNFFIHIAVIVFLVLFAGLMSGLTLGLMSLSLVDLEVLAKSGTPEHRKYAAKILPVVKNQHLLLVTLLICNAAAMETLPIFLDGLVTAWGAILISVTLILLFGEIIPQSICSRYGLAIGATVAPFVRVLVFICLPVAWPISKLLDFLLGHRRAALFRRAELKTLVDFHGNEAGKGGELTHDETTIIAGALELSEKMVKDAMTPISDIFVIDINAKLDRDLMNLILEKGHSRVPVYYEQPTNIIGLVLVKNLLTINPDEEIPVKNVTIRRIPRVPEILPLYDILNEFQKGLSHMAVVVRQCDKIHPLPSKNGSVKEARVDVDSEGTPTPQERMLRTKRSLQKWKSFPNRASSFKGGSKSKKWSKDNDADILQLNGNPLPKLAEEEEAVGIITMEDVIEELLQEEIFDETDHHFEDS
Protein: Rho-related GTP-binding protein RhoE (Protein MemB) (Rho family GTPase 3) (Rho-related GTP-binding protein Rho8) (Rnd3) (P61587)
Organism: Homo sapiens (Human)
Function: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.
Subcellular location: Golgi apparatus membrane; Peripheral membrane protein.
Interaction partners:
- Rho-associated protein kinase 1
- Rho GTPase-activating protein 35
- UBX domain-containing protein 11
- Pleckstrin homology domain-containing family G member 5
- Plexin-B1
- Rho GTPase-activating protein 5
- Plexin-B2
- Rho-associated protein kinase 2
- Cofilin-2
- Cofilin-1
Sequence:
MKERRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM