wanglab/gogpt-training-data huggingface dataset:
Protein: NADPH-ferredoxin reductase FprA (NFR) (EC 1.18.1.2) (P9WIQ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transports electrons between ferredoxin and NADPH. May supply electrons to P450 systems. The enzyme can use both NADPH and NADH as a reductant, but the catalytic efficiency is two orders of magnitude higher with NADPH.
Interaction partners:
- Glutamate synthase large chain
- Possible oxygenase
- Probable ferredoxin/ferredoxin--NADP reductase
- Ferredoxin
- Sulfite reductase [ferredoxin]
- Adenosine 5'-phosphosulfate reductase
- Possible electron transfer protein FdxB
- Probable O-acetylhomoserine sulfhydrylase MetC
- Peptide chain release factor 2
- Possible conserved transmembrane protein
Sequence:
MRPYYIAIVGSGPSAFFAAASLLKAADTTEDLDMAVDMLEMLPTPWGLVRSGVAPDHPKIKSISKQFEKTAEDPRFRFFGNVVVGEHVQPGELSERYDAVIYAVGAQSDRMLNIPGEDLPGSIAAVDFVGWYNAHPHFEQVSPDLSGARAVVIGNGNVALDVARILLTDPDVLARTDIADHALESLRPRGIQEVVIVGRRGPLQAAFTTLELRELADLDGVDVVIDPAELDGITDEDAAAVGKVCKQNIKVLRGYADREPRPGHRRMVFRFLTSPIEIKGKRKVERIVLGRNELVSDGSGRVAAKDTGEREELPAQLVVRSVGYRGVPTPGLPFDDQSGTIPNVGGRINGSPNEYVVGWIKRGPTGVIGTNKKDAQDTVDTLIKNLGNAKEGAECKSFPEDHADQVADWLAARQPKLVTSAHWQVIDAFERAAGEPHGRPRVKLASLAELLRIGLG
Protein: Inner membrane transport protein YdiN (P76198)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Quinate/shikimate dehydrogenase
- 3-dehydroquinate dehydratase
- Uncharacterized protein YdiL
Sequence:
MSQNKAFSTPFILAVLCIYFSYFLHGISVITLAQNMSSLAEKFSTDNAGIAYLISGIGLGRLISILFFGVISDKFGRRAVILMAVIMYLLFFFGIPACPNLTLAYGLAVCVGIANSALDTGGYPALMECFPKASGSAVILVKAMVSFGQMFYPMLVSYMLLNNIWYGYGLIIPGILFVLITLMLLKSKFPSQLVDASVTNELPQMNSKPLVWLEGVSSVLFGVAAFSTFYVIVVWMPKYAMAFAGMSEAEALKTISYYSMGSLVCVFIFAALLKKMVRPIWANVFNSALATITAAIIYLYPSPLVCNAGAFVIGFSAAGGILQLGVSVMSEFFPKSKAKVTSIYMMMGGLANFVIPLITGYLSNIGLQYIIVLDFTFALLALITAIIVFIRYYRVFIIPENDVRFGERKFCTRLNTIKHRG
Protein: Pentatricopeptide repeat-containing protein At2g29760, chloroplastic (Protein ORGANELLE TRANSCRIPT PROCESSING 81) (O82380)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rps12 transcript.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19934379}.
Interaction partners:
- Phosphoglycerate mutase family protein
- Multiple organellar RNA editing factor 2, chloroplastic
- Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial
- Protein HEAT-INDUCED TAS1 TARGET 3
- Multiple organellar RNA editing factor 1, mitochondrial
- Protein HEAT-INDUCED TAS1 TARGET 4
- Protein HEAT-INDUCED TAS1 TARGET 5
Sequence:
MAIFSTAQPLSLPRHPNFSNPNQPTTNNERSRHISLIERCVSLRQLKQTHGHMIRTGTFSDPYSASKLFAMAALSSFASLEYARKVFDEIPKPNSFAWNTLIRAYASGPDPVLSIWAFLDMVSESQCYPNKYTFPFLIKAAAEVSSLSLGQSLHGMAVKSAVGSDVFVANSLIHCYFSCGDLDSACKVFTTIKEKDVVSWNSMINGFVQKGSPDKALELFKKMESEDVKASHVTMVGVLSACAKIRNLEFGRQVCSYIEENRVNVNLTLANAMLDMYTKCGSIEDAKRLFDAMEEKDNVTWTTMLDGYAISEDYEAAREVLNSMPQKDIVAWNALISAYEQNGKPNEALIVFHELQLQKNMKLNQITLVSTLSACAQVGALELGRWIHSYIKKHGIRMNFHVTSALIHMYSKCGDLEKSREVFNSVEKRDVFVWSAMIGGLAMHGCGNEAVDMFYKMQEANVKPNGVTFTNVFCACSHTGLVDEAESLFHQMESNYGIVPEEKHYACIVDVLGRSGYLEKAVKFIEAMPIPPSTSVWGALLGACKIHANLNLAEMACTRLLELEPRNDGAHVLLSNIYAKLGKWENVSELRKHMRVTGLKKEPGCSSIEIDGMIHEFLSGDNAHPMSEKVYGKLHEVMEKLKSNGYEPEISQVLQIIEEEEMKEQSLNLHSEKLAICYGLISTEAPKVIRVIKNLRVCGDCHSVAKLISQLYDREIIVRDRYRFHHFRNGQCSCNDFW
Protein: Stage II sporulation protein Q (P71044)
Organism: Bacillus subtilis (strain 168)
Function: Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
Subcellular location: Forespore membrane {ECO:0000269|PubMed:15044948, ECO:0000269|PubMed:15574594, ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18077456, ECO:0000269|PubMed:18812514, ECO:0000269|PubMed:9140963}; Single-pass membrane protein {ECO:0000269|PubMed:15044948, ECO:0000269|PubMed:15574594, ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18077456, ECO:0000269|PubMed:18812514, ECO:0000269|PubMed:9140963}. Note=Localizes to the engulfing septal membranes.
Interaction partners:
- Stage III sporulation protein AH
- Stage II sporulation protein D
- Stage II sporulation protein P
- Stage III sporulation protein AA
- Stage IV sporulation protein FA
- Stage III sporulation protein AG
- Stage II sporulation protein E
- Spore coat protein E
- Stage II sporulation protein M
- Stage VI sporulation protein D
Sequence:
MREEEKKTSQVKKLQQFFRKRWVFPAIYLVSAAVILTAVLWYQSVSNDEVKDQLADNGGNSAYDNNDDAVEVGKSMENVAMPVVDSENVSVVKKFYETDAAKEEKEAALVTYNNTYSLSKGIDLAEKDGKDFDVSASLSGTVVKAEKDPVLGYVVEVEHADGLSTVYQSLSEVSVEQGDKVKQNQVIGKSGKNLYSEDSGNHVHFEIRKDGVAMNPLNFMDKPVSSIEKAATQETEESIQQSSEKKDGSTEKGTEEKSGEKKDDSTDKSGSKESSTTEDTEQS
Protein: (R)-3-hydroxyacyl-acyl carrier protein: coenzyme A transacylase (B5M4W4)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Interaction partners:
Sequence:
MSPEIPVLDIQGQYRVYTEFYRAEAAENTIILINGSLATTASFAQTVRNLHPQFNVVLFGQPYAGKSKPHNRQERLISKETEAHILLELIEHFQADHVMSFSWGGASTLLALAHQPRYVKKAVVSSFSPVINEPMRDYLDRGCQYLAACDRYQVGNLVNDTIGKHLPSLFKRFNYRHVSSLDSHEYAQMHFHINEVLQHDLERALDGARNINIPVLFINGDRDEYTTVEDARQFGKHVGRSQFSVIRDAGHFLDMETKAACEDTRNVMLGFLKPTVRETRQRYQPVQQGQHAFAI
Protein: adenylate cyclase (EC 4.6.1.1) (E1JIB3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLIHVILLFSVVKNIDFLTVLPYFAVMLLTPSILMPSREPNVEQYESIAILVSCLMALLLTAMDLILPICYFRPFSLVPSYDHVVIVLIYLMFPIAFVKNGRAYFLGLAVSLFYFGYMALIDKISTLDKVWELTAYGAYLFFLNMLCMFLSRFQEYNMRSGILSRYQVVYQNLVFQMAMKEEKALLDSIIPVTLARSLQDAIASHIEEDPSNLMPFTKTRHLFMEPHPEVSILEADMVDFTGLTTTMEVSDLVAILHELFVSFDLAANHNRATRIKFLGDSYTCVTGIPSYFPTHANACVNQALDMIEISREVSKRRNKKIDLRIGVHSGEILAGIIGLTKWQFDIWSKDVDITNRLESSGLPGMVHISSRTLGLLDNHYVYEEGTDTAKLDPLLQRSNLSTYLIRSRLPNFEDTDDLEDDNFSLNDYRFSFSFSQDYEDIQVKAQRDMILEVEHMPVNRVQTCKIRRPMHRIAKEDINEEYRFHLESYYLFTTFRSWRMEWSFNKMRDLLMKYSLGMMVFAGATIIAMDLLVKSEAMDYTMLFSLFLLILLPLLLASYKKLWLRGRRLSPITQPTFFLSRWFIKASDLIEKSVFVRIPLAIMVLFLLYVMSSETVFSCDIARLELEIINSELHNLRPQMLCFMPWGVTYAVVIVLSLMLVIIGIPLIIKLGVGLAILGSHVITVHAYYGFAFERSQTTNIGVTSSLAHSWYMVAFFIVVVVREGYLNYILKASYFMSMCFEKKHELTKVKTRTIKIIMANILPTHVAEVFKVRRRSDQLYYENFSQVAVMFATIENYEADKSGLRALHEMICYFDELLVNYQSWYKIEKIKVMGWTYLAACGLHVDHYTDFSVSVPISTNRESDKLQKSGSVRFAPMDGDEIMIKDLHPTQATTNEDDNTILVMTEFALNLLRILRDIRSKGIFFEKDSKLTGSLKIGIAHGPVMAGVVGLSKPHYDIWGHTVNMASRMTSTGVRDGIHVTESTANVLRDFNIRCTYRGMTFVKGVGQVPTYLVDLDENLHFQQHSPDNDSHKGSIVSVHWLDEKRAER
Protein: Ribonucleoside-diphosphate reductase large subunit (R1) (EC 1.17.4.1) (Ribonucleotide reductase large subunit) (P89462)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Ribonucleoside-diphosphate reductase holoenzyme that provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability. Prevents host necroptosis by targeting host RIPK1 and RIPK3, thereby hampering the formation of necroptotic RIPK1-RIPK3 complexes. May form hetero-amyloid structures with host proteins RIPK3 or ZBP1, thereby preventing RIPK3- and ZBP1-mediated necroptosis (By similarity). In addition, inhibits extrinsic apoptosis by targeting host CASP8.
Subcellular location: Host cell membrane {ECO:0000269|PubMed:7618272}. Host endosome membrane {ECO:0000269|PubMed:7618272}. Note=Associates with the host cytoskeleton. {ECO:0000305}.
Interaction partners:
Sequence:
MANRPAASALAGARSPSERQEPREPEVAPPGGDHVFCRKVSGVMVLSSDPPGPAAYRISDSSFVQCGSNCSMIIDGDVARGHLRDLEGATSTGAFVAISNVAAGGDGRTAVVALGGTSGPSATTSVGTQTSGEFLHGNPRTPEPQGPQAVPPPPPPPFPWGHECCARRDARGGAEKDVGAAESWSDGPSSDSETEDSDSSDEDTGSETLSRSSSIWAAGATDDDDSDSDSRSDDSVQPDVVVRRRWSDGPAPVAFPKPRRPGDSPGNPGLGAGTGPGSATDPRASADSDSAAHAAAPQADVAPVLDSQPTVGTDPGYPVPLELTPENAEAVARFLGDAVDREPALMLEYFCRCAREESKRVPPRTFGSAPRLTEDDFGLLNYALAEMRRLCLDLPPVPPNAYTPYHLREYATRLVNGFKPLVRRSARLYRILGVLVHLRIRTREASFEEWMRSKEVDLDFGLTERLREHEAQLMILAQALNPYDCLIHSTPNTLVERGLQSALKYEEFYLKRFGGHYMESVFQMYTRIAGFLACRATRGMRHIALGRQGSWWEMFKFFFHRLYDHQIVPSTPAMLNLGTRNYYTSSCYLVNPQATTNQATLRAITGNVSAILARNGGIGLCMQAFNDASPGTASIMPALKVLDSLVAAHNKQSTRPTGACVYLEPWHSDVRAVLRMKGVLAGEEAQRCDNIFSALWMPDLFFKRLIRHLDGEKNVTWSLFDRDTSMSLADFHGEEFEKLYEHLEAMGFGETIPIQDLAYAIVRSAATTGSPFIMFKDAVNRHYIYDTQGAAIAGSNLCTEIVHPASKRSSGVCNLGSVNLARCVSRQTFDFGRLRDAVQACVLMVNIMIDSTLQPTPQCTRGNDNLRSMGIGMQGLHTACLKMGLDLESAEFRDLNTHIAEVMLLAAMKTSNALCVRGARPFSHFKRSMYRAGRFHWERFSNASPRYEGEWEMLRQSMMKHGLRNSQFIALMPTAASAQISDVSEGFAPLFTNLFSKVTRDGETLRPNTLLLKELERTFGGKRLLDAMDGLEAKQWSVAQALPCLDPAHPLRRFKTAFDYDQELLIDLCADRAPYVDHSQSMTLYVTEKADGTLPASTLVRLLVHAYKRGLKTGMYYCKVRKATNSGVFAGDDNIVCTSCAL
Protein: Zinc finger and BTB domain-containing protein 34 (Q8NCN2)
Organism: Homo sapiens (Human)
Function: May be a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:16718364}.
Interaction partners:
Sequence:
MDSSSFIQFDVPEYSSTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYFRDHSALSTMSGLSISVIKNPNVFEQLLSFCYTGRMSLQLKDVVSFLTAASFLQMQCVIDKCTQILESIHSKISVGDVDSVTVGAEENPESRNGVKDSSFFANPVEISPPYCSQGRQPTASSDLRMETTPSKALRSRLQEEGHSDRGSSGSVSEYEIQIEGDHEQGDLLVRESQITEVKVKMEKSDRPSCSDSSSLGDDGYHTEMVDGEQVVAVNVGSYGSVLQHAYSYSQAASQPTNVSEAFGSLSNSSPSRSMLSCFRGGRARQKRALSVHLHSDLQGLVQGSDSEAMMNNPGYESSPRERSARGHWYPYNERLICIYCGKSFNQKGSLDRHMRLHMGITPFVCKFCGKKYTRKDQLEYHIRGHTDDKPFRCEICGKCFPFQGTLNQHLRKNHPGVAEVRSRIESPERTDVYVEQKLENDASASEMGLDSRMEIHTVSDAPD
Protein: Proline-rich protein 23E (Q8N813)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTGASEKQAEQKVRRAFEASEEAHGTLAASTPWVAMGSAYGSCTCLGAQPVTDLALWPVIYSCMGFSPQAYPAFWAYPWVLYGGYLWMGYPPPAALVPSVWLYWRGASSFDPLIGSPYLAALAPNLFPFPMKFPPTYSLASPTLGGATSSHCPQVGCWTPASSAPRAAVEGPSRGAPYLKTCKAPPSEWASRFGIWAPLPCCSSELRPLPPSPIEDSQLDPGCSRSSSRSPCRARRRLFEC
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na(+)/H(+) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1) (P70441)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling (By similarity). May participate in HTR4 targeting to microvilli. Involved in the regulation of phosphate reabsorption in the renal proximal tubules (By similarity). Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa.
Subcellular location: Cytoplasm. Apical cell membrane. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast. Present in lipid rafts of T-cells (By similarity). Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent manner. Colocalizes with CFTR at the midpiece of sperm tail. {ECO:0000250}.
Interaction partners:
- Ezrin
- Moesin
- Radixin
- Cystic fibrosis transmembrane conductance regulator
- Sodium-dependent phosphate transport protein 2A
- Beta-2 adrenergic receptor
- Sodium/hydrogen exchanger 3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Chloride anion exchanger
Sequence:
MSADAAAGEPLPRLCCLEKGPNGYGFHLHGEKGKVGQFIRLVEPGSPAEKSGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDERLKKLGVSIREELLRPQEKSEQAEPPAAADTHEAGDQNEAEKSHLRELRPRLCTMKKGPNGYGFNLHSDKSKPGQFIRAVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIKGGGDEAKLLVVDKETDEFFKKCKVIPSQEHLDGPLPEPFSNGEIQKESSREALVEPASESPRPALARSASSDTSEELNSQDSPKRQVSTEPSSTSSSSSDPILDLNISLAVAKERAHQKRSSKRAPQMDWSKKNELFSNL
Protein: Probable T-complex protein 1 subunit theta (TCP-1-theta) (CCT-theta) (P78921)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- Probable T-complex protein 1 subunit eta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit delta
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- Phosducin-like protein C2A9.09
- Heat shock protein 60, mitochondrial
- Probable prefoldin subunit 3
Sequence:
MALRVPKASGPQLFREGYRIMQGVEDAVIRNCNAIRELSEITRTSLGPNGKNKIVVNHLQQTFLTNDAATIIRELEVIHPAAKLVVDATQQQENELGDAANFVVVFTGELLAKAENMIRMGLTPLEIAKGYEMALSHTMEVLEEICADKIETVESEKELIKAIRTCISSKQYGNEDFLSDLVAKAILTVLPKDPSKFNVDNIRVVKIMGSSLYNSQVVKGMVFPREPEGTVTRSKEAKVAVFSCPLDISQTETKGTVLLHNAQEMLDFSKGEENLIESHIKEIYDAGVRVVVTSGNVNDLVLHYLNRFEILVIRVPSKFELRRLCRVVGATPLARMGVPMPEEMGSVDVVETIEIGGDRVTVFRQVEDITRTATIVLRGATKTYLDDLERAIDDGVNIVKALVKDNRLIFGAGASDMQLCIRLISVGEKTPGIYQHAIKQYGEAFEVVPRTISENAGLDPTDVISKLYAAHHKENGESIGVDVECENDGTLDAKEAGIFDVLLAKKSAIRLATETVLTVLNVDQVVMSKPAGGPKPPGPNPHWDDD
Protein: Alpha-fetoprotein (Alpha-1-fetoprotein) (Alpha-fetoglobulin) (P02773)
Organism: Rattus norvegicus (Rat)
Function: Binds estrogens, fatty acids and metals.
Subcellular location: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
Interaction partners:
- Prothrombin
- Glypican-3
- Keratin, type I cytoskeletal 19
- Apolipoprotein A-II
- Alpha-1-antiproteinase
- Plasminogen
- Transthyretin
- Albumin
- Alpha-2-HS-glycoprotein
- Tyrosine aminotransferase
Sequence:
MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAENGDKPEGLTLNPSEFLGDRNFAQFSSEEKLLFMASFLHEYSRNHPNLPVSVILKTAKSYQEILEKCSQSETPSKCQDNMEEELQKHIQESQALAKQSCNLYQKLGPYYLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKRSACGEGLADIYIGHLCLRHEANPVNSGINHCCSSSYSNRRLCITSFLRDETYVPPPFSEDKFIFHKDLCQAQGRALQTMKQELLINLVKQKPEMTEEQHAAVTADFSGLLEKCCKDQDQEACFAKEGPKLISKTREALGV
Protein: AP-1 complex subunit mu-1 (Q8IEK4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- AP-1 complex subunit gamma, putative
- AP-4 complex subunit epsilon, putative
- AP complex subunit sigma
- AP complex subunit beta
- Clathrin adaptor domain-containing protein, putative
- AP-2 complex subunit alpha, putative
- AP-3 complex subunit delta, putative
- AP complex subunit beta
- Aquaglyceroporin
- AP complex subunit sigma
Sequence:
MACISAIFIIDLKGKVIINRNYRGEVNVNLTEVFYNCVIDQEDNLIKPIFHVNGLTYCWVAHNNIYFLAVTRKNSNATLIIAFLYKLIQVLKDYFKVLEEESIKDNFVITYELLDEMIDNGFPQLSEVKILREYIKNKAHQLTVNNFKIPSALTNSVSWRSEGIKYKKNEIFLDVVESLNIIISSNGTVLRSEILGCLKMKSYLSGMPELKLGLNDKLLFNKNLNNYPNSSNNNLNNKTKLVELEDIKFHQCVRLSKFENDRTISFIPPDGIFNLMTYRLSTHVKPLFWLDINITKKSLTKIEYNVKAKSQFKNKSIANNVEFHLPVPADVDSPHFQTYIGTVKYYPDKDILIWKIKQFQGQKEYIMNAQFGLPSIVSNENKDLYYKRPVNVKFEIPYFTVSGITVRYLKIIEKSGYQALPWVRYITQNGDYQVRMS
Protein: Variant surface glycoprotein (VSG)-related, putative (Q57XY3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MRAINLCTVLLALVFPATVSGDRRIVNGDEFKTLCGMINLAEAALGKMKEAQEITKGAARIGAMYLEMSGDRDLNKTCEGAGKRNCALHKVFWNESKKELATRGNTTLLSVGGLSEREVVEIRKKVLSVAQIFQNITKNRRWVLKASDLEKGINRALYGVPYRPQEIKARSSDRRQVCEQQLSRSQKLKASVSLSRDLLCLCAPRMNLGRETQLCCSRCARGDNRAVWRPDEDAGERWYFLKEQCSSMEGPQEGFNKLVNDFRDMINHGVDGCTGTTYVFGDRRKFSFWRLWILPQEAPGHRVRYVVRGRNRDIKNIPWMRELLKVFNEMRDLKDYENDKRTLADAIEKLQKEFEESNRKIGNAKN
Protein: 18 kDa learning-associated protein of slug (Q9GNQ1)
Organism: Lehmannia marginata (Tree slug) (Limax marginatus)
Function: May be involved in modulating long-term memory formation and retention, at least with respect to odor-taste associative learning.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11168596}. Secreted {ECO:0000269|PubMed:11168596}. Note=Secreted to the cell surface, and to the terminals of neurites. {ECO:0000269|PubMed:11168596}.
Interaction partners:
Sequence:
MAKGLRCKHRIRMRNIKRQHYAKKDLERLKKIVSKSSELKDVVTMKTTEPIQENKTSEGTSTDGSMEVDKMAKVINKKTLQDENGHYPEWMNQRAVKKQKQKLNKLKIKKKSGKVSKAIKW
Protein: Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5) (Q9ULC5)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17681178, ECO:0000269|PubMed:33191500}. Endoplasmic reticulum {ECO:0000269|PubMed:17681178, ECO:0000269|PubMed:24269233, ECO:0000269|PubMed:33191500}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:24269233}.
Interaction partners:
- Carnitine O-palmitoyltransferase 1, liver isoform
- Fatty acid synthase
- Beta-alanine-activating enzyme
- Lipoprotein lipase
- Monoglyceride lipase
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Palmitoyl thioesterase CPT1C
Sequence:
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVSQKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGSCLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADIAMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLGKEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDVAISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYDKVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGAAPMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVADMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKLGVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLKAKRGELSKYFRTQIDSLYEHIQD
Protein: Uncharacterized protein (Q385P7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TFIIH basal transcription factor subunit
- TFIIH basal transcription factor subunit
- Dynein light chain
Sequence:
MAELREGLHPQTQECSGTKSETDADENFEAMRHAALSMFKQRTKDLTMVSALTAEADQVEQLNTQVQSTIQKLQEQKASLEAQIEAEERRVKQWEAQLREVHGMLAQMKEDQTMFAGTQRSSEKIVLTLQHFVSQYTEKGGDVSRLLDRAQEATGGRTPNEWRGAANDLRRRGVVLREHIEQIEKQQIVPQALMDLIIEWTKGGWKTSPDYSPALCVCEQLVFYDPEQDVRELVASRLRWDAAKSRTINASTEGAETLVDDAIRELDELLEAVAAVERECEDAGLCCTSTLKDSLNGVKEQWLNVPQSRQLLIDGVRLTEVWKKQLEEHVLVSNLVSERVGTLSSHIDEAESNFQHEKKNSESSREMCNNLQLSWTKALNLVLMHERNIAIREVAIWTVEAESQKLQTKLESILALTDARWGAIQAQVIQLCAAVAAGKQEAAAAQLLLEGTAKDCKSVSENLSELQDTCTKFEAELRHECEMIPGRLPICFTTEPPQSEEETSQTEEEEENLIPETTTRQDVLDELLKFPVGSDVGFTASALGTGLTSTGLEVELLRCVAQCVIAMKKQGLDVEEKYRAWKCRMDEELAAANAD
Protein: Ras-related protein Rab-26 (EC 3.6.5.2) (P51156)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach (By similarity). Plays a role in the secretion of amylase from acinar granules in the parotid gland.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:10857477, ECO:0000269|PubMed:16076461}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ULW5}; Lipid-anchor {ECO:0000250|UniProtKB:Q9ULW5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9ULW5}. Note=Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location (By similarity). Localized immediately around secretory granules in the acinar cells of the parotid gland (PubMed:10857477). Not localized in plasma membranes (PubMed:10857477). {ECO:0000250, ECO:0000269|PubMed:10857477}.
Interaction partners:
- Autophagy-related protein 16-1
Sequence:
MSRKKTPKSKGGSVPAASTLPAAANGPRLAHPRTARPGPEAPPNGPPQSGRPSLGGTGDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGMKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDITNKDSFDNIQAWLTEIQEYAQQDVVLMLLGNKVDSTQERVVKREDGEKLAKEYGLPFMETSAKSGLNVDLAFTAIAKELKQRSTKAPSEPRFRLHDYVKREGRGVSCCRL
Protein: UDP-glycosyltransferase 708C2 (EC 2.4.1.360) (C-glucosyltransferase b) (FeCGTb) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase) (A0A0A1H7N4)
Organism: Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum)
Function: UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols.
Interaction partners:
Sequence:
MMGDLTTSFPATTLTTNEQPHVVVCSGAGMGHLIPFLNLASTLSSAPYRCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSTLAPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPDHIFTSFTISNANYLSLSKGIIVNTFDSFEPETLSALNSGDSLPDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYVKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWSSGIQVAIVEKVKMIMGNNDLRNSAVRVGEEAKRACDVGGSSATALMNIIGSLKR
Protein: Kinesin-like protein (Q504B9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTDAAAECNIKVLCRFRPLNQAEILRGDKFLPTFQGDDTVIIGGKSYAFDRVFPTNTTQEQVYNTCAKQIVKDVLGGYNGTIFAYGQTSSGKTHTMEGNLHDPQQMGIIPRIAEDIFNHIFSMDENLEFHIKVSYFEIYMEKIRDLLDVTKTNLSVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQEHVETEQKLCGKLYLVDLAGSEKVSKTGAAGAVLDEAKNINKSLSALGNVISALAEGTKSHVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASINLELTAEQWKRKKKKK