wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor bHLH77 (Basic helix-loop-helix protein 77) (AtbHLH77) (bHLH 77) (Protein ACTIVATOR FOR CELL ELONGATION 3) (Transcription factor EN 87) (bHLH transcription factor bHLH077) (Q9LK48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor GTE2
- Probable disease resistance protein At5g43740
- Emb|CAB72159.1
Sequence:
MNMDKETEQTLNYLPLGQSDPFGNGNEGTIGDFLGRYCNNPQEISPLTLQSFSLNSQISENFPISGGIRFPPYPGQFGSDREFGSQPTTQESNKSSLLDPDSVSDRVHTTKSNSRKRKSIPSGNGKESPASSSLTASNSKVSGENGGSKGGKRSKQDVAGSSKNGVEKCDSKGDNKDDAKPPEAPKDYIHVRARRGQATDSHSLAERARREKISERMTLLQDLVPGCNRITGKAVMLDEIINYVQSLQRQVEFLSMKLATVNPRMEFNANASLSTEMIQPGESLTQSLYAMACSEQRLPSAYYSLGKNMPRFSDTQFPSNDGFVHTETPGFWENNDLQSIVQMGFGDILQQQSNNNNNNCSEPTLQMKLEP
Protein: STAM-binding protein (EC 3.4.19.-) (Associated molecule with the SH3 domain of STAM) (Q9CQ26)
Organism: Mus musculus (Mouse)
Function: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains. Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization. Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95630}. Membrane {ECO:0000250|UniProtKB:O95630}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95630}. Cytoplasm {ECO:0000250|UniProtKB:O95630}. Early endosome {ECO:0000250|UniProtKB:O95630}.
Interaction partners:
- Signal transducing adapter molecule 1
- Signal transducing adapter molecule 2
- Charged multivesicular body protein 3
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Growth factor receptor-bound protein 2
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 1B1
- Ubiquitin-like protein FUBI
- Ubiquitin carboxyl-terminal hydrolase 8
Sequence:
MSDHGDVSLPPQDRVRILSQLGSAVELNEDIPPRRYYRSGVEIIRMASVYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAIIPEKKDAVKKLKSVAFPKAEELKTELLRRYTKEYEQYKERKKKEEEELARNIAIQQELEKEKQRVAQQKQKQLEQEQFHAFEEMIQRQELEKERLKIVQEFGKVDPGPCGPLLPDLEKPCVDVAPSSPFSPTQTPDCNTGMRPAKPPVVDRSLKPGALSVIENVPTIEGLRHIVVPRNLCSEFLQLASANTAKGIETCGVLCGKLMRNEFTITHVLIPRQNGGPDYCHTENEEEIFFMQDDLGLLTLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESIAIVCSPKFQETGFFKLTDYGLQEISTCRQKGFHPHGRDPPLFCDCSHVTVKDRIVTITDLR
Protein: Arginosuccinase (Q59R31)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Protein ARG5,6
- Argininosuccinate synthase
- Arginine biosynthesis bifunctional protein ArgJ
- ornithine carbamoyltransferase
- Histidine biosynthesis trifunctional protein
- Adenylosuccinate lyase
- Arginase
- Carbamoyl phosphate synthase arginine-specific large chain
- Orotidine 5'-phosphate decarboxylase
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MSQQQDKQPSENKLWGGRFTGATDPLMDLYNASLPYDKVMYDADLTGTKVYTQGLNKLGLITTEELHLIHQGLEQIRQEWHDNKFIIKAGDEDIHTANERRLGEIIGKNISGKVHTGRSRNDQVATDMRIFVRESLLNLSKILHQFITAILERAHKEIDVLMPGYTHLQKAQPIRWAHWLSSYATYFTEDYKRLQEIITRVNQSPLGSGALAGHPYGIDREFLAKGLGFDGVIGNSLTAVSDRDFVVESLFWSTLFMNHISRFSEDLIIYSSGEFGFIKLADAYSTGSSLMPQKKNPDSLELLRGKSGRVFGQLSGFLMSIKSIPSTYNKDMQEDKEPLFDALTTVEHSILIATGVISTLSIDKQNMEKALTMDMLATDLADYLVRKGVPFRETHHISGECVRKAEEEKLSGIDQLSFEQFQQIDSRFEKDVMETFDFEASVERRDAIGGTAKSAVLKQLENLKSILS
Protein: Arylsulfatase A (ASA) (EC 3.1.6.8) (Cerebroside-sulfatase) (P50428)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes cerebroside sulfate.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P15289}. Lysosome {ECO:0000250|UniProtKB:P15289}.
Interaction partners:
- Galactocerebrosidase
- Arylsulfatase B
- Alpha-galactosidase A
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Sialidase-3
- Sialidase-2
- Sialidase-1
- Sialidase-4
- Arylsulfatase G
- Formylglycine-generating enzyme
Sequence:
MALGTLFLALAAGLSTASPPNILLIFADDLGYGDLGSYGHPSSTTPNLDQLAEGGLRFTDFYVPVSLCTPSRAALLTGRLPVRSGMYPGVLGPSSQGGLPLEEVTLAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPDIPCKGGCDQGLVPIPLLANLTVEAQPPWLPGLEARYVSFSRDLMADAQRQGRPFFLYYASHHTHYPQFSGQSFTKRSGRGPFGDSLMELDGAVGALMTTVGDLGLLEETLVIFTADNGPELMRMSNGGCSGLLRCGKGTTFEGGVREPALVYWPGHITPGVTHELASSLDLLPTLAALTGAPLPNVTLDGVDISPLLLGTGKSPRKSVFFYPPYPDEIHGVFAVRNGKYKAHFFTQGSAHSDTTSDPACHAANRLTAHEPPLLYDLSQDPGENYNVLESIEGVSPEALQALKHIQLLKAQYDAAMTFGPSQIAKGEDPALQICCQPSCTPHPVCCHCPGSQS
Protein: Liprin-alpha-4 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-4) (PTPRF-interacting protein alpha-4) (Q91Z80)
Organism: Rattus norvegicus (Rat)
Function: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with PTPRF at the cell surface. {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase F
- PPFIA binding protein 2
- Peripheral plasma membrane protein CASK
- PPFIA binding protein 1
- Protein lin-7 homolog A
- Regulating synaptic membrane exocytosis protein 1
- Peripheral-type benzodiazepine receptor-associated protein 1
- Regulating synaptic membrane exocytosis protein 2
Sequence:
DVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEETVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSGKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHVGSTTDVRFSLSTAAHVPPGLHRRYTALREESAKDWKPAPLPGVLAATTTPALTVTLRSPMWTRMSLGAWWALRLMSSHLVAILDAQTLAMMLQEQLDAINQEIRMIQEEKESTELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLASASPPLSGRSTPKLTSRSAAQDLDRMGVMTLPSDLRKHRRKLLSPVSREENREDKATIKCETSPPSSPRTLRLEKLGHPTLSQEEGKSALEGQDSNPSSSNSSQDSLHKGAKRKGIKSSIGRLFGKKEKGRLIHLSRDATGHVLLTDSELSLQEPMVPAKLGTQAEKDRRLKKKHQLLEDARRKGMPFAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLTSPSAPPTSRTSSGNVWVTHEEMETLATSTKTDSEEGSWAQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELEKRREESQHEIKDVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQNTQARQVMEREFNNLLALGTDRKLDDGEEKVFRRAPSWRKRFRPRDHHSGGMLGTSAETLPAGFRVSTLGPLQPPPAPPNKIMPEAHSHYLYGHMLSAFRD
Protein: V-type proton ATPase subunit D (V-ATPase subunit D) (Vacuolar proton pump subunit D) (Q86A77)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit F
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d
- V-type proton ATPase subunit G
Sequence:
MSGKNRLNIFPTRMALTVMKTKLKGAVTGHSLLKKKSDALTIRFRRILANIVENKQLMGTTMRDASFSLAAAKYAAGEFSNSVIENVSNPTIAVKMTTENVAGVHLPTFEKISEGVVSNSQELTGLSKGGQQINKSRESHIKAVEALIALASLQTAFITLDEVIKITNRRVNAIEYVVKPKLENTISYIITELDESEREEFYRLKKVQGKKKKDLKAKEAQKEENSANKTIMEPASVHKVRSLIDDEPEDAELLYED
Protein: Membrane protein (Q5FA01)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442}.
Interaction partners:
Sequence:
MKKALAALIALALPAAALAEGASGFYVQADAAHAKASSSLGSAKGFSPRISAGYRINDLRFAVDYTRYKNYKQAPSTDFKLYSIGASVIYDFDTQSPVKPYFGARLSLNRASAHLGGSDSFSKTSAGLGVLAGVSYAVTPNVDLDAGYRYNYVGKVNNVKNVRSGELSAGVRVKF
Protein: T-cell surface glycoprotein CD8 alpha chain (B8ZZZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV
Protein: 12S seed storage protein CRC (Cruciferin 3) (AtCRU3) (Cruciferin C) (Legumin-type globulin Cruciferin1) (Legumin-type globulin storage protein CRU1) [Cleaved into: 12S seed storage protein CRC alpha chain (12S seed storage protein CRC acidic chain); 12S seed storage protein CRC beta chain (12S seed storage protein CRC basic chain)] (Q96318)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seed storage protein.
Subcellular location: Protein storage vacuole {ECO:0000305}.
Interaction partners:
- 2S seed storage protein 1
- 2S seed storage protein 3
- 2S seed storage protein 2
- 2S seed storage protein 5
- Oleosin 21.2 kDa
- Oleosin 18.5 kDa
- 2S seed storage protein 4
- Oleosin 5
- 1-Cys peroxiredoxin PER1
- B3 domain-containing transcription factor ABI3
Sequence:
MVKLSNLLVATFGVLLVLNGCLARQSLGVPPQLQNECNLDNLDVLQATETIKSEAGQIEYWDHNHPQLRCVGVSVARYVIEQGGLYLPTFFTSPKISYVVQGTGISGRVVPGCAETFMDSQPMQGQQQGQPWQGRQGQQGQPWEGQGQQGQQGRQGQPWEGQGQQGQQGRQGQQGQPWEGQGQQGQQGFRDMHQKVEHVRRGDVFANTPGSAHWIYNSGEQPLVIIALLDIANYQNQLDRNPRVFHLAGNNQQGGFGGSQQQQEQKNLWSGFDAQVIAQALKIDVQLAQQLQNQQDSRGNIVRVKGPFQVVRPPLRQPYESEEWRHPRSPQGNGLEETICSMRSHENIDDPARADVYKPSLGRVTSVNSYTLPILEYVRLSATRGVLQGNAMVLPKYNMNANEILYCTGGQGRIQVVNDNGQNVLDQQVQKGQLVVIPQGFAYVVQSHGNKFEWISFKTNENAMISTLAGRTSLLRALPLEVISNGFQISPEEARKIKFNTLETTLTRAAGRQQQQLIEEIVEA
Protein: F-box/WD repeat-containing protein mec-15 (Mechanosensory abnormality protein 15) (Q22071)
Organism: Caenorhabditis elegans
Function: Plays a role in mechanosensory transduction (touch sensitivity), touch receptor neuron development and synapse formation. Regulates expression of the protein snb-1 and the distribution of synaptic vesicles at synapses to promote synaptic transmission at the neuromuscular junctions of GABAergic motor neurons.
Subcellular location: Perikaryon {ECO:0000269|PubMed:23527112}.
Interaction partners:
- RING-box protein 1
- RING-box protein 2
- Ubiquitin-ribosomal protein eL40 fusion protein
- Cell division control protein
- Cullin-3
- Cullin-1
- Polyubiquitin-A
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- Ubiquitin-like domain-containing protein
- Tubulin alpha-3 chain
Sequence:
MTNAQPTELISLPSELLCHLFTYLPQRQLITEIPLVCRRFNTILNDDKFWSRRIRTEQKVRLPDCELKHPEYEPKKSFYAMHRQRDRWRAWETQTVITAPGHSATVDSVMLFENNNKQFCLSGSRDRTIRLWSIENARNGEDTEQNPWTVAKDDTAHSGWIWNMAQESTSTNFYTTSWDSTVKSWHITDNGALQNLNSVNVGSAAQCISCSGNENEVVCTTFAKRVAVIDSRTFQVVADHKLHKRAVIALAVQGDKIFTSGEDRLMMMVDRRNFSKPVLFEYSPTAYKSCLSLQCNQLLTSTSDGKVKLYDANNFNVLQTYSVGSYTRQSFLEHGAHLIMARSLKRNYTFSIYSPGTRSQQWCASHELAAEPAKFDYSPSSRTLAIGNGDSSILFCLPASAPDQEN
Protein: NADAR domain-containing protein (G5EFJ3)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- SMP domain-containing protein
- NAD-dependent epimerase/dehydratase domain-containing protein
- F-box domain-containing protein
- CUB_2 domain-containing protein
Sequence:
MHTRILNAKNQQTYVLFYEDESVFSNFHPSNFEAETAKKLVNSGMFKEEEMLKFNCSEQYFMYHKALLVGDVDSAKVIITAKHPMVMKMTGRQLNMNRHDIDNWTQKSRDIMYLACLAKFSQNVELRKMLFRTQDMYLVEASGNDAIWGNGIWKEDKRSDDVANWHGTNYLGEILDRIRGELIGKPEFAAEKEAVQLESLEQRIQMLMA
Protein: Hydrolase-like protein family (F4HZW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein RESPONSE TO LOW SULFUR 1
- Protein RESPONSE TO LOW SULFUR 2
- Protein RESPONSE TO LOW SULFUR 3
- F17F16.6 protein
- Protein RESPONSE TO LOW SULFUR 4
- 5'-adenylylsulfate reductase 3, chloroplastic
- Sulfate transporter 1.2
- 5'-adenylylsulfate reductase 1, chloroplastic
- Protein SNOWY COTYLEDON 3
- Polyadenylate-binding protein 3
Sequence:
MSTASSWIQQPPFRYLPDRGGFSKPSSRSARQFSSGVVSASASSPSPSSSCSCGYSEILNFDFGSNRSWNQQGRRVQAMSSTAQRKFSLSKGDSDDKNEPDHLLVLVHGILASPSDWLYVEAELKRRLGRRFLIYASSSNTFTKTFGGIDGAGKRLAEEVRQVVQKSKSLKKISFLAHSLGGLFSRHAVAVLYSAAMAQVSDVAVSQSGNSNLLRGRIAGLEPINFITLATPHLGVRGRKQLPFLLGVPILEKLAAPIAPFFVGRTGSQLFLTDGKADKPPLLLRMASDGEDLKFLSALGAFRSRIIYANVSYDLDMVGWRTSSIRRETELIKPSRRSLDGYKHVVDVEYCPPVSSDGAHFPPEAAKAKEAAQSSPSPQNTLEYHEIVEEEMIRGLQRLGWKKVDVSFHSTFWPYLAHNNIHVKSERLYKAGAGVIAHVADSIKQQESSTFITASL
Protein: Subtilisin-like protease SBT4.3 (EC 3.4.21.-) (Subtilase subfamily 4 member 3) (AtSBT4.3) (Q9FIF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
Interaction partners:
- Putative pectinesterase 63
- Organic cation/carnitine transporter 3
- Putative pectinesterase/pectinesterase inhibitor 45
Sequence:
MAKLSTPLYLICLAFIFTRDVSANDYRQASSVYIVYMGTLPEIKYSPPSHHLSILQKLVGTIAASHLLVRSYKRSFNGFAANLSQAESQKLQNMKEVVSVFPSKSHELTTTRSWDFVGFGEKARRESVKESDVIVGVIDSGIWPESESFDDEGFGPPPKKWKGSCKGGLKFACNNKLIGARFYNKFADSARDEEGHGTHTASTAAGNAVQAASFYGLAQGTARGGVPSARIAAYKVCFNRCNDVDILAAFDDAIADGVDVISISISADYVSNLLNASVAIGSFHAMMRGIITAGSAGNNGPDQGSVANVSPWMITVAASGTDRQFIDRVVLGNGKALTGISVNTFNLNGTKFPIVYGQNVSRNCSQAQAGYCSSGCVDSELVKGKIVLCDDFLGYREAYLAGAIGVIVQNTLLPDSAFVVPFPASSLGFEDYKSIKSYIESAEPPQAEILRTEEIVDREAPYVPSFSSRGPSFVIQNLLKPDVSAPGLEILAAFSPVASPSSFLNPEDKRSVRYSVMSGTSMACPHVAGVAAYVKSFHPDWSPSAIKSAIMTTATPMNLKKNPEQEFAYGSGQINPTKASDPGLVYEVETEDYLKMLCAEGFDSTTLTTTSGQNVTCSERTEVKDLNYPTMTTFVSSLDPFNVTFKRTVTNVGFPNSTYKASVVPLQPELQISIEPEILRFGFLEEKKSFVVTISGKELKDGSFVSSSVVWSDGSHSVRSPIVAYSIQP
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Oligosaccharyl transferase subunit alpha) (Q10176)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Uncharacterized protein C553.06
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Probable protein transport protein Sec61 subunit gamma
- Protein transport protein sec61 subunit beta
- Protein transport protein sec61 subunit alpha
- Dol-P-Glc:Glc
- Probable mannosyl-oligosaccharide glucosidase
Sequence:
MLVLKLLLWSIISGLSLAEQVWRNSNAIRTIDLRSTYTKTLTSLIIVNEGDEPQNTYRYFQQTSPGESVLSLSVSIKEEEKKGTNPIKVNNNVYDIPLQPPVKPGESRTLLIQAGLDGGVRPLPAAVDQDEEQYLVYLTTLYLDSPYTTDLQRTRLILPSAKIDTYTTYNIDGAELPNRVGNTLVYESRETITGEDNDLGEIYVRYEHTVPIPRGADLYVQIDMHEYRKMLEVSERVVFENHAAKLKSNFDRAKWYMGNFYNPVSTAINRVVYSLPRNSKDVYYTDEVGNITTSHMRVEPHQTWIELNPRYPVFGGWNYLFQLDWKMPYEEFRSSKNRREYLDIPLAWSPGDMIYEKAVWSYVFPEGATNIEIEMPVEISNSNVTKIHKFLDTLGRQVFTYEALNVTDGVPSDIVHISYEYNSSAFFLRIAIITTLLILLAAAAYMIWAP
Protein: Photosystem II reaction center protein H (PSII-H) (Photosystem II 10 kDa phosphoprotein) (P56780)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:11113141, ECO:0000269|PubMed:20923938}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00752}.
Interaction partners:
- Photosystem II reaction center protein M
- Photosystem II reaction center protein T
- Cytochrome b559 subunit alpha
- Photosystem II protein D1
- Photosystem II CP47 reaction center protein
- Cytochrome b559 subunit beta
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein Z
- Photosystem II reaction center protein I
Sequence:
MATQTVEDSSRSGPRSTTVGKLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISVN
Protein: Uric acid-xanthine permease (UAPA transporter) (Q07307)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Uric acid-xanthine transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20002879}; Multi-pass membrane protein {ECO:0000269|PubMed:20002879}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 2
- Uncharacterized protein
- Got1 family protein
- Uricase
- Dihydroorotate dehydrogenase
Sequence:
MDNSIHSTDGPDSVIPNSNPKKTVRQRVRLLARHLTTREGLIGDYDYGFLFRPELPFMKKDPRAPPFFGLNEKIPVLLAFILGLQHALAMLAGVVTPPLIISSSLSLPSDLQQYLVSTSLIVCGLLSMVQITRFHIYKTPYYIGSGVLSVMGVSFSIISVASGAFNQMYSNGFCQLDEAGNRLPCPEAYGALIGTSACCALVEILLAFVPPKVIQKIFPPIVTGPTVMLIGISLIGTGFKDWAGGSACMDDGMLCPSATAPRPLPWGSPEFIGLGFLVFVSIILCERFGAPIMKSCSVVIGLLVGCIVAAACGYFSHADIDAAPAASFIWVKTFPLSVYGPMVLPIIAVFIICACECIGDVTATCDVSRLEVRGGTFESRIQGAVLADGINSVVAALATMTPMTTFAQNNGVIALTRCANRWAGYCCCLILIVAGIFAKFAAAIVAIPNSVMGGMKTFLFASVVISGQAIVAKAPFTRRNRFILTASMALGYGATLVPTWFGNVFPQTENRDLEGFENAIELVLETGFAVTAFVAMLLNAIMPAEVEEIGAVTPMPVSAHDNRDGEAEYQSKQA
Protein: BfmR (Q9HWS7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- histidine kinase
- Uncharacterized protein
- DoxX family protein
- EF-hand domain-containing protein
- UPF0276 protein PA4106
- Uncharacterized protein
- histidine kinase
- histidine kinase
- Sensor protein kinase PmrB
- histidine kinase
Sequence:
MEHVDHILIVDDDREIRELVGNYLKKNGLRTTIVADGRQMRAFLEANTVDLIVLDIMMPGDDGLLLCRELRVGKHKATPVLMLTARNDETDRIIGLEMGADDYLTKPFSARELLARINAVLRRTRMLPPNLTVSESSRLIGFGQWQLDTSARHLLDDAGTVVALSGAEYRLLRVFLDHPQRVLSRDQLLNLTQGREADIFDRSIDLLVSRLRQRLGDDAREPEYIKTVRSEGYVFSLPVRLVEAHP
Protein: Multidrug efflux pump Tap (Tetracycline/aminoglycoside resistance-like efflux pump) (P9WJX9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Efflux pump that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy (By similarity). Confers resistance to rifampicin. Confers low-level resistance to tetracycline and to several aminoglycosides, including streptomycin, gentamicin, 2'-N-ethylnetilmicin and 6'-N-ethylnetilmicin.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable oxidoreductase
- N-acetyltransferase Eis
- Fluoroquinolones export permease protein Rv2686c
- Drug efflux pump JefA
- Multidrug resistance protein Mmr
- Multidrug efflux system ATP-binding protein Rv1218c
- Small ribosomal subunit protein uS5
- Uncharacterized MFS-type transporter EfpA
- Uncharacterized protein Rv1260
Sequence:
MRNSNRGPAFLILFATLMAAAGDGVSIVAFPWLVLQREGSAGQASIVASATMLPLLFATLVAGTAVDYFGRRRVSMVADALSGAAVAGVPLVAWGYGGDAVNVLVLAVLAALAAAFGPAGMTARDSMLPEAAARAGWSLDRINGAYEAILNLAFIVGPAIGGLMIATVGGITTMWITATAFGLSILAIAALQLEGAGKPHHTSRPQGLVSGIAEGLRFVWNLRVLRTLGMIDLTVTALYLPMESVLFPKYFTDHQQPVQLGWALMAIAGGGLVGALGYAVLAIRVPRRVTMSTAVLTLGLASMVIAFLPPLPVIMVLCAVVGLVYGPIQPIYNYVIQTRAAQHLRGRVVGVMTSLAYAAGPLGLLLAGPLTDAAGLHATFLALALPIVCTGLVAIRLPALRELDLAPQADIDRPVGSAQ
Protein: ABC transporter, putative (Q386J8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peroxin 19
- ABC transporter, putative
- Peroxin-13
- ABC transporter, putative
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein, putative
- Nonspecific lipid-transfer protein, putative
- propanoyl-CoA C-acyltransferase
- Aldehyde dehydrogenase
- AAA+ ATPase domain-containing protein
Sequence:
MSSVLDGLKQLLVASPFSHAKYALLVVIALLFQGVHKCVLARRANPSSPRRHAGKASGRHRRPTVRFDSTLFWRVVGLLRICFPSVLSPESGTMVALTLLLALRTRLTLMLSRVAGNNVKALVQKNFRELLLGIGDIALYALPATVVNVGIGYTISSIEWRFRERLQHALHKEYFQGRRVYDLATTGTVDNPGHRVTNDVQCFSRELAVLIPSILKPSMDIVTFSSALAEHGGHNESLLIFSYYAFVAVLFRLILPNFATMMAASHAKEGNLRTMHTQLLHHAEEVAFYRGADVERATADRLLRSYLRLESNIKRLKWWSTLVSSMFVEYGSTCVGLAVCGFAVARRADSMDAAGMAQLYARNAKLCTSLAKSIARLFSIHLKVSAVCGGAHRVGELQDSLRSLERNERETTLSLVEESSDDKIVFKNAYILSPSDKMILANYNATFKADRHVLIMGCNGAGKTALIRVITGVWSLREGSLKRPPPSQMVVLTQRVYLPPGTLRTQFTYPTSEADKRAGDIEDAKLVEFATRVGLRGLLTRVGGLDAWKEWSEVLSGGERQRVAFVRALYHRPTFVFLDECTSAVSQNIEPTLYKLLLDEGMTLITTSHRESLKKFHHDIMMLDGVGGYTETEVGQPRVTI
Protein: Zygotic DNA replication licensing factor mcm6-A (EC 3.6.4.12) (Zygotic minichromosome maintenance protein 6-A) (zMCM6-A) (zMCM6a) (Q498J7)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development. May replace mmcm6 in the mcm2-7 complex.
Subcellular location: Nucleus {ECO:0000250}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250}.
Interaction partners:
Sequence:
MDLVDPSQSAAAAAGTQLVKDEVAEKCQKLFQDFLEEFQGSDGELKYQSDAEELIRPERNTLLVSFVDLEQFNQQLATTIQEEFYRVYPYLCRAVRAFARDHGNIPQNKEFYVAFQDLPTRHKIRELTTPRIGSLLRISAQVVRTHPVHPELVSGTFLCLDCQTLVRDVEQQFKYTQPSICRNPVCANRRRFMLDTNKSRFVDFQKVRIQETQAELPRGSIPRSVEVILRAEAVESCQAGDRCDFTGSLIVVPDISQLSTPGVRAETSSRVGGREGYEAEGVQGLRALGVRDLSYKLVFLACYVCPTNPRFGGKELHEEDMTAESIKNQMSVKEWEKVFEMSQDKNLYHNLCTSLFPTVHGNDEVKRGILLMLFGGVPKSTMEGTSLRGDINVCVVGDPSTAKSQFLKHVEEFSPRAVYTSGKASTAAGLTAAVVKDEESHEFVIEAGALMLADNGVCCIDEFDKMDTKDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVGGRYDRAKSLKQNVNLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYTVDEVRRYLLFARQFKPKISKESADFIVEQYKRLRQRDGSGVTKSAWRITVRQLESMIRLSEGMARMHCSDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQDDEHEPEDETQEGTNGDAEVPNGVNGHVNGINGHSQESNAAAAKPSLRLNFAEYKRISNLLVQQLRKMEDEDETSQRRSELMNWYLKEIESEIDSEEELINRKQIIDKVIHRLVHYDQILIELTQTELKGTGDEVVAKEEDPYLVVNPNYILED