wanglab/gogpt-training-data huggingface dataset:
Protein: Protein OS-9 (Q5RKH6)
Organism: Rattus norvegicus (Rat)
Function: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4 (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q13438}.
Interaction partners:
- Protein sel-1 homolog 1
- Endoplasmin
- Derlin
- E3 ubiquitin-protein ligase synoviolin
- Derlin
- Derlin
- Transitional endoplasmic reticulum ATPase
- Egl nine homolog 1
- E3 ubiquitin-protein ligase AMFR
- alpha-1,2-Mannosidase
Sequence:
MAAEALLSSLLGLLFLGLLLPAHLTGGVGSLNLEELSEMRYGIQILPLPVMGGQSQASDVVVVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPELLSPMRDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGDVLYLGYYQSAFNWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGKPREAEVRFLCDEGAGISGDYIDRVDEPFSCSYVLSIRTSRLCPHPLLRPPASAAPQAILCHPALQPDEYMAYLQRQAESKQHEEKVTEEVQDTDHQVWSGSKAAGAPPKKEDVSPTKEDKESEFWKMLQEPEEQATGTEEAQAGEQDLNHEAAADPAPAPPTDFQNNVQVKLIRSPADLIRLIEELKGAEKGKPSVRQEQPGDDTTEAPQREAEAKGKGGEPRGLVEEEDGDEEEEDEDEDEQQLLGEFEKELEGMLLPSDRERLRSEVKAGMERELENIIQETEKELDPEGLRKESEREQAILALTSTLDKLIKRLQESQSPELVQKYKKRRVVPQKPPPSPHPTEEEPEHRVRVRVTKLRHGGPNQDLTVLEMNRENPQLKQIEGLVTEVLEREGLTAEGKIEIKIVRPGAEGKEEDTRWLTDEDTRNLKEIFFNILVQGAEEANKERQRQSELESNYRRVWGSPGGEDTGDLDEFDF
Protein: UNC-76 (E0AHC6)
Organism: Caenorhabditis elegans
Interaction partners:
- Short coiled-coil protein homolog
- Kinesin heavy chain
- Protein unc-119
- Cell death protein 6
- Serine/threonine-protein kinase unc-51
- RUN domain-containing protein
- Kinesin-like protein vab-8
- Synaptotagmin-1
- Thioredoxin-related transmembrane protein 1
- CED-5
Sequence:
MEAADLRVPDIPLASCDDDDIDSNKNLSNHSSDEKHHCNSNSDEERLHDEFSGSLEDLVGNFDEKIAACLKDHEVTTADIAPVQIRTQEEVMNESQTWWTLTGNFGNIQPLDFGTSSICKKMAAALDSDSLKDDASTRRSMTNSDDEDLLRQQMDVHQMIGHHHGSTDTGGETPPQTADQVIEEIDEMLQSCDFTGSMMTDRTMESVDSMYSSMRSPFPSSIQSSDADIKLRSAQALVSNPDTAAKTAAFHSDLQELSYSKLVTLCAEMEQLIRVYNESLVDELAHRDELDYEKEMKNSFISLLLAIQNKRRVYANDRKRKVGKASDASQLPQYLTATIPYNDHQHIDNASIASLIKILRAIHDDNTTVPTLLTDYILTHVCPKNISC
Protein: Solute carrier family 28 member 3 (Concentrative Na(+)-nucleoside cotransporter 3) (CNT 3) (hCNT3) (Q9HAS3)
Organism: Homo sapiens (Human)
Function: Sodium-dependent, pyrimidine- and purine-selective. Involved in the homeostasis of endogenous nucleosides. Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine). Employs a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:21998139}; Multi-pass membrane protein {ECO:0000269|PubMed:32776918}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18827020}; Multi-pass membrane protein {ECO:0000269|PubMed:32776918}.
Interaction partners:
- Equilibrative nucleoside transporter 1
- Equilibrative nucleoside transporter 2
- Equilibrative nucleoside transporter 3
- Deoxycytidine kinase
- Equilibrative nucleoside transporter 4
Sequence:
MELRSTAAPRAEGYSNVGFQNEENFLENENTSGNNSIRSRAVQSREHTNTKQDEEQVTVEQDSPRNREHMEDDDEEMQQKGCLERRYDTVCGFCRKHKTTLRHIIWGILLAGYLVMVISACVLNFHRALPLFVITVAAIFFVVWDHLMAKYEHRIDEMLSPGRRLLNSHWFWLKWVIWSSLVLAVIFWLAFDTAKLGQQQLVSFGGLIMYIVLLFLFSKYPTRVYWRPVLWGIGLQFLLGLLILRTDPGFIAFDWLGRQVQTFLEYTDAGASFVFGEKYKDHFFAFKVLPIVVFFSTVMSMLYYLGLMQWIIRKVGWIMLVTTGSSPIESVVASGNIFVGQTESPLLVRPYLPYITKSELHAIMTAGFSTIAGSVLGAYISFGVPSSHLLTASVMSAPASLAAAKLFWPETEKPKITLKNAMKMESGDSGNLLEAATQGASSSISLVANIAVNLIAFLALLSFMNSALSWFGNMFDYPQLSFELICSYIFMPFSFMMGVEWQDSFMVARLIGYKTFFNEFVAYEHLSKWIHLRKEGGPKFVNGVQQYISIRSEIIATYALCGFANIGSLGIVIGGLTSMAPSRKRDIASGAVRALIAGTVACFMTACIAGILSSTPVDINCHHVLENAFNSTFPGNTTKVIACCQSLLSSTVAKGPGEVIPGGNHSLYSLKGCCTLLNPSTFNCNGISNTF
Protein: Elongation factor 1-alpha (Q3LUM2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-beta 2-like
- Elongation factor 1-beta 2-like isoform X1
- Elongation factor 1-beta 2-like
- Elongation factor 1-delta-like
- Elongation factor 1-delta-like
- GTP-binding nuclear protein
- GTP-binding nuclear protein
Sequence:
MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPEKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFGPSGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGFVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAELLTKIDRRSGKELEKEPKFLKNGDAGMIKMVPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKSAAKKGK
Protein: Energy-coupling factor transporter ATP-binding protein EcfA2 (ECF transporter A component EcfA2) (EC 3.6.3.-) (ECF transporter A component EcfA') (A2RI02)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. In this organism these probably include biotin, thiamine precursor, niacin, pantothenic acid, queuosine precursor, riboflavin and thiamine. Uptake of niacin or riboflavin into proteosomes containing EcfA1A2T and Niax or RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-containing proteosomes did not transport riboflavin.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Peripheral membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Energy-coupling factor transporter transmembrane protein EcfT
- Energy-coupling factor transporter ATP-binding protein EcfA1
- Putative cobalt ABC transporter permease protein
- Biotin transporter BioY
- Pantothenic acid transporter PanT
- Thiamine transporter ThiT
- Riboflavin transporter RibU
- Thiamine precursor transporter HmpT
- Biotin transporter BioY2
- Putative ABC transporter ATP-binding protein
Sequence:
MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATHFADQLQKTGAVAFEKLPITRAELVTLLTSLSVNSGGEN
Protein: Prefoldin subunit 6 (Protein Ke2) (O15212)
Organism: Homo sapiens (Human)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Interaction partners:
- Prefoldin subunit 5
- p53 and DNA damage-regulated protein 1
- Prefoldin subunit 4
- Prefoldin subunit 3
- Prefoldin subunit 1
- Prefoldin subunit 2
- Protein UXT
- RNA polymerase II-associated protein 3
- Dynein axonemal assembly factor 10
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRAQAAKAGAPGKA
Protein: DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4) (Q9UBS4)
Organism: Homo sapiens (Human)
Function: As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998, ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}. Note=Associated with the ER membrane in a C-terminally epitope-tagged construct.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- Stromal cell-derived factor 2-like protein 1
- Stromal cell-derived factor 2
- Protein disulfide-isomerase A4
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase A6
- Peptidyl-prolyl cis-trans isomerase B
- Heat shock cognate 71 kDa protein
- Mesencephalic astrocyte-derived neurotrophic factor
Sequence:
MAPQNLSTFCLLLLYLIGAVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHPIFERRGDDLYTNVTISLVESLVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAREGIKQLLKQGSVQKVYNGLQGY
Protein: Transcription factor bHLH147 (ATBS1 interacting factor 3) (Basic helix-loop-helix protein 147) (AtbHLH147) (bHLH 147) (Transcription factor EN 142) (bHLH transcription factor bHLH147) (Q9LSN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical bHLH transcription factor probably unable to bind DNA. Negatively regulates brassinosteroid signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor PRE3
- SAP domain-containing protein
- Transcription factor IBH1
- Transcription factor bHLH48
- Transcription factor bHLH79
- GDSL esterase/lipase At1g28580
- Transcription factor PRE6
- 2-oxoglutarate
- Transcription factor bHLH49
- Putative transcription factor bHLH041
Sequence:
MESISPVSNQLLQPTTTSSNSDRSRRKRKKKSSPSSVEKSPSPSISLEKWRSEKQQQIYSTKLVHALRELRISQQPSSSSSSSIPRGGRAVREVADRALAVAARGKTLWSRAILSKAVKLKFRKHKRQRISNPTTTTLTTGSIRSKKQRATVLRLKAKGLPAVQRKVKVLSRLVPGCRKQSLPVVLEETTDYIAAMEMQIRTMTAILSAVSSSPPPPTPGHEGGQTHMLG
Protein: Bifunctional purine biosynthesis protein PurH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)] (P9WHM7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Phosphoribosylglycinamide formyltransferase
- Adenylosuccinate lyase
- Bifunctional protein FolD
- N5-carboxyaminoimidazole ribonucleotide synthase
- Adenylosuccinate synthetase
- Phosphoribosylamine--glycine ligase
- Serine hydroxymethyltransferase 2
- Serine hydroxymethyltransferase 1
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Phosphoribosylglycinamide formyltransferase 2
Sequence:
MSTDDGRRPIRRALISVYDKTGLVDLAQGLSAAGVEIISTGSTAKTIADTGIPVTPVEQLTGFPEVLDGRVKTLHPRVHAGLLADLRKSEHAAALEQLGIEAFELVVVNLYPFSQTVESGASVDDCVEQIDIGGPAMVRAAAKNHPSAAVVTDPLGYHGVLAALRAGGFTLAERKRLASLAFQHIAEYDIAVASWMQQTLAPEHPVAAFPQWFGRSWRRVAMLRYGENPHQQAALYGDPTAWPGLAQAEQLHGKDMSYNNFTDADAAWRAAFDHEQTCVAIIKHANPCGIAISSVSVADAHRKAHECDPLSAYGGVIAANTEVSVEMAEYVSTIFTEVIVAPGYAPGALDVLARKKNIRVLVAAEPLAGGSELRPISGGLLIQQSDQLDAHGDNPANWTLATGSPADPATLTDLVFAWRACRAVKSNAIVIAADGATVGVGMGQVNRVDAARLAVERGGERVRGAVAASDAFFPFPDGLETLAAAGVTAVVHPGGSVRDEEVTEAAAKAGVTLYLTGARHFAH
Protein: ESX-1 secretion-associated protein EspL (P9WJB9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably plays a role in host phagosome maturation arrest.
Interaction partners:
- ESX-1 secretion-associated protein EspB
- ESX-1 secretion system protein EccE1
- ESX-1 secretion-associated protein EspH
- Mycosin-1
- ESX-1 secretion-associated protein EspK
- Recombination protein RecR
- ESX-1 secretion-associated protein EspI
Sequence:
MSMDELDPHVARALTLAARFQSALDGTLNQMNNGSFRATDEAETVEVTINGHQWLTGLRIEDGLLKKLGAEAVAQRVNEALHNAQAAASAYNDAAGEQLTAALSAMSRAMNEGMA
Protein: Ferric enterobactin-binding periplasmic protein FepB (P0AEL6)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex FepBDGC involved in ferric enterobactin uptake. Binds ferric enterobactin. Can also bind ferric enantioenterobactin, the left-handed stereoisomer of the natural E.coli siderophore, and the apo-siderophore, enterobactin, but does not bind ferric agrobactin.
Subcellular location: Periplasm {ECO:0000269|PubMed:10986237, ECO:0000269|PubMed:3011753, ECO:0000305|PubMed:2529253}.
Interaction partners:
- Ferric enterobactin transport system permease protein FepG
- Ferric enterobactin transport ATP-binding protein FepC
- Ferric enterobactin transport system permease protein FepD
- Iron
- Enterobactin exporter EntS
- Isochorismate synthase EntC
- Ferrienterobactin receptor
- Enterobactin synthase component B
- Enterobactin synthase component E
- Enterobactin synthase component F
Sequence:
MRLAPLYRNALLLTGLLLSGIAAVQAADWPRQITDSRGTHTLESQPQRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADDQGFLRQWSKVAKERKLQRLYIGEPSAEAVAAQMPDLILISATGGDSALALYDQLSTIAPTLIINYDDKSWQSLLTQLGEITGHEKQAAERIAQFDKQLAAAKEQIKLPPQPVTAIVYTAAAHSANLWTPESAQGQMLEQLGFTLAKLPAGLNASQSQGKRHDIIQLGGENLAAGLNGESLFLFAGDQKDADAIYANPLLAHLPAVQNKQVYALGTETFRLDYYSAMQVLDRLKALF
Protein: Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (Renin/prorenin receptor) (Vacuolar ATP synthase membrane sector-associated protein M8-9) (V-ATPase M8.9 subunit) [Cleaved into: Renin receptor extracellular fragment; Renin receptor cytoplasmic fragment] (P81134)
Organism: Bos taurus (Bovine)
Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit C 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 1
- V-type proton ATPase 116 kDa subunit a 1
- Ribonuclease kappa
- V-type proton ATPase subunit F
Sequence:
MAVLVVFLSFLVADVFGNEFSILRSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVDKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLTSLPLNSLSRNNEVDLLFLSELQVLRDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKHYGEDSEQFRDASKILIDALQKFADDMYNLYGGNAVVELVTVRSFDTSLVRKTRNILETKQVKDPSTTYNLAYKYNFEYPVVFNLVLWIMIGLALTLIVTCYNIWNMDPGYDSIIYRMTNQKIRMD
Protein: Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I) (Q13541)
Organism: Homo sapiens (Human)
Function: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22684010}. Nucleus {ECO:0000269|PubMed:22684010}. Note=Localization to the nucleus is unaffected by phosphorylation status. {ECO:0000250|UniProtKB:Q60876}.
Interaction partners:
- Regulatory-associated protein of mTOR
- Eukaryotic translation initiation factor 4E
- Serine/threonine-protein kinase mTOR
- Target of rapamycin complex subunit LST8
- Eukaryotic translation initiation factor 4E type 2
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E type 1B
- GTP-binding protein Rheb
- Mitogen-activated protein kinase 1
- Proline-rich AKT1 substrate 1
Sequence:
MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI
Protein: Tropomyosin (Tropomyosin, slow-tonic isoform) (Tm-Chio-tonic) (A2V735)
Organism: Chionoecetes opilio (Atlantic snow crab) (Cancer opilio)
Function: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Interaction partners:
Sequence:
MDAIKKKMQAMKLEKDNAMDKADTLEQQNKEANLRAEKTEEEIRANQKKSQLVENELDHAQEQLSAATHKLVEKEKAFANAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAESGESKIVELEEELRVVGNNLKSLEVSEEKANQREETYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKNIADEMDQAFSELSGF
Protein: Sperm protein associated with the nucleus on the X chromosome N3 (Nuclear-associated protein SPAN-Xn3) (SPANX-N3) (SPANX family member N3) (Q5MJ09)
Organism: Homo sapiens (Human)
Interaction partners:
- F-box/WD repeat-containing protein 2
Sequence:
MEQPTSSTNGEKTKSPCESNNKKNDEMQEVPNRVLAPEQSLKNTKTSEYPIIFVYYLRKGKKINSNQLENEQSQENSINPIQKEEDEGVDLSEGSSNEDEDLGPCEGPSKEDKDLDSSEGSSQEDEDLGLSEGSSQDSGED
Protein: Small ribosomal subunit protein eS27B (40S ribosomal protein S27-B) (RP61) (YS20) (P38711)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS8A
- Small ribosomal subunit protein eS21B
- Small ribosomal subunit protein eS25A
- Small ribosomal subunit protein eS1B
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS11A
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS19B
Sequence:
MVLVQDLLHPTAASEARKHKLKTLVQGPRSYFLDVKCPGCLNITTVFSHAQTAVTCESCSTVLCTPTGGKAKLSEGTSFRRK
Protein: Mitochondrial ATP-independent inner membrane protease subunit 2 (AtIMP2) (EC 3.4.21.-) (Q84VZ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:28936218}.
Interaction partners:
- Mitochondrial inner membrane protease ATP23
- Mitochondrial ATP-independent inner membrane protease subunit 1a
- Peptidase S24/S26A/S26B/S26C family protein
- Mitochondrial inner membrane protease subunit 2
- Mitochondrial metalloendopeptidase OMA1
- Mitochondrial intermediate peptidase, mitochondrial
- Cyanate hydratase
- Probable thylakoidal processing peptidase 2, chloroplastic
- RHOMBOID-like protein 12, mitochondrial
- Intermediate cleaving peptidase 55, mitochondrial
Sequence:
MASISTWFRYMAHKLEYSLTLSLKSHRSNKLSDRELIQIICKNLFYGKITYLHSDKGPEMSPTMTANENTLLIRKIPIANTRFVFIGDAVVLKDPNDSDKYLVRRLAAVEGFEMVSGDEKEEPFVLEKNQCWVTAENQELKAKEAYDSRTFGPVSTADIVGRAIYCLRTAVDHGPVRNSQTAMGQDSPILAVELDVDEMAKNHKA
Protein: Protein PAM68, chloroplastic (PHOTOSYNTHESIS AFFECTED MUTANT 68) (O49668)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in early steps in photosystem II (PSII) biogenesis and in maturation and stability of newly synthesized psbA protein.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:20923938}; Multi-pass membrane protein {ECO:0000269|PubMed:20923938}.
Interaction partners:
- Photosystem II stability/assembly factor HCF136
- Protein LPA2
- Protein LOW PSII ACCUMULATION 1
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244
- Photosystem II CP43 reaction center protein
- Thylakoid membrane protein TERC, chloroplastic
- Photosystem II D1 precursor processing protein PSB27-H2, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Chloroplast protein HCF243
- Light-harvesting complex-like protein OHP1, chloroplastic
Sequence:
MASVPCSFKLSAHRRSSSKLDGNNKQCSSLVERLRDKTKSQVPKSITCINRLEISRIAPLHATMNSPKGFGPPPKKTKKSKKPKPGNQSDEDDDDEDEDDDDEEDERERGVIPEIVTNRMISRMGFTVGLPLFIGLLFFPFFYYLKVGLKVDVPTWVPFIVSFVFFGTALAGVSYGIVSSSWDPLREGSLLGWNEAKKNWPVFWQSFWNSSDKR
Protein: Cell wall integrity and stress response component 3 (Q12215)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- RHO1 GDP-GTP exchange protein 2
- RHO1 GDP-GTP exchange protein 1
- Cell wall integrity and stress response component 2
- Protein SLG1
- Cell wall integrity sensor MID2
- Protein MTL1
- Protein kinase C-like 1
- GTP-binding protein RHO1
- MAP kinase kinase MKK1/SSP32
- Serine/threonine-protein kinase BCK1/SLK1/SSP31
Sequence:
MERVWFAKLTNKGTIKIGYISFILLSLLCQSLIGLVNADFNYEGCYSAADIQSAGLSLKNSYIYQSVSYCQNQCPESAVVALFNGSDCYCGNSVSFLTSLTKSTDSNCGTKCSGWPYQMCGGSSYMNVYVNAETFVSSVESSSSKEGSSTSYMPSTTSSLSSAQISSTTRRTSTDMKSSEMIATTVSTTSTTSSSTSSTTSSTTSSTTSSTTSSTTSSSTSSTTSSTTSSTTSSTTSSTTSSTTSSTTSSTTSSTTSIFSVTSSSSSITLSSSEHTTVDSRTSSPSSTLVPVSSSSSTLSTPKVTSMTPSTSSTIPIVTSVELVTSVVTKAIVSTSDQHQETIFVTRTSVVERSSEVATATAAASNNRSNSTSKQRLSGGAIAGIVIGVVFGVIFIILILLFLIWRRRKSHDQLDLEETKHYQPYSFGDEDANPIGPPPSSGTTNWMRHSRGNTAGSIGTSNMYGFSMSNGANYSSPSSNTSGSIINNLAGLQDATVQKQNLPSTVFEEANTLNSANERFSANSLPDMMMSGPLQVVNPDNPDNPELSSTVSHNRA
Protein: Probable pinoresinol-lariciresinol reductase 3 (AtPLR3) (EC 1.23.1.-) (lariciresinol reductase) (O65679)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable reductase that might be involved in the reduction of lariciresinol into secoisolariciresinol. In most plant species, a single enzyme is able to reduce both pinoresinol and lariciresinol efficiently while in Arabidopsis, PRR1 and PRR2 show a strict substrate selectivity for pinoresinol.
Interaction partners:
- Protein PHOTOPERIODIC CONTROL OF HYPOCOTYL 1-LIKE
- Probable receptor-like serine/threonine-protein kinase At4g34500
- Uncharacterized acetyltransferase At3g50280
- Small ribosomal subunit protein eS25x
Sequence:
MEEEKKKSRVLIIGATGRLGNYLTRFSIESGHPTFALIRNTTLSDKLKSLSDAGVTLLKGSLEDEGSLAEAVSKVDVVISAIPSKHVLDQKLLVRVIKQAGSIKRFIPAEYGANPDKTQVSDLDHDFYSKKSEIRHMIESEGIPYTYICCGLFMRVLLPSLVQPGLQSPPTDKVTVFGDGNVKAVFVNDVDVAAFTIKTIDDPRTLNKTLYLSPPGNICSMNDLVELWEGKIEKKLEKTFATENQLLKKIKETPYPDNMEMVFIYSVFIKGDHTYFDIESCGGVNGTELYPDVKYMTVSEFLDTLL