wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (Complex I-B14) (NADH-ubiquinone oxidoreductase B14 subunit) (Q7JZK1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- GM23292p
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
Sequence:
MAGREAVKRAVQQVRPILSVDREEARKRALNLYKAWYRQIPYIVMDYDIPMTVEQCRDKLREEFVKHRNVTDIRVIDMLVIKGQMELKESVEIWKQKGHIMRYWKESQDPKPTDFLSKFIQGVN
Protein: Pectate lyase (EC 4.2.2.2) (E0SM75)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU367009}.
Interaction partners:
- Pectate lyase C
- Pectate lyase B
- Pectate lyase L
- Pectate lyase D
- Pectate lyase E
- Pectate lyase A
- pectate lyase
- Endoglucanase Z
- Pectate lyase
- Pectate lyase
Sequence:
MFKYVIPLCALTLAAPSFAAQTTLMLSQKSDVNYLGWSTDESKVARQEVYRGTTSNPDLRERIAVLDAETRTFKDADTNSGLNYWYWVDVVSENQAQVVSNAVTTAPNAGPLRAAKASSECKPGATFENRTVDCGGVTIGTSCPNDSDKQKPLIILKNATVKNLRISASGGADGIHCDSGNCTIENVIWEDICEDAATNNGKTMTIVGGIAHNAKDGYGGKPDKVLQHNSKNSTTVVKGNFTLTGEHGKLWRSCGDCSNNGGPRFLTVTSATVNGTIDSIAGVNRNYGDVATISGLKIKNYKEGKPPVCEEFKGVVKGQGSTEKYGEKWDTTNCKVSRSGVSKL
Protein: Uncharacterized protein C23C11.06c (O13912)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
Sequence:
MNTSQDVNAEAANERSALLPRFLGSHRGNVPENTDTYALTPLFYWIRSTSVGLLLITIICHLFLLLNIFISIPIISHLSPGFMPVGFTALAAILLAMQIMFVYSPNAPERVTQRIICFLLAIDVLVVFLSPILRHREGWRSNAFVLWAFLMSLWIVITDLMLFRQYKEEHPDYDAIAHRGYYWSWSPSTWPWRQVGSLTASTILSVILTILTIHTLVTLIMRAYDGALSAPGQLYTVTDSKARVHLECFGSSSSNNKTTVLVEGGEVSVHPFKEWLLNLQHTSPDLYEESKDFEGYENDVKPYLSPDTRVCVWDRPGMGWSDNIGSPSSVGIVMDLLTEALAQADVSGPYVLVAHGIGGVYSNVFAARHLSEVKGIVFVDAGSVQTLKDSGQFLSRFLLFVRGWLSPLGINRIFGSIFMGKTRQDRVYGMYSWTSDRWVKSKIEESLTGPSFSRYELQSAQSVLPKDLPVSVISAGKSMKRFKKWPDEQRQLSKLTQRTVWDIVNNAPHDVWLSDDGGDLIMKRLGEIIYGGWPN
Protein: Teg14 (B7T1D9)
Organism: uncultured soil bacterium
Interaction partners:
Sequence:
MNGIRWIASYPKAGNTWLRCMLAAYITGKAPQTWKDMETVSLELEGMLHLGDMPPTEPTKPVLVKTHLKADVPVLGLYSEATAKVLYLVRNPRDILLSAMRMTAISRDDMESSRTFARDFIANEGLRMRGRGGGAGLGSWPENVRIWTESSRDRFPNADVLTMRYEDLKGDPVARFSEIVEFLDLGDPVDIEDIRRAVAACTLERMRELEKRSQQQGQWASMTGGRGGEKHPFVGEGRYDQSLSFLGEDIESAYQELLHGDSEFAHYAKQYGYAG
Protein: Transmembrane protein 231 (Q9H6L2)
Organism: Homo sapiens (Human)
Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to the transition zone of primary cilia; SEPT2 is required for localization to the transition zone. {ECO:0000250}.
Interaction partners:
- B9 domain-containing protein 1
- B9 domain-containing protein 2
- Tectonic-1
- Coiled-coil and C2 domain-containing protein 2A
- Meckelin
- Tectonic-2
- Transmembrane protein 216
- Tectonic-like complex member MKS1
- Centrosomal protein of 290 kDa
- Transmembrane protein 17
Sequence:
MALYELFSHPVERSYRAGLCSKAALFLLLAAALTYIPPLLVAFRSHGFWLKRSSYEEQPTVRFQHQVLLVALLGPESDGFLAWSTFPAFNRLQGDRLRVPLVSTREEDRNQDGKTDMLHFKLELPLQSTEHVLGVQLILTFSYRLHRMATLVMQSMAFLQSSFPVPGSQLYVNGDLRLQQKQPLSCGGLDARYNISVINGTSPFAYDYDLTHIVAAYQERNVTTVLNDPNPIWLVGRAADAPFVINAIIRYPVEVISYQPGFWEMVKFAWVQYVSILLIFLWVFERIKIFVFQNQVVTTIPVTVTPRGDLCKEHLS
Protein: Cytochrome c-type protein NrfB (P0ABL1)
Organism: Escherichia coli (strain K12)
Function: Plays a role in nitrite reduction.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Protein NrfC
- Cytochrome c-552
- Protein NrfD
- Formate-dependent nitrite reductase complex subunit NrfG
- Probable cytochrome c-type biogenesis protein NrfE
- Formate-dependent nitrite reductase complex subunit NrfF
- Cytochrome c-type protein NapC
- Ferredoxin-type protein NapH
- Nitrite reductase small subunit
- Prophage side tail fiber protein homolog StfR
Sequence:
MSVLRSLLTAGVLASGLLWSLNGITATPAAQASDDRYEVTQQRNPDAACLDCHKPDTEGMHGKHASVINPNNKLPVTCTNCHGQPSPQHREGVKDVMRFNEPMYKVGEQNSVCMSCHLPEQLQKAFWPHDVHVTKVACASCHSLHPQQDTMQTLSDKGRIKICVDCHSDQRTNPNFNPASVPLLKEQP
Protein: Eukaryotic translation initiation factor 4E-1 (PeaeIF4E) (eIF-4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (K0P2S0)
Organism: Arachis hypogaea (Peanut)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as peanut stripe virus (PStV).
Subcellular location: Nucleus {ECO:0000269|PubMed:28344571}. Cytoplasm {ECO:0000269|PubMed:28344571}.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- MI domain-containing protein
- MI domain-containing protein
- RNA helicase
- Polyadenylate-binding protein
Sequence:
MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI
Protein: ATP synthase subunit c (ATP synthase F(0) sector subunit c) (Dicyclohexylcarbodiimide-binding protein) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) (P68699)
Organism: Escherichia coli (strain K12)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit a
- ATP synthase epsilon chain
- ATP synthase subunit b
- ATP synthase subunit delta
- ATP synthase gamma chain
- ATP synthase protein I
- Membrane protein insertase YidC
- Inorganic pyrophosphatase
Sequence:
MENLNMDLLYMAAAVMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA
Protein: Uncharacterized protein C16E9.15 (O14330)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein alpha-1 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
- Enhancer of rudimentary homolog 1
- Heat shock factor protein
- Transcription factor prr1
Sequence:
MSASVRGNSKNPQSTSAITTLTDKLLEDISGDFETLQKQFSEKLETMSTRLDQLEESMREAMNKKSSVSPVTSTE
Protein: Synapsin-2 (Synapsin II) (Q63537)
Organism: Rattus norvegicus (Rat)
Function: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons (By similarity).
Subcellular location: Synapse.
Interaction partners:
- Synaptotagmin-1
- Syntaxin-1A
- Vesicle-associated membrane protein 2
- Multifunctional fusion protein
- Syntaxin-binding protein 1
- Disks large homolog 4
- Ras-related protein Rab-3A
- Complexin-1
- Regulating synaptic membrane exocytosis protein 1
- Synaptophysin
Sequence:
MMNFLRRRLSDSSFIANLPNGYMTDLQRPEPQQPPPAPGPGTATASAATSAASPGPERRPPPAQAPAPQPAPQPAPTPSVGSSFFSSLSQAVKQTAASAGLVDAPAPSAASRKAKVLLVVDEPHTDWAKCFRGKKILGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFGMAENEDFRHLVIGMQYAGLPSINSLESIYNFCDKPWVFAQMVAIFKTLGGEKFPLIEQTYYPNHREMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDAKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDACSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITDLVISKMNQLLSRTPALSPQRPLTTQQPQSGTLKEPDSSKTPPQRPAPQGGPGQPQGMQPPGKVLPPRRLPSGPSLPPSSSSSSSSSSSSSAPQRPGGPTSTQVNASSSSNSLAEPQAPQAAPPQKPQPHPQLNKSQSLTNAFSFSESSFFRSSANEDEAKAETIRSLRKSFASLFSD
Protein: Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-II); Copeptin] (P01185)
Organism: Homo sapiens (Human)
Function: Specifically binds vasopressin.
Subcellular location: Secreted.
Interaction partners:
- Vasopressin V1a receptor
- Vasopressin V2 receptor
- Vasopressin V1b receptor
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 1A
- Oxytocin-neurophysin 1
- Alcohol dehydrogenase 1C
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 6
Sequence:
MPDTMLPACFLGLLAFSSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAAFGVCCNDESCVTEPECREGFHRRARASDRSNATQLDGPAGALLLRLVQLAGAPEPFEPAQPDAY
Protein: Succinate dehydrogenase assembly factor 4, mitochondrial (SDH assembly factor 4) (SDHAF4) (Found in mitochondrial proteome protein 21) (P38345)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit SDH1 in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit SDH2 into the SDH catalytic dimer.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:24954416}.
Interaction partners:
- Uncharacterized protein YER034W
- UPF0743 protein YCR087C-A
Sequence:
MLCAIKSTGYRYPRTGALNLLRGRPFNMATRKITTERIPGPPKLPREEQEEFERLQRIATSQEAIDQYNAQATGDRTKESLNSPLLTKNDIGSFSPEFSKTIPEFEGDVNPKTGEVGGPKQDPLRHGDYSFNGRVTDF
Protein: EtpA (Q29XT7)
Organism: Escherichia coli
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MNRIYKLKFDKRRNELVVVSEITTGVGNAKATGSVEGEKSPRRGVRAMALSLLSGMMIMAHPAMSANLPTGGQIVAGSGSIQTPSGNQMNIHQNSQNMVANWNSFDIGKGNTVQFDQPSSSAVALNRVVGGGESQIMGNLKANGQVFLVNPNGVLFGEGASVSTSGFVASTRDIKNDDFMNRRYTFSGGQKAGAAIVNQGELTTNAGGYIVLAADRVSNSGTIRTPGGKTVLAASERITLQLDNGGLMSVQVTGDVVNALVENRGLVSARDGQVYLTALGRGMLMNTVLNVSGVVEASGMHRQDGNIVLDGGDSGVVHLSGTLQADNASGQGGKVVVQGKNILLDKGSNITATGGQGGGEVYVGGGWQGKDSNIRNADKVVMQGGARIDVSATQQGNGGTAVLWSDSYTNFHGQISAKGGETGGNGGRVETSSHGNLQAFGTVSASAKKGKAGNWLLDSADITIVNGSNVSKTETTQSPPHTQFAPTAAGSAVSNTSINNRLNNGTSVTILTHRTRTGTAQGGNITVNAAINKSNGSDVNLTLQAGGNITVNNSITSTEGKLNVNLSGARTSNGSITISNNANITTNGGDITVGTTNTSNRVNISINNTTLNASNGNIQLTGTGTDSGILFAGNNRLTASNIALTGNSTSGNAINLTGTATLNATNNITLTGSSTSGNAINLKGNNTLTASNITLTGESTSGNAINLTDTTGTTTLNATNNITMQGTRVQIKHSNITAGNFALNATVAGSEISNTTLTATNNINLAAKTNSASSGVYLKDARITSTNGSITANGTATANGKATHLDGNVTLNASNGRIKLTGNGHGSASGILFAGNNRLTASNIALTGNSTSGNAINLTGTATLNATNDITLTGSSTSGNAINLTGTATLNATNNITLTGSSTSGNAINLKGNNTLTASNITLTGESTSGNAINLTDTTGTTTLNATNNITMQGTRVQIKHSNITAGNFALNATVAGSEISNTTLTATNNINLAAKTNSASSGVYLKDARITSTNGSITANGTATANGKATHLDGNVTLNASNGRIKLTGNGHGSASGILFAGNNRLTASNIALTGNSTSGNAINLTGTATLNATNDITLTGSSTSGNAINLTGTATLNATNNITLTGSSTSGNAINLKGNNTLTASNITLTGESTSGNAINLTDTTGTTTLNATNNITMQGTRVQIKHSNITAGNFALNATVAGSEISNTTLTATNNINLAAKTNSASSGVYLKDARITSTNGSITANGTATANGKATHLDGNVTLNASNGRIKLTGNGHGSASGILFAGNNRLTASNIALTGNSTSGNAINLTGTATLNATNDITLTGSSTSGNAINLTGTATLNATNNITLTGSSTSGNAINLKGNNTLTASNITLTGESTSGNAINLTDTTGTTTLNATNNITMQGTRVQIKHSNITAGNFALNATVAGSEISNTTLTATNNINLAAKTNSASSGVYLKDARITSTNGSITTNGTATANGKATHLDGNVTLNASNGRIKLTGNGHGSASGILFAGNNRLTASNIALTGNSTSGNAINLTGTATLNATNDITLTGSSTSGNAINLTGTATLNATNNITLTGSSTSGNAINLKGNNTLTASNITLTGESTSGNAINLTDTTGTTTLNATNNITMQGTRVQIKHSNITAGNFALNATVAGSEISNTTLTATNNINLAAKTNSASSGVYLKDARITSTNGSITANGTAPANDNATYLDGNVTLNASNGSIKLTGNGNGSTSGILFAGNNTLTASNITLTGNSEVYWQ
Protein: 2-methylcitrate synthase, mitochondrial (Methylcitrate synthase) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase 2) (EC 2.3.3.16) (Q9TEM3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate and also from acetyl-CoA and oxaloacetate with a greater efficiency. Also has citrate synthase activity and can substitute for the loss of citA activity.
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- ATP citrate synthase
- ATP citrate synthase
- Aconitate hydratase, mitochondrial
- Pyruvate carboxylase
- Malate dehydrogenase
- malate dehydrogenase
- malate dehydrogenase
- Acetyltransferase component of pyruvate dehydrogenase complex
- Acetyl-coenzyme A synthetase
Sequence:
MALPLRTARHASRLAQTIGRRGYATAEPDLKSALKAVIPAKRELLAEVKKQGDEVIGEVKVSNVIGGMRGLKSMLWEGSVLDADEGIRFHGKTIKDCQKELPKGPTGTEMLPEAMFWLLLTGEVPSTSQVRAFSKQLAEESHLPDHILDLAKSFPKHMHPMTQISIITAALNTESKFAKLYEKGINKADYWEPTFDDAISLLAKIPRVAALVFRPNEIDVVGRQKLDPAQDWSYNFAELLGKGGANNADFHDLLRLYLALHGDHEGGNVSAHATHLVGSALSDPFLSYSAGLLGLAGPLHGLAAQEVLRWILAMQEKIGTKFTDEDVRAYLWDTLKSGRVVPGYGHGVLRKPDPRFQALMDFAATRKDVLANPVFQLVKKNSEIAPGVLTEHGKTKNPHPNVDAASGVLFYHYGFQQPLYYTVTFGVSRALGPLVQLIWDRALGLPIERPKSINLLGLKK
Protein: Cytohesin-1b (Zgc:73134) (Q6PC26)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MVLKSDDEIVPHDLTPEEKQELENIRRRKQELLEDIQRLKDEITKVTNEIECLGSTQERINMQRSKQMAMGRKKFNMDPKKGIQFLIENELLKNTCEDIAQFLYKGEGLNKTAIGDYLGERDEFNIQVLHAFVELHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCQCNPGVFQSTDTCYVLSFAIIMLNTSLHNPNVKDKPSAERFICMNRGINDGGDLPEDLLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDSKKPNCFELFIPDNKDQVIKACKTEADGRVVEGNHTFYRISAPTTEEKEDWIKSIKSAISRDPFYEMLAARKKKASSLKRQ
Protein: Protein STE5 (P32917)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.
Subcellular location: Cytoplasm.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Serine/threonine-protein kinase STE11
- Serine/threonine-protein kinase STE7
- Mitogen-activated protein kinase FUS3
- Guanine nucleotide-binding protein subunit beta
- Mitogen-activated protein kinase KSS1
- Serine/threonine-protein kinase STE20
- Pheromone alpha factor receptor
- Bud emergence protein 1
- Guanine nucleotide-binding protein alpha-1 subunit
Sequence:
MMETPTDNIVSPFHNFGSSTQYSGTLSRTPNQIIELEKPSTLSPLSRGKKWTEKLARFQRSSAKKKRFSPSPISSSTFSFSPKSRVTSSNSSGNEDGNLMNTPSTVSTDYLPQHPHRTSSLPRPNSNLFHASNSNLSRANEPPRAENLSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQCIPENDELKDILISDFLIHKIPDSELSITPQSRFPPYSPLLPPFGLSYTPVERQTIYSQAPSLNPNLILAAPPKERNQIPQKKSNYTFLHSPLGHRRIPSGANSILADTSVALSANDSISAVSNSVRAKDDETKTTLPLLRSYFIQILLNNFQEELQDWRIDGDYGLLRLVDKLMISKDGQRYIQCWCFLFEDAFVIAEVDNDVDVLEIRLKNLEVFTPIANLRMTTLEASVLKCTLNKQHCADLSDLYIVQNINSDESTTVQKWISGILNQDFVFNEDNITSTLPILPIIKNFSKDVGNGRHETSTFLGLINPNKVVEVGNVHDNDTVIIRRGFTLNSGECSRQSTVDSIQSVLTTISSILSLKREKPDNLAIILQIDFTKLKEEDSLIVVYNSLKALTIKFARLQFCFVDRNNYVLDYGSVLHKIDSLDSISNLKSKSSSTQFSPIWLKNTLYPENIHEHLGIVAVSNSNMEAKKSILFQDYRCFTSFGRRRPNELKIKVGYLNVDYSDKIDELVEASSWTFVLETLCYSFGLSFDEHDDDDEEDNDDSTDNELDNSSGSLSDAESTTTIHIDSPFDNENATANMVNDRNLLTEGEHSNIENLETVASSVQPALIPNIRFSLHSEEEGTNENENENDMPVLLLSDMDKGIDGITRRSSFSSLIESGNNNCPLHMDYI
Protein: Programmed cell death 1 ligand 1 (PD-L1) (PDCD1 ligand 1) (Programmed death ligand 1) (hPD-L1) (B7 homolog 1) (B7-H1) (CD antigen CD274) (Q9NZQ7)
Organism: Homo sapiens (Human)
Function: Plays a critical role in induction and maintenance of immune tolerance to self. As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response. Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:36232715}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:28813417}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:28813417}; Single-pass type I membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:32929201}. Note=Associates with CMTM6 at recycling endosomes, where it is protected from being targeted for lysosomal degradation (PubMed:28813417). Translocates to the nucleus in response to hypoxia via its interaction with phosphorylated STAT3 (PubMed:32929201). {ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:32929201}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Endomembrane system {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:30564891}.
Interaction partners:
- T-lymphocyte activation antigen CD80
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death protein 1
- Hepatitis A virus cellular receptor 2
- T-cell-specific surface glycoprotein CD28
- Programmed cell death 1 ligand 2
- Inducible T-cell costimulator
- Signal transducer and activator of transcription 3
- Lymphocyte activation gene 3 protein
- T-cell immunoreceptor with Ig and ITIM domains
Sequence:
MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET
Protein: Enkurin domain-containing protein (Q583F4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIGGAVLNPHKPATEKPSTETPQRPSRLPTAAAAQHDKKYHHCDCYGHPLGLPNYKVLAQPRTNNYYNATGGCPCIPRSAAHPGSWRNKREQLRSTANHFPFGCTKKRPGTTCCVHAGETYGWLPGPHKVLAKNCAASGLCDTFGNMAFKKPIRSQDKDSDVSSVTTQKLAKLEELILREHGERRRIEMDVDELEDIKKRGAENDYKVDYENEKKRKQAMAASEGQLKELLREVRGIVNRPLNQTNIDILRGIVDRQEQFMQLRSLRAHEDFPPIIHP
Protein: CARD-like apoptotic protein (V-CARMEN) (Q9YJN5)
Organism: Equid gammaherpesvirus 2 (Equine herpesvirus 2)
Interaction partners:
Sequence:
MAEKYPLQAGDPCVTLTEEDIWDVERLCLEELRVLLVSHLKSHKHLDHLRAKKILSREDAEEVSSRATSRSRAGLLVDMCQDHPRGFQCLKESCKNEVGQEHLVDLLERAFEKHCGDKLTQKWWESGADGRNPRRPPGSEDNSGYTALLPTNPSGGGPSIGSGHSRPRGRDDSGGIGGGVYPFSHGGARVVGGGWGGWGESGGAGRGGSLLSGGHGGHPPHGGPGGGGRDYYGGGGSGYYESIPEPANFPNSGGGGRGGGVRYDAGGDGRLGGLPPDPQEVDDPSLSVQGRGGPAPDPPSPPLRTRRFFCC
Protein: VAMP (vesicle-associated membrane protein)-associated protein B and C (Vapb protein) (Vesicle-associated membrane protein, associated protein B and C) (Vesicle-associated membrane protein-associated protein B/C) (Q6P2B0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
- StAR-related lipid transfer protein 3
- TAR DNA-binding protein 43
- Acyl-CoA-binding domain-containing 4.
- Alsin Rho guanine nucleotide exchange factor ALS2 a.
- Transitional endoplasmic reticulum ATPase
- Oxysterol-binding protein
- Senataxin.
- Sigma non-opioid intracellular receptor 1
- Novel protein similar to vertebrate caldesmon 1
- Guanine nucleotide exchange C9orf72 homolog
Sequence:
MARPEQVLLLEPQHELRFRGPFTDVVTTTLKLANPTDRNVCFKVKTTAPRRYCVRPNSGVIDAGTSINVSVMLQPFDYDPNEKSKHKFMVQSLLAPPDMTDTEGVWKDAKPEDLMDSKLRCVFDMPAENEKTHEMESNKISSLSKSESSTLSMKSMASSMDDGEVKKIMEECKRLQTEVQRLREENKQIRQEDDGLRMRKSTVMSAPHSSLAVRVKEEGLSSRVIALIVLFFVVGVIVGKLAL
Protein: Chromosome 11 open reading frame 54 (E9PQS1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAGPFQTLGFNSEFMPVIQTESEHKPPVNGSYFAHVNPADGGCLLEKYSEKCHDFQCALLANLFASEGQPGKVIEVKAKRRTGPLNFVTCMRETLEKHYGNKPIGMGGTFIIQKGKVKSHIMPAEFSSCPLNSDEEVNKWLHFYEMKAPLVCLPVFVSRDP
Protein: Proline-rich antimicrobial peptide 1 (P85214)
Organism: Galleria mellonella (Greater wax moth)
Function: Antimicrobial protein. Has antibacterial activity against the Gram-positive bacterium M.luteus (MIC=55.0 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, and L.monocytogenes, and the Gram-negative bacteria E.coli D31 and E.coli ATCC 25922. Has antifungal activity against P.pastoris (MIC=16.5 uM), Z.marxianus (MIC=16.5 uM), S.pombe (MIC=11.0 uM), and C.wickerhami (MIC=16.5 uM), but lacks antifungal activity against A.niger and C.albidus.
Subcellular location: Secreted {ECO:0000269|PubMed:11995991, ECO:0000269|PubMed:17194500}.
Interaction partners:
Sequence:
DIQIPGIKKPTHRDIIIPNWNPNVRTQPWQRFGGNKS
Protein: Glycosomal membrane protein (O60944)
Organism: Trypanosoma brucei
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
Sequence:
MSEFQRFVKLLEQTDGRDKILKAFSGVFKALGSLDTCQSRSSAFGAVGKSIGDARCLLRMAKWVGDVPKMQNAIQDCRAKGKVNMKEVLKFLRVLCNFLYVLGDNVAFVARYNLLALRHKSIHLKAKTAQFWGFFLAAVLDVVALYGALQKRASDPATSKKEMKAALISFVKDASDTLVTMAFVGYLREVWRPSATTSGALTAVAGGVATYLNWNKIK