wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 2 subunit gamma (eIF2-gamma) (EC 3.6.5.3) (Q09130)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- Probable eukaryotic translation initiation factor 2 subunit beta
- Probable eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit G
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MAENLDISELSPIHPAIISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKCSNEECPRPGCYRSYSSNKEDHPPCEICNSPMNLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMQLKHIIILQNKVDLIRESAAEEHYQSILKFIKGTVAENSPIVPISAQLKYNIDAILEYIVKKIPIPVRDFTTAPRLIVIRSFDVNKPGAEVDDLKGGVAGGSILTGVLRLNDEIEIRPGIVTKDDDGRIRCQPIFSRIISLFAEHNDLKIAVPGGLIGVGTTVDPTLCRADRLVGQVLGSKGNLPEVYTELEINYFLLRRLLGVKSGDKNTTKVQKLAKNEVLMVNIGSTSTGGRVMMVKADMAKILLTAPACTEIGEKVALSRRIEKHWRLIGWAKVVEGKTLKV
Protein: Nuclear pore complex protein Nup85 (Q22078)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
- Nucleoporin SEH1
- Nsp1_C domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- Nuclear pore complex protein 5
- Nuclear pore complex protein 15
- Protein SEC13 homolog
- Nuclear Pore complex Protein
- Nuclear pore complex protein Nup98-Nup96
- Nuclear Pore complex Protein
- Nuclear pore protein
Sequence:
MTDVAREFGIAVSDSSTVFAFLTDKKGFSNKETVLVEKVSQNRQILATPNLRRLVIEMYSVFDKCQKGSSPDAPLDTPTCCTFSRAYRSVLYNAAVSHSSSDFMTDFALWSLYEKLWFGRGDSSICADLISWANQSFTFSRGAMESAVEYLHPGKTIPEEYWKGVAVSLLSCNFSDCVELLELHGGGSECDAFIEALTFFNPENLVDEALANTVNEWKDIMRENLTSGKYGSNENFKYLTKLLLGEERYLVSMASRIFDTWWHFLPFFVLVKNPFAGHVELIELADECRTLFVGEEEEEGAKENDVFWCLISKDDINFQQLIASNPWLAVHLVDLIHKSTLDPEFEVMRKMHMLDYASVLISHSPLWEIGAGYLIACGTEGLLRLETHIEGLHIEDDEMAEQLLEICEEHRLEDAKSCVTNTMTFRYLKQGHWSSTLAWALKTGSKKTIDWTVSRIVGSSSKDELAALRVLSSITNHSVLSLPSLTFLYSYQRFVKMMHCGDVLDCVQHLIPLIMMPDVPTQYYYDLFDYLITIIKEDGRAGIRFSKEILYELSTFLSTFTLDKHRDLNDNYMKKVKVLKKMVMLKLTDSIAKGIACS
Protein: N-acetyltransferase eco (EC 2.3.1.-) (Establishment of cohesion 1 homolog) (ECO1 homolog) (Q9VS50)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Precocious dissociation of sisters 5, isoform A
- FI11703p
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein 5
- Chromosomal protein D1
- histone acetyltransferase
- SD25546p
Sequence:
METPTGSGRPSRMATPRLSERKRQLFGSPRSRLRQINDDEDDADVDSLGVLPLKTHVAANRKGRSLFAAVPGKSSSSANSSPETNKENKKTRGGVMTATAEQLPQLFTATMRLNSNSSSNSRNSSPRQTRVQRKRADSSMSSPTSSSEGTPSSRARNSIRRSPRTFSAQKDPDAFSSPESFQTRLSKVAAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKTSPAEESQSDDEKPSSSKNSRKNTEVRETRSSQIISPKTRNRRRPFTSADINCKTLKAAAHLHENMRSYDEEKTAAVKLENSRSRSKSPVEVFKSNDDAVKRNTGNTNNKTAKSSEVATAKRPESPGSSMKIDVEVPESDEEASNHKPQKRQHPETSTPVAPSADADSGSPQSKMRKVTLSSSIPTMAFYSHSGEAVTKSRRRPSISKNSLKQPTKISPTSRPLLGINKGVHHKIRKRHGFANRLPATDMDNILNSLSNERLKNLITTKREERAKVEEVHQILRNAKDPIKMAKPLSVIEADDANNNNNLPATAWQETSADFSDLSDVEDIDPIIEVEPIIPIIRHEPVQKSPTAEPADLSKRKFFKSGRRSSTCMEVRITDNIRASVSQGKIELVQTIRRKPRQVRVKSATIFSAEQATVDAILKNLDDTVVDEIVEANPVVQATPIDAEETTMETESLPDIIEYAPEANDVEIDPFAEFRQRLPYQTDDPNVVEQQQILLEFLISNNICTEKNFEIFIANPDDYKDEANQIVDNLYMVVNSEEAAQLAQMETVENTAVAIAPKQDAPAVEEVQPKLFPIFTQRLQPVVQKSLRRRPDTSMRLLTAAGGSNQYQIDAGQKAFGARQCQQCGLVYTVHEPEEELLHREYHNSIHVLRFKGWIDEDIVSVYPEWASDGRIIRINERAPTARLDRLRDLIGVVDKELGYSSYIVPKIFVAFIAVRKQQIVGFCLVQPLSQAHRFIQVDGTDYFSEESYPASCGVSRIWVSPLQRRSGIASKLLRVVQCHTVLGQEIARECIAFSTPTDDGRALARQFTGLDNFLTYDQ
Protein: Catalase (EC 1.11.1.6) (P77872)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Catalase-related peroxidase
- Glycolate oxidase subunit
- Tat pathway signal protein
- Isocitrate dehydrogenase
- Peptide methionine sulfoxide reductase MsrA/MsrB
- Alkyl hydroperoxide reductase C
Sequence:
MVNKDVKQTTAFGAPVWDDNNVITAGPRGPVLLQSTWFLEKLAAFDRERIPERVVHAKGSGAYGTFTVTKDITKYTKAKIFSKVGKKTECFFRFSTVAGERGSADAVRDPRGFAMKYYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHTQKRDPQTNLPNHDMVWDFWSNVPESLYQVTWVMSDRGIPKSFRHMDGFGSHTFSLINAKGERFWVKFHFHTMQGVKHLTNEEAAEVRKYDPDSNQRDLFNAIARGDFPKWKLSIQVMPEEDAKKYRFHPFDVTKIWYLQDYPLMEVGIVELNKNPENYFAEVEQAAFSPANVVPGIGYSPDRMLQGRLFSYGDTHRYRLGVNYPQIPVNKPRCPFHSSSRDGYMQNGYYGSLQNYTPSSLPGYKEDKSARDPKFNLAHIEKEFEVWNWDYRADDSDYYTQPGDYYRSLPADEKERLHDTIGESLAHVTHKEIVDKQLEHFKKADPKYAEGVKKALEKHQKMMKDMHGKDMHHTKKKK
Protein: Bifunctional arginine demethylase and lysyl-hydroxylase PSR (EC 1.14.11.-) (Phosphatidylserine receptor) (Q6Q4H1)
Organism: Hydra vulgaris (Hydra) (Hydra attenuata)
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Subcellular location: Nucleus {ECO:0000269|PubMed:15193161}.
Interaction partners:
Sequence:
MDKRTDDAVRETKLKARPELKGDEGWTRLGYANNFDLSYQHIKDTLPRIHCKSISHDEFIARYEKPRIPVILTGCTDSWLANQKWKLSSLAKKYRNQKFKVGEDNDGFSVKMKMKYYIEYLKHQKDDSPLYIFDGSYGEHPKKRKLLDDYHPPSFFQDDLFKYAGEKRRPPYRWIVIGPARSGTGIHIDPLGTSAWNALISGHKRWMMFPTETPKHLLEVSKQDGQHQSGEGIQWFVKVYPKVKSPTWPKEYAPLEIIQHPGETVFVPGGWWHVVLNLDQTVAVTQNFSSPTNFHVVWHKTVRGRPKLSQKWLRALKIYRPEIARIAAEVDLLRQSGLASDSSSDSSSSSSSSSSEESNSESEESTADSIPEQSESKRRKVDAVE
Protein: Lectin-C (PL-C) (Q9AYP9)
Organism: Phytolacca americana (American pokeweed) (Phytolacca decandra)
Function: N-acetyl-D-glucosamine binding lectin. Almost no hemagglutinating activity towards human erythrocytes. Low mitogenic activity towards human peripheral blood lymphocytes.
Interaction partners:
Sequence:
MKRSNSIAVMLVLVLSSLMLLLPVEGQGHEGHGVGEILLMGKLGAPVCGVRASGRVCPDGYCCSQWGYCGTTEEYCGKGCQSQCDYNRCGKEFGGKECHDELCCSQYGWCGNSDGHCGEGCQSQCSYWRCGKDFGGRLCTEDMCCSQYGWCGLTDDHCEDGCQSQCDLPTLLPSPLRRIIAIRKLKANLANMLS
Protein: FXYD domain-containing ion transport regulator 11 (C0HJJ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May modulate the activity of a sodium/potassium-transporting ATPase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21423371}; Single-pass type I membrane protein {ECO:0000269|PubMed:21423371}.
Interaction partners:
- FXYD domain-containing ion transport regulator
- FXYD domain-containing ion transport regulator
- Large ribosomal subunit protein uL6
- Cleavage and polyadenylation-specific factor 4.
- Forkhead box I3a.
- FXYD domain-containing ion transport regulator
Sequence:
MSQLTELVLLTVFLALFSRAEANPFVYNYEALRIGGLVFTCVLVAGAVTALCWGQCKPKRKHDDDASKI
Protein: Cell division protein FtsA (A0A1D3IEB2)
Organism: Neisseria gonorrhoeae
Subcellular location: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-Rule:MF_02033}.
Interaction partners:
Sequence:
MEQQKRYISVLDIGTSKVLALIGEVQDDDKINIIGLGQAPSRGLRAGMVTNIDATVQAIRQAVNDAELMADTKITHVTTGIAGNHIRSLNSQGVVKIKDGEVTQADIDRAIETAKAINIPPDQKILDAVVQDYIIDTQLGVREPIGMSGVRLDTRVHIITGASTAVQNVQKCIELCGLKSDQIMLQPLASGQAVLTEDEKDLGVCVIDIGGGTTDIAVYMNGAIRHTSVIPAGGNLITKDLSKSLRTPLDAAEYIKIHYGVASCDTEGLGEMIEVPGVGDRTSRQVSSKVLAAIISARIQEIFGVVLGELQKSGFPKEVLNAGIVLTGGVSMMTGIVEFAEKIFDLPVRTGAPQEMGGLSDRVRTPRFSTAIGLLHAACKLEGNLPQPENGTVQEREGGGGLLARLKRWIENNL
Protein: Inactive CLIP domain-containing serine protease A28 [Cleaved into: Inactive CLIP domain-containing serine protease A28 light chain; Inactive CLIP domain-containing serine protease A28 heavy chain] (A0A1S4H5M5)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Inactive serine protease which plays an essential role in the innate immune response against bacteria, fungi and protozoa infection by activating the melanization cascade. In the melanization cascade, acts downstream of TEP1, SPCLIP1 and CLIPA8 to promote CLIPC9 proteolytic cleavage. In the susceptible strain G3, appears to be dispensable for parasite P.berghei ookinete elimination which occurs by lysis. Required for the melanization of Gram-positive and Gram-negative bacteria. Required for the melanization of fungus B.bassiana.
Subcellular location: Secreted {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:31765430, ECO:0000269|PubMed:33045027}.
Interaction partners:
Sequence:
MKVLLFCIVISLTTLIASGQDIEEELRCPGGYCVSKYLCPNGTFIDDIKHAQTTQLIGLRAGLDIDDFDDCNDYLLVCCQSAPAPTATSTEKPATSDELIEPPPSTNLACGQANEGGLIYDLRNNETLSQYAEYPWVVYILALKKQEANSGDFVCGGTLIHSRLVVTTAHNTDGKTDLVARFGEWDISTTKEPFPQQDIDVAEVIKHPQYVFNPIQNDIALLVLAENVQYAAHIRPICLPQPTDEFVGQRCVSNGWGKERGVYANVMKKLTLPVIGRANCTRMLRYAGLGPFYTLREGFLCAGGEVAVDMCKGDGGSPLACQTESGTYVLAGIVSWGIGCGGFNTPGVYVAVNRYVQWLNEHIVDQALNESFDIKL
Protein: Arachidonate 12-lipoxygenase (EC 1.13.11.31) (Q7T2A9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cytosolic phospholipase A2
- Zgc:101699.
- Si:ch73-55i23.1
- Si:ch73-55i23.1.
- Arachidonate 5-lipoxygenase a
- Group XIIB secretory phospholipase A2-like protein
- Prostaglandin-endoperoxide synthase 2a.
- Prostaglandin-endoperoxide synthase 1.
- Prostaglandin G/H synthase 2
- Phospholipase A2
Sequence:
MEYKVTVATGTSEYSGTNNYVYVTLIGEKGKSERTLLDNPGLDFCRGAVDDYIVKSDTDLGPLILVRLEKHKYFIEDNWFCRYVKVSVPGERCCYTFPCYRWLVGDGVFVELREGTAKKLSEDSLPLEMAHRQSELQERQKTYRWVAWAPGIPKCIDAKSEADLPQDARFDNEKRSDFEGSLHYALLELSLKKLAIRFGKSWSDLEDFRRIFWKLRSPIAEYTMEHWKEDWFFAYQFLNGSNPRNITRLKKVPSNFLVTGDMVQSSLIPTTTLNEELKKGNIFLVDHAILDGIPANVIRNSPQYIAAPLCLLYEHPEKGLIPIAIQLEQKPDKDTPVFLPSDPPLAWLLAKMWVRHAEFQVFQLLSHLLRTHLMVEVICVATLRQLPAVHPIYKLLTPHLRYTLEINCRGRTQLLSPEGIFKRVVSTGGEGLLILAQREYKVLTYRSLQPKFDFLDRGVTKVKGYVYRDYSLMLWDVIQNFVSGIVSLYYQCDSDVQEDSELQAWIHDVAVEGFVDVPEFGLASDMKTKEELITLLSVAIFTSTAQHAATNNGQFDWCAWVPNTPCTMRHPPPRDKDAVTMEMIMDTLPDISQSCVQMAITWHLGRAQPDAIPMGQYVEQYFTEPAALKVIDKFRKELKELEDKIMAQNEGLELQYLYLCPSRMENSITI
Protein: Glutamine sensor pib2 (Q9Y7M3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as an intracellular glutamine sensor that directly activates the TORC1 signaling pathway, to promote cell growth when glutamine is available.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding protein gtr1
- GTP-binding protein gtr2
- Nitrogen permease regulator 2 homolog
Sequence:
MTTVHQLSGHGPLSRLNIYSGASPYTQRVRPSYELIEAPTRQATNGTGSVSGSPNSSSNSTPANQGSLPSHTNPQLYSSITRKERPELFRSYSGNPRLSKPYASSKLAASSRTASYQAMSYSVSPTSTNSSVATSLNYQSSRETGISKDHWKPDSDVSVCSFPSCSVRFGLFDRRHHCRRCGDIFCALHCDRNIPLTMDVKFCLAGSLYRSCVSCFYEYLKWKQSIDLASSNDITVIESTIAPQQATTHPPSQPKNAVSVPIPKMDSTDSKGELPSESLVLGTVPDNWVWSTF
Protein: Histone H1 [Cleaved into: Oncorhyncin II] (P06350)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
Subcellular location: Nucleus. Chromosome.; SUBCELLULAR LOCATION: [Oncorhyncin II]: Secreted.
Interaction partners:
Sequence:
MAEVAPAPAAAAPAKAPKKKAAAKPKKAGPSVGELIVKAVSASKERSGVSLAALKKSLAAGGYDVEKNNSRVKIAVKSLVTKGTLVQTKGTGASGSFKLNKKAVEAKKPAKKAAAPKAKKVAAKKPAAAKKPKKVAAKKAVAAKKSPKKAKKPATPKKAAKSPKKVKKPAAAAKKAAKSPKKATKAAKPKAAKPKAAKAKKAAPKKK
Protein: Protein-glutamine gamma-glutamyltransferase 4 (EC 2.3.2.13) (Fibrinoligase) (Prostate transglutaminase) (Prostate-specific transglutaminase) (Transglutaminase P) (TG(P)) (TGP) (TGase P) (Transglutaminase-4) (TGase-4) (P49221)
Organism: Homo sapiens (Human)
Function: Associated with the mammalian reproductive process. Catalyzes the cross-linking of proteins and the conjugation of polyamines to specific proteins in the seminal tract.
Interaction partners:
- Prostatic acid phosphatase
- Kallikrein-2
- Beta-microseminoprotein
- Plasma kallikrein
- Prostate-specific antigen
- Metalloreductase STEAP2
Sequence:
MMDASKELQVLHIDFLNQDNAVSHHTWEFQTSSPVFRRGQVFHLRLVLNQPLQSYHQLKLEFSTGPNPSIAKHTLVVLDPRTPSDHYNWQATLQNESGKEVTVAVTSSPNAILGKYQLNVKTGNHILKSEENILYLLFNPWCKEDMVFMPDEDERKEYILNDTGCHYVGAARSIKCKPWNFGQFEKNVLDCCISLLTESSLKPTDRRDPVLVCRAMCAMMSFEKGQGVLIGNWTGDYEGGTAPYKWTGSAPILQQYYNTKQAVCFGQCWVFAGILTTVLRALGIPARSVTGFDSAHDTERNLTVDTYVNENGEKITSMTHDSVWNFHVWTDAWMKRPDLPKGYDGWQAVDATPQERSQGVFCCGPSPLTAIRKGDIFIVYDTRFVFSEVNGDRLIWLVKMVNGQEELHVISMETTSIGKNISTKAVGQDRRRDITYEYKYPEGSSEERQVMDHAFLLLSSEREHRRPVKENFLHMSVQSDDVLLGNSVNFTVILKRKTAALQNVNILGSFELQLYTGKKMAKLCDLNKTSQIQGQVSEVTLTLDSKTYINSLAILDDEPVIRGFIIAEIVESKEIMASEVFTSFQYPEFSIELPNTGRIGQLLVCNCIFKNTLAIPLTDVKFSLESLGISSLQTSDHGTVQPGETIQSQIKCTPIKTGPKKFIVKLSSKQVKEINAQKIVLITK
Protein: NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NKG2-D-activating NK receptor) (CD antigen CD314) (O54709)
Organism: Mus musculus (Mouse)
Function: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}; Single-pass type II membrane protein {ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:15294961}. Note=Colocalized with HCST and TYROBP on the cell surface.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Hematopoietic cell signal transducer
- Retinoic acid early-inducible protein 1-delta
- UL16 binding protein 1
- MHC class I-like protein MILL2
- Retinoic acid early-inducible protein 1-epsilon
- mRNA export factor
- Natural cytotoxicity triggering receptor 1
- Nectin-2
- Perforin-1
Sequence:
MALIRDRKSHHSEMSKCHNYDLKPAKWDTSQEQQKQRLALTTSQPGENGIIRGRYPIEKLKISPMFVVRVLAIALAIRFTLNTLMWLAIFKETFQPVLCNKEVPVSSREGYCGPCPNNWICHRNNCYQFFNEEKTWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQIPANGSWQWEDGSSLSYNQLTLVEIPKGSCAVYGSSFKAYTEDCANLNTYICMKRAV
Protein: La ribonucleoprotein 4B (A0A087X183)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
RKNSFGYRKKREEKFTSSQTQSPTPPKPPSPSFELGLSSFPPLPGAAGNLKTEDLFENRLSSLIIGPSKERTLSADASVNTLPVVVSREPSVPASCAVSATYERSPSPAHLPDDPKVAEKQRETHSVDRLPSALTATACKSVQVNGAATHCPGKN
Protein: Asparagine synthetase [glutamine-hydrolyzing] 2 (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase 2) (P49090)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Asparagine synthetase 1
- Aspartate aminotransferase, cytoplasmic
- Argininosuccinate synthase
- Aspartate aminotransferase, mitochondrial
- L-asparaginase 1
- Multifunctional protein URA2
- Adenylosuccinate synthetase
- L-asparaginase 2-1
- CTP synthase 1
- Aspartokinase
Sequence:
MCGIFAAFKHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYNHIQLREMCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSPETVYFASELKCLTDVCDSIISFPPGHVYDSETDKITRYFTPDWLDEKRIPSTPVDYHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKANADANEDNNVDEKQLAGIDDQGHLHTSGWSRLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTDEPDVKPYLPEEILWRQKEQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTVMRWIPKADWGCAEDPSGRYAKIHEKHVSA
Protein: Probable beta-1,4-xylosyltransferase IRX14H (EC 2.4.2.-) (Protein IRREGULAR XYLEM 14 homolog) (Xylan xylosyltransferase IRX14H) (Q9FH90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:20335400}; Single-pass type II membrane protein {ECO:0000305|PubMed:20335400}.
Interaction partners:
- Probable beta-1,4-xylosyltransferase IRX10
- Probable beta-1,4-xylosyltransferase IRX10L
- Probable glucuronoxylan glucuronosyltransferase IRX7
- Probable glucuronoxylan glucuronosyltransferase F8H
- Probable galacturonosyltransferase-like 1
- Probable galacturonosyltransferase 12
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 2
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Protein IRX15-LIKE
- Beta-1,2-xylosyltransferase
Sequence:
MKLSVFRLSYWNRRGSSFRSSPSLDPSFDGKSPSSVFWFVIHGLCCLISLILGFRFSHLVLFFLFSTSVTNLYTTPFLFAGNGGVSQLLRLKPLETATNSTVKKNSRVVVGRHGIRIRPWPHPNPIEVLRAHQLLVRVQKEQKSMYGVRSPRTVIVVTPTYVRTFQALHLTGVMHSLMLVPYDLVWIVVEAGGITNETASFIAKSGLKTIHLGFDQKMPNTWEDRHKLETKMRLHALRVVREKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAHSGNADELSSILKNEQGKNKEKPSMPIQGPSCNSSEKLVGWHIFNTQPYAKKTAVYIDEKAPVMPSKMEWSGFVLNSRLLWKESLDDKPAWVKDLSLLDDGYAEIESPLSLVKDPSMVEPLGSCGRRVLLWWLRVEARADSKFPPGWIIKSPLEITVPSKRTPWPDSSSELPAAAIKEAKSNSKPRVSKSKSYKEKQEPKAFDGVKVSATS
Protein: von Hippel-Lindau disease tumor suppressor (Protein G7) (pVHL) (P40337)
Organism: Homo sapiens (Human)
Function: Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:9751722}. Cell membrane {ECO:0000269|PubMed:19584355}; Peripheral membrane protein {ECO:0000269|PubMed:9751722}. Endoplasmic reticulum {ECO:0000269|PubMed:12169691, ECO:0000269|PubMed:34290272}. Nucleus {ECO:0000269|PubMed:9751722}. Note=Found predominantly in the cytoplasm and with less amounts nuclear or membrane-associated (PubMed:9751722). Colocalizes with ADRB2 at the cell membrane (PubMed:19584355). {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:9751722}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:9751722}. Nucleus {ECO:0000269|PubMed:9751722}. Note=Equally distributed between the nucleus and the cytoplasm but not membrane-associated. {ECO:0000269|PubMed:9751722}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Cullin-2
- E3 ubiquitin-protein ligase RBX1
- Elongin-B
- Elongin-C
- Hypoxia-inducible factor 1-alpha
- Egl nine homolog 1
- Ubiquitin-like protein NEDD8
- Ubiquitin carboxyl-terminal hydrolase 33
- Prefoldin subunit 3
Sequence:
MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
Protein: Aldo-keto reductase family 1 member C18 (EC 1.1.-.-) (20-alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (EC 1.1.1.149) (HSD1) (P51652)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of progesterone into 20-alpha-dihydroprogesterone (20 alpha-OHP).
Subcellular location: Cytoplasm.
Interaction partners:
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Polyprenal reductase
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Steroid 21-hydroxylase
- Cytochrome P450 11B3, mitochondrial
- Aldo-keto reductase family 1 member D1
- Aldo-keto reductase family 1, member C1
Sequence:
MNSKIQKMELNDGHSIPVLGFGTYATEENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPVLLDDPILCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFPANMFKAHPNFPFSDEY
Protein: Vacuolar protein sorting-associated protein 21 (GTP-binding protein YPT51) (Vacuolar protein-targeting protein 12) (P36017)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:10679018, ECO:0000269|PubMed:12589066}; Lipid-anchor {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:14576278}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 8
- Vacuolar protein sorting-associated protein 3
- Vacuolar morphogenesis protein 6
- E3 ubiquitin-protein ligase PEP5
- Vacuolar protein sorting-associated protein 9
- GTP-binding protein YPT52
- Vacuolar segregation protein PEP7
- Phosphatidylinositol 3-kinase VPS34
- Rab proteins geranylgeranyltransferase component A
- Rab GDP-dissociation inhibitor
Sequence:
MNTSVTSIKLVLLGEAAVGKSSIVLRFVSNDFAENKEPTIGAAFLTQRVTINEHTVKFEIWDTAGQERFASLAPMYYRNAQAALVVYDVTKPQSFIKARHWVKELHEQASKDIIIALVGNKIDMLQEGGERKVAREEGEKLAEEKGLLFFETSAKTGENVNDVFLGIGEKIPLKTAEEQNSASNERESNNQRVDLNAANDGTSANSACSC