wanglab/gogpt-training-data huggingface dataset:
Protein: Photosystem I reaction center subunit IX (PSI-J) (P56769)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May help in the organization of the PsaE and PsaF subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00522}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00522}.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit III, chloroplastic
- Chlorophyll a-b binding protein 4, chloroplastic
- Chlorophyll a-b binding protein 6, chloroplastic
Sequence:
MRDLKTYLSVAPVLSTLWFGSLAGLLIEINRLFPDALTFPFFSF
Protein: Alkaline phosphatase, germ cell type (EC 3.1.3.1) (Alkaline phosphatase 5) (Alkaline phosphatase, placental-like) (Embryonic alkaline phosphatase) (EAP) (Embryonic-type alkaline phosphatase) (P24823)
Organism: Mus musculus (Mouse)
Function: Alkaline phosphatase that can hydrolyze various phosphate compounds.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- GTP cyclohydrolase 1
- Cancer-related nucleoside-triphosphatase homolog
- 6-pyruvoyl tetrahydrobiopterin synthase
- Thiamine pyrophosphokinase 1
- Glutathione hydrolase 6
Sequence:
MWGACLLLLGLSLQVCPSVIPVEEENPAFWNRKAAEALDAAKKLKPIQTSAKNLVILMGDGMGVSTVTATRILKGQQQGHLGPETQLAMDRFPHMALSKTYNTDKQIPDSAGTGTAFLCGVKTNMKVIGLSAAARFNQCNTTWGNEVVSVMHRAKKAGKSVGVVTTTSVQHASPAGTYAHTVNRGWYSDAQMPASALQDGCKDISTQLISNMDIDVILGGGRKFMFPKGTPDQEYPTDTKQAGTRLDGRNLVQEWLAKHQGARYVWNRSELIQASLNRSVTHLMGLFEPNDMKYEIHRDPAQDPSLAEMTEVAVRMLSRNPKGFYLFVEGGRIDHGHHETVAYRALTEAVMFDSAVDKADKLTSEQDTMILVTADHSHVFSFGGYTQRGASIFGLAPFKAEDGKSFTSILYGNGPGYKLHNGARADVTEEESSNPTYQQQAAVPLSSETHSGEDVAIFARGPQAHLVHGVQEQNYIAHVMAFAACLEPYTDCGLASPAGQSSAVSPGYMSTLLCLLAGKMLMLMAAAEP
Protein: Phosphatidylinositol transfer protein CSR1 (CHS5 SPA2 rescue protein 1) (SEC14 homolog protein 2) (Q06705)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Activates SPO14/PLD1 (phospholipase D1) by stimulating phosphoinositide synthesis via the STT4 PtdIns 4-kinase. Modulates ArfGAP function through effects on SPO14 activity. Inhibits phosphatidylcholine degradation by PLB1 (phospholipase B1). May also regulate post-Golgi membrane-trafficking events and have a role resistance to oxidative stress. Inhibits fatty acid synthase activity in response to heme depletion and oleic acid starvation, preventing saturated fatty acid (SFA) accumulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12869188}. Microsome {ECO:0000269|PubMed:12869188}. Endosome {ECO:0000269|PubMed:10848624}.
Interaction partners:
- Phosphatidylinositol transfer protein SFH5
- SEC14 cytosolic factor
- Putative uncharacterized protein YLR379W
- Zinc-regulated transporter 2
Sequence:
MSFDRQLTEDQEVVLKQIWTHLFHLWQVPVDGTHIFPNNSLHSSSTPAKKKKSSWFSKLQSSDHTQDSSEAAEAAHLYEKGKIHKALANLDPQTTKKQFWHDIKNETPDATILKFIRARKWNADKTIAMLGHDLYWRKDTINKIINGGERAVYENNETGVIKNLELQKATIQGYDNDMRPVILVRPRLHHSSDQTEQELEKFSLLVIEQSKLFFKENYPASTTILFDLNGFSMSNMDYAPVKFLITCFEAHYPESLGHLLIHKAPWIFNPIWNIIKNWLDPVVASKIVFTKNIDELHKFIQPQYIPRYLGGENDNDLDHYTPPDGSLDVHLKDTETRAMIEKEREELVEQFLTVTAQWIEHQPLNDPAYIQLQEKRVQLSTALCENYSKLDPYIRSRSVYDYNGSLKV
Protein: Pyruvate kinase PKM (EC 2.7.1.40) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (P52480)
Organism: Mus musculus (Mouse)
Function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Subcellular location: [Isoform M2]: Cytoplasm {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli. Nuclear translocation is promoted by acetylation by EP300. Deacetylation by SIRT6 promotes its nuclear export in a process dependent of XPO4, thereby suppressing its ability to activate transcription and promote tumorigenesis. {ECO:0000250|UniProtKB:P14618}.; SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm {ECO:0000250|UniProtKB:P14618}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Alpha-enolase
- L-lactate dehydrogenase A chain
- Fructose-bisphosphate aldolase A
- Catenin beta-1
- Glucose-6-phosphate isomerase
- Beta-enolase
- L-lactate dehydrogenase B chain
- POU domain, class 5, transcription factor 1
- Gamma-enolase
Sequence:
MPKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVEMLKEMIKSGMNVARLNFSHGTHEYHAETIKNVREATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKEKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEAAAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDAVLNAWAEDVDLRVNLAMDVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Protein: Proapoptotic nucleolar protein 1 (I0J062)
Organism: Homo sapiens (Human)
Function: Apoptosis-inducing protein that modulates the tumor suppressor function of CDKN2A/p14ARF. Enhances the stability of CDKN2A/p14ARF protein by protecting it from degradation. May act as a tumor suppressor.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:22094112}. Note=Colocalizes with CDKN2A/p14ARF in the nucleolus. {ECO:0000269|PubMed:22094112}.
Interaction partners:
Sequence:
MGVRLRVWPAAPHSISRCPRPLGAVLSILLAGGSRKGTPTARCLGQRTKEKRVGGRSLRSEAGSGPCPTAGAQPTAPSSAWPPRLRPRTCPQMSGELPRVRPTRVGLSSLGSGPGHPPSGTRMCGERARNRRGRARRLTPEQPRIGASAGPGPPLPPARPRCSGSCHLPRPPQHLSPPQPGRVRMGAAEGSRRADTHHARRRRRARLPAPRSAST
Protein: Protein FAM170B (Acrosome-related protein) (A6NMN3)
Organism: Homo sapiens (Human)
Function: Plays a role in fertilization through the acrosome reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:26179146}. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000250|UniProtKB:E9PXT9}.
Interaction partners:
Sequence:
MKCYFTDHRGEQSPTDGTTLSLTSPESTEESVEVFWPGTIQREGSSPRPGPAIPREEGLYFAARDRGMRDWSSSPSSESSEYQSYSQYQSCCSCMCDEDNAAPQSVCAFYTHVQTVRGVAVAWETEAGFEPVTRKPRIHEAQFIKRQRWNGSSFEMASNTDMRWDLEACKSNCSPEPEDIDLLECCLQELREPPDWLVTTNYGVRCVACCRVLPSLDALLEHAQHGIREGFSCQIFFEEMLERRRAQGQAHDQQLEEEQSPSDNSECSRPQGEVLSAQQQEKQ
Protein: Indole-3-acetic acid-amido synthetase GH3.4 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 4) (AtGH3-4) (CF4-like protein) (Q9LQ68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp, Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or no product formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic and butyric acid analogs of IAA, PAA and the synthetic auxin naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be used as substrates.
Interaction partners:
- Auxin transporter protein 1
- RING/FYVE/PHD zinc finger superfamily protein
- Serine/threonine-protein kinase SRK2F
- Two-component response regulator ARR16
Sequence:
MAVDSLLQSGMASPTTSETEVKALKFIEEITRNPDSVQEKVLGEILSRNSNTEYLKRFDLNGAVDRKSFKSKVPVVIYEDLKTDIQRISNGDRSPILSSHPITEFLTSSGTSAGERKLMPTIEEDINRRQLLGNLLMPVMNLYVPGLDKGKGLYFLFVKSESTTSGGLPARPALTSYYKSDYFRTSDSDSVYTSPKEAILCCDSSQSMYTQMLCGLLMRHEVNRLGAVFPSGLLRAISFLQNNWKELSQDISTGTLSSKIFDHAIKTRMSNILNKPDQELAEFLIGVCSQENWEGIITKIWPNTKYLDVIVTGAMAEYIPMLEYYSGGLPMASMIYASSESYFGINLNPMCKPSEVSYTIFPNMAYFEFLPHNHDGDGGVEATSLVELADVEVGKEYELVITTYAGLYRYRVGDILRVTGFHNSAPQFKFIRRENVLLSIESDKTDEADLQKAVENASRLLAEQGTRVIEYTSYADTKTIPGHYVIYWELLSRDQSNALPSDEVMAKCCLEMEESLNAVYRQSRVSDKSIGPLEIRVVQNGTFEELMDFSISRGSSINQYKVPRCVSLTPIMKLLDSRVVSAHFSPSLPHWSPERRH
Protein: Transcription initiation factor TFIID subunit 12 (TBP-associated factor 12) (O13722)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex subunit Spt3
- SAGA complex subunit Sgf29
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Ngg1
- SAGA complex subunit Hfi1
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 4
- SAGA complex subunit Sgf73
- Transcription initiation factor TFIID subunit 2
- SAGA complex/transcription factor TFIID complex subunit Taf6
Sequence:
MNGQHSSPGTPVQRPSAGPVNQAQFSQQRTNQLTSLLHTMTMYQQLAQNVGLNTPQGQVYLLQAQTIRRQLQGHAQSGQLPNQQLLQQLQSNGALQQGTPEPSNTRPRPQLNAQEQTMLLVRHRQLQTAQNYLTEMKEALGRIKNELSTNERLDTSAREALVKQESELTVKIAQFTAAISNGIRSIQQLQNRQASSANGNNTGTSTPVNASTDTRKSTASTPQLQQTQAQANAPQQRINPETSSVPETPVGVSAANVSNESTELATSATQQSGLANNVEKSQTPSYMSANHLPKVDSKSPIPFSVPPSRATLTGGYASGSIGLSTPGLSRAPHYELDNGNRLLSKRKLHDLLQQIDSEEKIEPEVEELLLEIADEFVESVTNFACRLAKHRKSDTLDVRDVQLHLERNWNIRLPGFASDDIVKSARKTGPTPSYQQKQNAIGTAKSLNKD
Protein: IFNc (K4LAX8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- CRFB3
- Interferon alpha/beta receptor 1a-like
- CRFB5c
- Interferon regulatory factor 3
- Interferon regulatory factor 7
- IFNd
- Interferon gamma receptor 1-like
- Interferon gamma receptor 1
- CRFB1a
- CRFB2
Sequence:
MALQTITWMSAFLCVAHVCSMPMPCQLQGQLVRITHNLLRDMGGNFPLECLQENVFVAFPATAFASSGAPQLGSSGAKAIYETLKNIDILFEADDLPTQWDQQKLKNFQNIVYRQIEESKCMMGSVDTSDYLIRTEGLNTYFGNIAAVLKEKNFSYCAWEVVRKELLYTLQFILEHNSDSLLWANRT
Protein: Protein TonB (P02929)
Organism: Escherichia coli (strain K12)
Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment.
Subcellular location: Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Interaction partners:
- Biopolymer transport protein ExbD
- Biopolymer transport protein ExbB
- Vitamin B12 transporter BtuB
- Ferrichrome outer membrane transporter/phage receptor
- Ferrienterobactin receptor
- Fe
- Hydroxamate siderophore receptor FhuE
- Outer membrane porin PhoE
- Catecholate siderophore receptor Fiu
- Translation initiation factor IF-2
Sequence:
MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ
Protein: Octaketide synthase 2 (OKS 2) (EC 2.3.1.-) (Polyketide synthase 4) (C4NF90)
Organism: Aloe arborescens (Kidachi aloe)
Function: Catalyzes the iterative condensations of 8 molecules of malonyl-CoA to produce aromatic octaketides, SEK4 and SEK4b, the products of the minimal polyketide synthase for the benzoisochromanequinone actinorhodin. May be involved in the biosynthesis of the octaketide barbaloin.
Interaction partners:
Sequence:
MGSLSNYSPVMEDVQAIRKAQKADGTATVMAIGTAHPPHIFPQDTYADFYFRATNSEHKVELKKKFDRICKKTMIGKRYFNYDEEFLKKYPNITSFDEPSLNDRQDICVPGVPALGAEAAVKAIAEWGRPKSEITHLVFCTSCGVDMPSADFQCAKLLGLRTNVNKYCVYMQGCYAGGTVMRYAKDLAENNRGARVLVVCAELTIIGLRGPNESHLDNAIGNSLFGDGAAALIVGSDPIIGVERPMFEIVCAKQTVIPNSEDVIHLHMREAGLMFYMSKDSPETISNNVEACLVDVFKSVGMTPPEDWNSLFWIPHPGGRAILDQVEARLKLRPEKFGATRTVLWDCGNMVSACVLYILDEMRRKSVADGLATYGEGLEWGVLLGFGPGMTVETILLHSLPPV
Protein: 1-Cys peroxiredoxin PER1 (EC 1.11.1.24) (Rehydrin homolog) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin) (A2SZW8)
Organism: Zea mays (Maize)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O04005}. Cytoplasm {ECO:0000250|UniProtKB:O04005}.
Interaction partners:
- NADPH-dependent thioredoxin reductase 3
- Glutaredoxin-dependent peroxiredoxin
- Glutaredoxin-dependent peroxiredoxin
- Glutaredoxin-dependent peroxiredoxin
- Uncharacterized protein
- Sulfiredoxin chloroplastic/mitochondrial
- Sulfiredoxin chloroplastic/mitochondrial
- sulfiredoxin
- O-fucosyltransferase family protein
- Thioredoxin reductase
Sequence:
MPGLTIGDTVPNLELDSTHGKIRIHDYVGDGYAIIFSHPADFTPVCTTEMAAMAGYAKEFEKRGVKLLGISCDDVESHRQWTKDVEAYGGKQQQQQATTTKVTFPILADPARDAIRQLNMVDPDEKDAAGRSMPSRALHVVGPDKAVKLSFLYPATTGRNMDEVLRAVDSLLTAAKHGGKVATPANWKPGECAVIAPGVSDEEARKMFPQGFETADLPSKKGYLRFTKV
Protein: Flagellar hook-basal body complex protein FliE (P24502)
Organism: Bacillus subtilis (strain 168)
Subcellular location: Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar motor switch phosphatase FliY
- Flagellar motor switch protein FliG
- Flagellar M-ring protein
- FlaA locus uncharacterized protein YlxG
- Probable flagellar assembly protein FliH
- Flagellar basal-body rod protein FlgG
- Flagellar basal-body rod protein FlgC
- Flagellar basal body rod protein FlgB
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
Sequence:
MINAISPFQVQNTQNTQNATNQVNNSQKTDSSNQTSFSELLKNSISSLNESQVASDNMTNALAAGKDVNLDEVMIAAQKASISLTAATEFRNKAVEAYQEIMRMQM
Protein: Uncharacterized protein YER079W (P40052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YER078W-A
- Altered inheritance of mitochondria protein 9, mitochondrial
- Protein FDO1
- Putative uncharacterized protein YOR248W
Sequence:
MPDSSHSISSKDVASAISLYDQSIYTNNRSTNLDLDQRSMSPSNIASGEDRITRTNSGCSITSGASMIATKDGIQGINVKRDGIPKYSLNLLNSMVRKQYDHNNGTKSPTPKTSNMVDPKNKKKNKKKKNDKDDKYKVSHDQTEKFYKLNTTSNSNLTSDSTTSLSDQFYFQKSNADSAPLDNANYPLSDHSPSLNSMDNTTKHSSNVHT
Protein: Ubiquilin-like protein (Q8IYU4)
Organism: Homo sapiens (Human)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
Sequence:
MWHAISRTSRMSQSGCPSGLLADKNISSSATRVIVKTAGNQKDFMVADDISVRQFKEMLLAHFQCQMDQLVLVFMGCLLKDHDTLSQRGIMDGHTIYLVIKSKQGSRSLAHSFRDLPTNDPCHRDRNTKGNSSRVHQPTGMNQAPVELAHFVGSDAPKVHTQNLEVSHPECKAQMLENPSIQRLLSNMEFMWQFISEHLDTQQLMQQNPEVSRLLLDNSEILLQTLELARNLAMIQEIMQIQQPSQNLEYPLNPQPYLGLETMPGGNNALGQNYADINDQMLNSMQDPFGGNPFTALLAGQVLEQVQSSPPPPPPSQEQQDQLTQHPATRVIYNSSGGFSSNTSANDTLNKVNHTSKANTAMISTKGQSHICATRQPAWIPALPSIELTQQLQEEYKDATVSLSSSRQTLKGDLQLSDEQSSSQITGGMMQLLMNNPYLAAQIMLFTSMPQLSEQWRQQLPTFLQQTQISDLLSA
Protein: Probable membrane transporter protein YfcA (P0AD30)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Elongation factor P lysine hydroxylase
- Penicillin-insensitive murein endopeptidase
- Uncharacterized protein YfcL
- Chorismate synthase
- Putative NAD
- Ribosomal protein uL3 glutamine methyltransferase
Sequence:
METFNSLFMVSPLLLGVLFFVAMLAGFIDSIAGGGGLLTIPALMAAGMSPANALATNKLQACGGSISATIYFIRRKVVSLSDQKLNIAMTFVGSMSGALLVQYVQADVLRQILPILVICIGLYFLLMPKLGEEDRQRRMYGLPFALIAGGCVGFYDGFFGPAAGSFYALAFVTLCGFNLAKATAHAKLLNATSNIGGLLLFILGGKVIWATGFVMLVGQFLGARMGSRLVLSKGQKLIRPMIVIVSAVMSAKLLYDSHGQEILHWLGMN
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A5HV10)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
AAATEEPEVIPDPAKQTDRVVKIAGISAGVLVFILLLLVVIVIVKKSKLAKKRKDAMGNTRQEMTHMVNAMDRSYADQSTLHAEDPLSLTFMDQHNFSPRYENHSATAESSRLLDVPRYLCEGTESPYQTGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLESS
Protein: 14-3-3-like protein GF14 upsilon (General regulatory factor 5) (P42645)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. May be involved in cell cycle regulation by binding to soluble EDE1 and sequestering it in an inactive form during the early stages of mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21558460}. Nucleus {ECO:0000269|PubMed:21558460}. Note=Not associated with microtubules (PubMed:21558460). Translocates from the cytosol to the nucleus when phosphorylated (By similarity). {ECO:0000250|UniProtKB:P48349, ECO:0000269|PubMed:21558460}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31z fusion protein
- Dual specificity phosphatase Cdc25
Sequence:
MSSDSSREENVYLAKLAEQAERYEEMVEFMEKVAKTVETEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEDSRGNSDHVSIIKDYRGKIETELSKICDGILNLLEAHLIPAASLAESKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLVAYKSAQDIALADLAPTHPIRLGLALNFSVFYYEILNSSDRACSLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDLNDEAGDDIKEAPKEVQKVDEQAQPPPSQ
Protein: Protein Rv1367c (P9WLZ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Carboxypeptidase Rv3627c
- D-alanyl-D-alanine carboxypeptidase DacB2
- D-alanyl-D-alanine carboxypeptidase DacB1
- Putative amidase AmiB2
- Conserved protein
- Lipase LipV
- Possible penicillin-binding lipoprotein
Sequence:
MNLDGNQASIREVCDAGLLSGAVTMVWQREKLLQVNEIGYRDIDAGVPMQRDTLFRIASMTKPVTVAAAMSLVDEGKLALRDPITRWAPELCKVAVLDDAAGPLDRTHPARRAILIEDLLTHTSGLAYGFSVSGPISRAYQRLPFGQGPDVWLAALATLPLVHQPGDRVTYSHAIDVLGVIVSRIEDAPLYQIIDERVLGPAGMTDTGFYVSADAQRRAATMYRLDEQDRLRHDVMGPPHVTPPSFCNAGGGLWSTADDYLRFVRMLLGDGTVDGVRVLSPESVRLMRTDRLTDEQKRHSFLGAPFWVGRGFGLNLSVVTDPAKSRPLFGPGGLGTFSWPGAYGTWWQADPSADLILLYLIQHCPDLSVDAAAAVAGNPSLAKLRTAQPKFVRRTYRALGL
Protein: DNA replication complex GINS protein PSF2 (GINS complex subunit 2) (Q7ZT46)
Organism: Xenopus laevis (African clawed frog)
Function: Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730133}. Chromosome {ECO:0000269|PubMed:12730133}. Note=Associates with chromatin. {ECO:0000269|PubMed:12730133}.
Interaction partners:
Sequence:
MDASEVEFLAEKEQVTVIPNFSLDKVYLIGGDLGPFNPSLPVEVPLWLAINLKQRQKCRIVPPEWMDVEKLEAIRDQERREETFTPMPSPYYMELTKLLLNHAADNIPKADEIRTLVKDTWDTRIAKLRLSADSFVKGQEAHAKLDNLTLMEINTIGTFFTESLNHMYKLRTSLQNPEEGQSQDY
Protein: Kell blood group glycoprotein homolog (EC 3.4.24.-) (CD antigen CD238) (Q9EQF2)
Organism: Mus musculus (Mouse)
Function: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Spans the erythrocyte membrane, and is attached to the underlying cytoskeleton. {ECO:0000250}.
Interaction partners:
- Endoplasmic reticulum membrane adapter protein XK
- Glycophorin-A
- Endothelin-3
- Ammonium transporter Rh type A
- Band 3 anion transport protein
- Tripartite motif-containing protein 10
- Blood group Rh
- Erythroid membrane-associated protein
- Claudin-13
- Spectrin alpha chain, erythrocytic 1
Sequence:
MGPPWSQESSPEERLPTEWSRQLTRARWVLLAVLLCGLLLGSSMLWFYIFRNCGPCPCETPVCMELLDHYLASGNRSVAPCTDFFSFACEKANGTSDSFQALTEENKSRLWRLLEAPGSWHLGSGEEKAFQFYNSCMDTDAIEASGSGPLIQIIEELGGWNITGNWTSLDFNQNLRLLMSQYGHFPFFRAYLRPHPAPPHTPIIQIDQPEFDILLQQEQEQKVYAQILREYVTYLNRLGTLLGSNPQEAQQHASWSIVFTSRLFQFLRPQQQQQAQDKLFHVVTIDELQEMAPAIDWLSCLQAIFTPMSLNSSQTLVVHDLDYLRNMSQLVEEGLLNHRESIQSYMILGLVDTLSPALDTKFQEARRELIQELRKLKERPPLPAYPRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFAEIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAVKPDIATQEYNDIQLGPSFLQSFLSCVRSLRARNVQSFLQPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCPACDTHVLQEALLCLERHYAAFPLPSISSFNGSHTLLENAADIGGVAIAFQAYSKRIVEHTGELTLPNLDLSPYQLFFRSYAQVMCRGLSSQDPQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCKLW
Protein: Putative polypeptide N-acetylgalactosaminyltransferase 13 (pp-GaNTase 13) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 13) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13) (Q8MYY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MHAGGKYCGPRHCSFYIIAFLICQLFFLVIFIRNDDASSANELLSFMNESEESDHLDWRVFISHTPETSEDFYQYNIHLSNALGLIRKLPVTRHHSCTTRNSILPAPLEANVSVVISFHNEARSMLLRTIVSLLSRSPEDYLHELILVDDGSQRDVTLLDDLKRWMGGVFGSRYRLGLTFLRNQERMGLIWSRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHWLKRQLTNQESLEMPYQSPAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKLWLCGGQIEIVPCSRIGHIFRRRHAFDFPPQSDRQLSPAQETYLHNSKIIAESWLDEYKNMFYALRPAARRIPLDHTYDELQRMRKERRCHPFEWYLRHVSPELRMHFDELSATGTLRNEDRCVHARQKDSQPILASCYLSDITQWSMLRQSGQLSTHRELCLAVGFGMRIALEPCGRNETVRRSQRWVRLGTHLLHAESHLCLDNPLKDRLEMSTCRSHAVSQSFQFALEMEGQT