wanglab/gogpt-training-data huggingface dataset:
Protein: Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein) (P53995)
Organism: Mus musculus (Mouse)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Interaction partners:
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 23 homolog
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit CDC26
Sequence:
MSNFSEERATMIAAGDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGVSEIGDAADYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSTVQQALWCDFIISQDKSEKIYKSHELEKCICILQSSCMNMHSIDGKDYIASLPFQVANVWATKYGLLFERCSSSHEVPPSLPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQYVVDPAVKIVFLNIDPSIVMTYDAVQNVHSVWTLRRVKPEEENAVLKFPEQAGTLQNATTSSSLTAHLRSLSKGESPVASPFQNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALGVHSFSGAQRFNLSSHSQSPKRHSISHSPSGSFNDSFLAPETEPIVPELCIDHLWTETLPNIREKNSQASKVFITTDLCGQKFLCFLVEAQLQLRCVKFQESNDKTQLIFGSVTNIHAKDAAPVEKIHTMLVLEGNGNLVLYTGVVRVGKVFIPGLPAPSLTMSNMMPRPSTPLDGVGTPKPLSKLLGSMDEVVLLSPVPELRDSSKLNDSLYNEDCTFQQLGTYIHSVRDPVHNRVTLELSNGSMVRITIPEVATSELVQTCLQAIKFILPKEVAIQVLVKWYNVHSAPGGPSCHSEWSLFVICLLNMMGYNTDRLAWTRSFDFEGSLSPVIAPKKARPSDTGSDEDWEYLLNSEYHRNVESHLLNKSLCLTALEVSNAKDEDFSQNLSLDSSTLLFAHIPAIFFVLHLVYEELKLNTLMGEGICSLIDLLVQLARDLKLDSYLDHYYRDSPTLVKTTGQVCTIDQGQMGFMHHPPFFTSEPPSIYQWVSSCLKGEGMPPYPYLPGICERSRLVVLSIALYTLGDESCVSDETCQYLSKVTSTPQKPQAEQEENRFTFRHSASVSVLAERLVVWMASVGFTLRDLETLPFGIALPIRDAIYHCREQPDSDWSEAVCLLIGRQDLSKQACEGNLPRGKSVLSSEVSSGTEAEEEDDGMNDLNHEVMSLIWSEDLRVQDVRRLLQSAQPVRVNVVQYPELSDHEFIEEKENRLLQLCQRTMALPVGRGMFTLFSYHPVPTEPLPVPKLNLTGRAPPRNTTVDLNSGNIDVPPNMASWASFHNGVAAGLKIAPASQIDSAWIVYNKPKHAELANEYAGFLMALGLNGHLTKLATLNIHDYLTKGHEMTSIGLLLGVSAAKLGTMDMSITRLLSIHVPALLPPTSTELDVPHNVQVAAVVGIGLVYQGTAHRHTAEVLLAEIGRPPGPEMEYCTDRESYSLAAGLALGMVCLGHGSNLIGMSDLNVPEQLYQYMVGGHRRFQTGMHREKHKSPSYQIKEGDTINVDVTCPGATLALAMIYLKTNNRSIADWLRAPDTMYLLDFVKPEFLLLRTLARCLILWDDILPNSKWVDSNVPQIIRENSISLSEIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFSCLHKFAKDFMNYLSAPNASVTGPYNLETCLSVVLLSLAMVMAGSGNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSLSTSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRLLVPVDVDTNTPCYALIEVTYKGTQWYEQTKEELMAPTLLPELHLLKQMKVKGPRYWELLIDLSKGEQHLRSILSKDGVLYVKLRAGQLSYKEDPMGWQSLLAQTVANRNSEARAFKPETISSFTSDPALLSFAEYFCKPTVSMGPKQEILDLFSSILYECVAQETPEMLPAYIAMDQALRSLKKRDMSDTSDLWQIKLILEFFSSRSHQDRQHTYPKRGLFINSEFLPVVKCTVDATLDQWLQAGGDVCVHAYLSGQPVEKSQLNMLACFLVYHSVPAPRHLPPMGLEGSTSFAELLYRFRHLKMPVRALLRLAPVLLGNPQPMVM
Protein: Leucine-rich repeat and guanylate kinase domain-containing protein (Q96M69)
Organism: Homo sapiens (Human)
Function: Involved in multiple aspects of sperm assembly including acrosome attachment, shaping of the sperm head and in the early aspects of axoneme development. Not essential for primary cilium biogenesis.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9D5S7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9D5S7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9D5S7}. Note=Localizes to the acrosome and acroplaxome in round spermatids. Localizes to the manchette during spermiogenesis. Also found in the basal body of elongating spermatids, and in primary cilia of somatic cells. {ECO:0000250|UniProtKB:Q9D5S7}.
Interaction partners:
- Sperm-associated antigen 17
- Protein dpy-30 homolog
- Cilia- and flagella-associated protein 74
- Cilia- and flagella-associated protein 119
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Cilia- and flagella-associated protein 221
- c-Myc-binding protein
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MATSERALLRTRAASLLRGLGRSRTGARSLQFRAEKERQPCWSFPMGQKTKGSSNIASSYLLQQLMHRYQELDSDGDEDQGEGEAGSEESSESEMLNLEEEFDGVLREEAVAKALHHLGRSGSGTEQVYLNLTLSGCNLIDVSILCGYVHLQKLDLSANKIEDLSCVSCMPYLLELNASQNNLTTFFNFKPPKNLKKADFSHNQISEICDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGLNKLPIKILCLSNNQIEMITGLEDLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIAELREIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEKVSAVNKYDPPPEVVAAQDHLTHVVNSVMQPQRIFDSTLPSLDAPYPMLILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNRDTVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIEFAVSRVDLYIKINQNFPGYFDEVINADDLDVAYQKLSQLIREYLGLTEEPAKSLATTADVKTSHLKPEAHPTKYISSNMGDFLHSTDRNYLIKFWAKLSAKKTPAERDSIHRQHEAARQALMGRIRPDHTLLFQRGPVPAPLTSGLHYYTTLEELWKSFDLCEDYFKPPFGPYPEKSGKDSLVSMKCSLFRFCPWSKELPFQPPEGSISSHLGSGASDSETEETRKALPIQSFSHEKESHQHRQHSVPVISRPGSNVKPTLPPIPQGRR
Protein: 3-methylornithine synthase (EC 5.4.99.58) ((2R,3R)-3-methylornithine synthase) ((3R)-3-methyl-D-ornithine synthase) (Pyrrolysine biosynthesis protein PylB) (Q8TUB9)
Organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Function: Catalyzes the isomerization of L-lysine to (2R,3R)-3-methylornithine via a radical-based mechanism (Probable). Is required for the biosynthesis of pyrrolysine.
Interaction partners:
- 3-methyl-D-ornithine--L-lysine ligase
- Pyrrolysine synthase
- Pyrrolysine--tRNA ligase
- Diaminopimelate decarboxylase
- L-lysine 2,3-aminomutase
- Monomethylamine methyltransferase MtmB1
- Trimethylamine methyltransferase MttB1
- Trimethylamine methyltransferase MttB2
- Biotin operon repressor/biotin-pyruvate carboxylase ligase
- Biotin synthesis BioY protein
Sequence:
MIKKMATEDLDRFGEKIIEGFQLSDDDLRALLSLESEEELEKLYYVARKVRNHYFGNRVFLNCFIYFSTYCKNQCAFCYYNCKNEINRYRLSREEIKETCKALKGAGFHMIDLTMGEDPYYYEEPDRFVELVQMVKNELGLPIMISPGVMDNATLLKAREKGANFFALYQETYDQELYEKLRVGQSFKGRYNTRRFAKEQGYCIEDGILTGVGNDIESTIKSLRGMKSNDPDMVRVMTFLPQEGTPLERFKENSNLSELKIIAILRLIFPKCLIPASLDLEGIDGMVHRLNAGANIVTSILPSDSKLEGVANYDRDLEERDRDIKSVIKRLEGMGMEPAPQAEFETVLRC
Protein: Decapping nuclease RAI1 (ScRai1) (EC 3.6.1.-) (NAD-capped RNA hydrolase RAI1) (DeNADding enzyme RAI1) (EC 3.6.1.-) (RAT1-interacting protein) (P53063)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates. Stimulates exoribonuclease activity of RAT1, allowing it to degrade RNAs with stable secondary structure more effectively. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000269|PubMed:12612077}.
Interaction partners:
- Regulator of Ty1 transposition protein 103
- 5'-3' exoribonuclease 2
- Polynucleotide 5'-hydroxyl-kinase GRC3
- Exosome complex component RRP42
- 5'-3' exoribonuclease 1
- Decapping and exoribonuclease protein 1
- Ribosomal RNA-processing protein 17
- Ribosome biogenesis protein 15
- Cell division control protein 48
Sequence:
MGVSANLFVKQRGSTTALKQPKEIGFYSRTKDEEYLISDDTNLNYYYLPDAELDRKLDLSSGFQKFKDYYKDFEDRCSLRGLLETIESSERHKGKKINADIITFRGIARKLISCAFDSPSFNTVDLRIVSFNGQLFIKEVPEAVNAAKASSATEAGRNINQDLNVFTGYKFETLATLSNPLQYTPREVIEKRTKRIVSHGDEYISVVRTGVGNCKLILGAEVDCIFDFKENGRDNLKHYAELKCTQQVANISDTHKFERKLFRTWLQCFLVGIPRIIYGFKDDHYVLKTVEEFSTEEVPVLLKNNNPQVGSACLEAIKWYGLLTEWLLKMIPRDEDPHSQIRAFKLVFENNHLRLSEIEESDEEYSGLIDGEHILSNGFKEWRKSLK
Protein: Mycosin-3 (EC 3.4.21.-) (MycP3 protease) (O53695)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000269|PubMed:10974545}; Single-pass membrane protein {ECO:0000255}. Note=Cell wall-associated. {ECO:0000269|PubMed:10974545}.
Interaction partners:
- ESX-3 secretion system protein EccD3
- ESX-3 secretion system protein EccE3
- ESX-3 secretion-associated protein EspG3
- ESX-3 secretion system ATPase EccB3
- ESX-3 secretion system protein EccC3
- ESX-3 secretion system protein EccA3
- PPE family protein PPE4
- ESAT-6-like protein EsxH
- ESAT-6-like protein EsxG
Sequence:
MIRAAFACLAATVVVAGWWTPPAWAIGPPVVDAAAQPPSGDPGPVAPMEQRGACSVSGVIPGTDPGVPTPSQTMLNLPAAWQFSRGEGQLVAIIDTGVQPGPRLPNVDAGGDFVESTDGLTDCDGHGTLVAGIVAGQPGNDGFSGVAPAARLLSIRAMSTKFSPRTSGGDPQLAQATLDVAVLAGAIVHAADLGAKVINVSTITCLPADRMVDQAALGAAIRYAAVDKDAVIVAAAGNTGASGSVSASCDSNPLTDLSRPDDPRNWAGVTSVSIPSWWQPYVLSVASLTSAGQPSKFSMPGPWVGIAAPGENIASVSNSGDGALANGLPDAHQKLVALSGTSYAAGYVSGVAALVRSRYPGLNATEVVRRLTATAHRGARESSNIVGAGNLDAVAALTWQLPAEPGGGAAPAKPVADPPVPAPKDTTPRNVAFAGAAALSVLVGLTAATVAIARRRREPTE
Protein: Secretin (Q08535)
Organism: Mus musculus (Mouse)
Function: Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis. Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells. Acts as a key gastrointestinal hormone by regulating the pH of the duodenal content. Secreted by S cells of the duodenum in the crypts of Lieberkuehn and regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas. Production of bicarbonate is essential to neutralize the pH and ensure no damage is done to the small intestine by the gastric acid. In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation: released into the systemic circulation in response to hyperosmolality and acts at different levels in the hypothalamus, pituitary and kidney to regulate water homeostasis. Also plays a role in the central nervous system, possibly by acting as a neuropeptide hormone: required for hippocampal synaptic function and neural progenitor cells maintenance.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11384}.
Interaction partners:
- Secretin receptor
- VIP peptides
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- Vasoactive intestinal polypeptide receptor 2
- Vasoactive intestinal polypeptide receptor 1
- Cholecystokinin
- Gastrin
- Somatostatin
- Gastric inhibitory polypeptide
Sequence:
MEPPLPTPMLLLLLLLLSSSAALPAPPRTPRHSDGMFTSELSRLQDSARLQRLLQGLVGKRSEQDTENIPENSLARSKPLEDQLCLLWSNTQTLQDWLLPRLSLDGSLSLWLPPGPRSAVDRSEWTETTRPPR
Protein: H/ACA ribonucleoprotein complex subunit DKC1 (Dyskerin) (C9IYT0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, Cajal body {ECO:0000256|ARBA:ARBA00004408}.
Interaction partners:
Sequence:
MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYR
Protein: Urotensin-2B (Urotensin II-related peptide) (Urotensin IIB) (U-IIB) (UIIB) (Urotensin-2 domain-containing protein) (Q765I0)
Organism: Homo sapiens (Human)
Function: Potent vasoconstrictor.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Urotensin-2 receptor
- Urotensin-2
Sequence:
MNKILSSTVCFGLLTLLSVLSFLQSVHGRPYLTQGNEIFPDKKYTNREELLLALLNKNFDFQRPFNTDLALPNKLEELNQLEKLKEQLVEEKDSETSYAVDGLFSSHPSKRACFWKYCV
Protein: Uncharacterized protein PB8E5.10 (Q9C0X5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Meiotically up-regulated gene 93 protein
- Meiotic expression up-regulated protein 27
- Uncharacterized family 31 glucosidase C1039.11c
- RNA-binding protein mde7
Sequence:
MAVLSRIMKPYRAFQRLPFELKPLAILIGIAGSTAIFTMGYKIYSDPEIRRSPSWVAQTQQKEETKVKKPQFH
Protein: Putative inactive methylesterase 20 (AtMES20) (Protein MATERNAL EFFECT EMBRYO ARREST 69) (F4JRA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-splicing factor SLU7-B
- Nuclear pore complex protein NUP58
- Amino-terminal region of chorein
Sequence:
MKHYVLVHGGCHGAWCWYKVKPVLEASGHRVTVVDLTASGVNMSKVEEIQTLADYAKPLLEVLESFGSEDKVILVAHSLGGISVGLAADMFPSKISVAVFITSFMPDTTNPHLFMFSKSFVGALWSLRHMGHMIVL
Protein: Nucleotide sugar transporter SLC35D1 (Solute carrier family 35 member D1) (UDP-galactose transporter-related protein 7) (UGTrel7) (UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter) (UDP-GlcA/UDP-GalNAc transporter) (Q9NTN3)
Organism: Homo sapiens (Human)
Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar. Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D-glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides. May couple UDP-GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics. Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11322953}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 35 member B1
- UDP-N-acetylglucosamine transporter
- CMP-sialic acid transporter
- Nucleotide sugar transporter SLC35B4
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Adenosine 3'-phospho 5'-phosphosulfate transporter 2
- Alpha-mannosidase 2x
- Alpha-mannosidase 2
- UDP-galactose translocator
Sequence:
MAEVHRRQHARVKGEAPAKSSTLRDEEELGMASAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKALRVVKFPDLDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGVLLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYAFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAVEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNISIAGSLVYSYITFTEEQLSKQSEANNKLDIKGKGAV
Protein: Middle T antigen (MT) (MT-AG) (P03077)
Organism: Murine polyomavirus (strain A2) (MPyV)
Function: Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with host Ppp2/PP2A the Src tyrosine kinase components Src, Yes and Fyn, thereby activating their kinase activity. Activation of Shc1, Pclg1 and p85 mediate signal transduction pathways leading to cell cycle progression and cell division. MT also plays a role in regulation of early and late gene expression and in viral DNA replication.
Subcellular location: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPKRRSEELRRAATVHYTMTTGHSAMEASTSQGNGMISSESGTPATSRRLRLPSLLSNPTYSVMRSHSYPPTRVLQQIHPHILLEEDEILVLLSPMTAYPRTPPELLYPESDQDQLEPLEEEEEEYMPMEDLYLDILPGEQVPQLIPPPIIPRAGLSPWEGLILRDLQRAHFDPILDASQRMRATHRAALRAHSMQRHLRRLGRTLLLVTFLAALLGICLMLFILIKRSRHF
Protein: Probable pectin methyltransferase QUA2 (EC 2.1.1.-) (Protein OVERSENSITIVE TO SUGAR 1) (Protein QUASIMODO 2) (Protein TUMOROUS SHOOT DEVELOPMENT 2) (Q9C9Q8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the synthesis of homogalacturonan. Required for normal cell adhesion and plant development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17425712, ECO:0000269|PubMed:17461780}; Single-pass type II membrane protein {ECO:0000269|PubMed:17425712, ECO:0000269|PubMed:17461780}.
Interaction partners:
- Galacturonosyltransferase 8
- Protein ESMERALDA 1
- Probable pectin methylesterase CGR2
- Probable pectin methylesterase CGR3
- Glycosylinositol phosphorylceramide mannosyl transferase 1
- Protein FRIABLE 1
- Glutamate receptor 1.1
- Outer arm dynein light chain 1 protein
- Xylogalacturonan beta-1,3-xylosyltransferase
- Fucosyltransferase
Sequence:
MSMPLQRGISGVRVSDSSDDLRDSQMKDKTERARSTENNNLTLRFPFGFLFSNQSSSKHGGGGENGFSADPYSARSRHRLMLLFLKISLVLIVVIALAGSFWWTISISTSSRGHVYHNYRRLQEQLVSDLWDIGEISLGPNRWKELEYCNIESENFVPCFNVSENLALGYSNGDENDRFCGPGSKQECLELPPVKYRVPLRWPTGKDIIWHSNVKITAQEVVSSGSITKRMMMMEDDQISFRSASPMSDEVEDYSHQIAEMIGIKKDNFIEAGVRTILDIGCGYGSFGAHLLSKQILTMCIANYEASGSQVQLTLERGLPAMIGSFISKQLPYPSLSFDMLHCLRCGIDWDQKDGLLLVEIDRVLKPGGYFVWTSPLTNPRNKDHLKRWNFVHDFAESICWTLLNQQDETVVWKKTINTKCYSSRKPGVGPSVCTKGHDVESPYYRPLQMCIGGTRSRRWIPIEGRTRWPSRSNMNKTELSLYGLHPEVLGEDAENWKITVREYWSLLSPLIFSDHPKRPGDEDPSPPYNMLRNVLDMNAQFGGLNSALLEARKSVWVMNVVPTAGPNHLPMILDRGFVGVLHNWCEPFPTYPRTYDLVHADNLLSLQTSQPRKTCLLIDIFTEIDRLLRPEGWVIIRDTAQLVEKARETITQLKWEARVIEVESSSEQRLLICQKPFTKRQSI
Protein: Pollux, isoform F (A0A0B4KG76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFTVPFHRDTILTTSVSDASVLNKSRAMAELMHQMRDPAHTLGGSVGSIPQTLIGGGGGSHGNSNGALNGIHATPATNLKMSEAMRNAQHDTSPNPVSSKMKASKSYTHGLSSSSGTVNIPTSTSAQSNLSLLADISPNHTHFFEVMYVGKIRVSQKRVPNTFIDDALPKFKAYDAQRLRLLQNRKMSLSSEGGVGIEAKPSSSLKSHDLKEEDEEEQEQHKGHDDSQDSQAKPLVQLQLTGAEEGAAPRPLEDNKENKSPEKRPLLRGQSQIELGHKEHIPKQRDRSASQGCIPPYVEQNRTMVFLVGRCDLRLISPDRKQVLLYKDFKDVASCVHGQKSLDHFGIICRELNNDGYIGYVFKCQSEHVCDDIVAAIAQAFDTCAEQKKKQDTQIFSCEHCPMLWYHKLCTDVEGLSEKKTQALILRRIETLSDDEQEIVWAKFCGSEKTNSPVAEQNQFLMMLLRAHCESRQQRHVHDTAENRSEFLNQYLGGSTIFMKAKRSLTNSFDNLLKRKPSKDDIAVPSHNLRDIREGSAEPLGTQSPPEGFRSRSNTVGASPSSKPTAEQLKSPMMDIFIKVGNSPKEAETHQGSWRQAILNSVVTPSKGLDSEVPTEFLSPMRKPAKRGKRDAAELRELWRTAIRQTIMLNRMETENAMLQARQNENELKRIKLDYEEIVPCDKQLIERWEQIIERNSTQIGNKKDPKVLGHAIRTGVPRSKRGDVWTFLAEQHSMNTAPVDTKRFPNFNTPYHMLLKHLTEHQHAIFIDLGRTFPNHQFYKDPLGLGQLSLFNLLKAYSILDPELGYCQGLGFICGVLLLHCDEANSFQLLKHLMFRRNMRTKYLPDMKKFQLQLYQLSRLVKDHLPDLYVWLDQNDVSPTLYAAPWILTVFSSQFPLGFVARVFDLLFLESSDVIFKFAIALLSVHKQQLLAKDNFEEIMDYLKTVVPKMEHTCMEQIMKLVFSMDIGKQLAEYKVEYNVLQEEITTTNHHLEMLNREKTQNQHLEQQLQFAQSSIAQLETTRSSQQAQITTLQSQVQSLELTIQTLGRYVGQLVEHNPDLELPNEVRRMLQQLDDLDRQRRKPIFTERKIGKSVSVNSHLGFPLKVLEELTERDELGSPQKQKKEKTPFFEQLRQQQQQHRLNGGGQSSNVGESGSPTPPSRPNRLLDNASARTVMQVKLDELKLPEHVDKFVANIKSPLEVDSGVGTPLSPPSTASNSSGGSIFSRMGYRTTPPALSPLAQRQSYGVAITTAPCPQHMEEVAPATTMAVMPQEDVEEPQPMHPLSMVGGDVNVRFKGTTQLKSIRPVHHMRAIPLGGVQHPSSTEPAVRVAPVPVELAPPAATATTGRS
Protein: Cupincin (EC 3.4.-.-) (52 kDa globulin-like protein) (allergen Ory s NRA) (Q852L2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Seed storage protein (Probable). Globulin-like protein that acts as zinc metalloprotease. Cleaves specifically between Leu-15 and Tyr-16 of insulin B chain, and Gln-1 and Leu-2 of neurotensin (NT) peptide in vitro. May play a role as an initiating endopeptidase in germinating seeds (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAKKKTSSSMARSQLAALLISLCFLSLASNAVGWSRRGEREEEDERRRHGGEGGRPYHLGEESFRHWTRTRHGRFSVLERFPDEQVVGAAVGGYRVAVLEAAPRAFLQPSHYDADEVFYVKEGEGVIVLLREGRRESFCVREGDAMVIPAGAIVYSANTHSSKWFRVVMLLNPVSTPGHFEEYFPVGGDRPESFFSAFSDDVLQAAFNTRREELEKVFERQREGGEITTAPEEQIRELSKSCSRGGGGGSGSEWEIKPSSLTGKSPYFSNNHGKLFELTGDECRHLKKLDLQIGLANITRGSMIAPNYNTRATKLAVVLQGSGYFEMACPHVSGGGSSERREREREHGRRREEEQGEEEHGERGEKARRYHKVRAQVREESVIVIPASHPATIVASEGESLAVVCFFVGANHDEKVFLAGRNSPLRQLDDPAKKLVFGGSAAREADRVLAAQPEQILLRGPHGRGSVSDM
Protein: Bursicon (Bursicon subunit alpha) (Cuticle-tanning hormone) (Q9VD83)
Organism: Drosophila melanogaster (Fruit fly)
Function: Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading. Heterodimer specifically activates the G protein-coupled receptor rk.
Subcellular location: Secreted {ECO:0000269|PubMed:15242619, ECO:0000269|PubMed:15703293}.
Interaction partners:
- Partner of bursicon
- Rickets
- Cardioactive peptide
- Eclosion hormone
- Ecdysis triggering hormone
- Beta glycoprotein hormone related polypeptide
- GEO08248p1
- Adipokinetic hormone
- Glycoprotein hormone alpha 2
- Neuropeptide F
Sequence:
MLRHLLRHENNKVFVLILLYCVLVSILKLCTAQPDSSVAATDNDITHLGDDCQVTPVIHVLQYPGCVPKPIPSFACVGRCASYIQVSGSKIWQMERSCMCCQESGEREAAVSLFCPKVKPGERKFKKVLTKAPLECMCRPCTSIEESGIIPQEIAGYSDEGPLNNHFRRIALQ
Protein: CTP synthase 2 (EC 6.3.4.2) (CTP synthetase 2) (UTP--ammonia ligase 2) (Q9NRF8)
Organism: Homo sapiens (Human)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides.
Interaction partners:
- CTP synthase 1
- Nucleoside diphosphate kinase, mitochondrial
- Nucleoside diphosphate kinase A
- Adenylate kinase 9
- Nucleoside diphosphate kinase 6
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase homolog 7
- Nucleoside diphosphate kinase B
- Bis
Sequence:
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQVICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Protein: Endoribonuclease HigB (EC 3.1.-.-) (Host inhibition of growth protein B) (Killer protein) (Toxin HigB) (mRNA interferase HigB) (Q7A225)
Organism: Proteus vulgaris
Function: Toxic component of a type II toxin-antitoxin (TA) system. A ribosome-associated translation-dependent mRNA interferase. Inhibits translation by sequence-specific cleavage of mRNA. Prefers either in-frame or out-of-frame 5'-AAA-3' codons (lysine). Cleaves also the first three AAAs of stretches of four or more A sequences. 20% of codons containing AA are cleaved and occassionally cuts even at a single A.
Interaction partners:
Sequence:
MIKSFKHKGLKLLFEKGVTSGVPAQDVDRINDRLQAIDTATEIGELNRQIYKLHPLKGDREGYWSITVRANWRITFQFINGDAYILNYEDYH