wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC 2.7.8.27) (Sphingomyelin synthase 2) (Sms2) (Q4JM44)
Organism: Rattus norvegicus (Rat)
Function: Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane (By similarity). Does not use free phosphorylcholine or CDP-choline as donors (By similarity). Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) (By similarity). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting (By similarity). To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1. Required for normal bone matrix mineralization (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein {ECO:0000255}. Note=Primarily localized at the plasma membrane with a small fraction at the Golgi apparatus. {ECO:0000250|UniProtKB:Q8NHU3}.
Interaction partners:
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase 3
- Ceramide kinase
- Ceramide synthase 4
- Ceramide synthase 2
- Ceramide glucosyltransferase
- Sphingolipid delta
- Ceramide synthase 3
Sequence:
MDIIETAKLEGHLESQTNNSTNTYTSPTEAVEEEDKNGKGKPKTLSNGLRKGAKKYPDYIQISMPNDSRNKLPLEWWKTGIAFVYALFNLILTTVMITVVHERVPPKELSPPLPDKFFDYVDRVKWAFSVSEINGMVLVGLWLTQWLFLRYKSIVGRRFFFIMGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKIQRILRLLSGGGLSITGSHILCGDFLFSGHTVVLTLTYLFIKEYSPRHFWWYHLVCWLLSAAGIICILVAHEHYTVDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGEDNEKST
Protein: Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (Nucleoside-2-P kinase) (Q59636)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. The 12-kDa membrane-associated form synthesizes GTP in preference to other nucleoside triphosphates. Important for alginate synthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:8606147}. Note=Ndk is predominantly cytoplasmic. The 12-kDa form is predominantly membrane-associated. {ECO:0000269|PubMed:8606147}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS14
Sequence:
MALQRTLSIIKPDAVSKNVIGEILTRFEKAGLRVVAAKMVQLSEREAGGFYAEHKERPFFKDLVSFMTSGPVVVQVLEGEDAIAKNRELMGATDPKKADAGTIRADFAVSIDENAVHGSDSEASAAREIAYFFAATEVCERIR
Protein: Cytochrome P450 3A12 (EC 1.14.14.1) (CYPIIIA12) (Cytochrome P450-PBD-1) (P24463)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2C21
- Cytochrome P450 family 7 subfamily A member 1
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDPGT domain-containing protein
- Cytochrome P450 2E1
- UDP-glucuronosyltransferase 2B31
- Cytochrome P450 2B11
- Cytochrome P450 family 2 subfamily J member 2
Sequence:
MDLIPSFSTETWLLLAISLVLLYLYGTYTHGIFRKLGIPGPTPLPFVGTALGYRNGFYVFDMKCFSKYGRMWGFYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRTLGPVGFMKSAISLSEDEEWKRMRTLLSPTFTTGKLKEMFPIIGQYGDVLVNNLRKEAEKGKAINLKDVFGAYSMDVITSTSFGVNIDSLNHPQDPFVENTKKLLKFDFLDPFFFSILLFPFLTPVFEILNIWLFPKKVTDFFRKSVERMKESRLKDKQKHRVDFLQLMINSQNSKEMDTHKALSDLELVAQSIIFIFAGYETTSTSLSFLMYELATHPDVQQKLQEEIDATFPNKALPTYDALVQMEYLDMVLNETLRLYPIAGRLERVCKKDVEISGVFIPKGTVVMVPTFTLHRDQSLWPEPEEFRPERFSRKNKDSINPYTYLPFGTGPRNCIGMRFAIMNMKLALVRVLQNFSFKPCKETQIPLKLNAQGIIQPEKPIVLKVEPRDGSVNGA
Protein: Serine/threonine-protein kinase AGC1-5 (EC 2.7.11.1) (AGC serine/threonine-protein kinase subfamily 1 member 5) (Q9LTW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions redudantly with AGC1-7 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
Interaction partners:
- Rac-like GTP-binding protein ARAC11
- Rho guanine nucleotide exchange factor 8
- Probable protein kinase At2g41970
- Probable LRR receptor-like serine/threonine-protein kinase At4g31250
- Rop guanine nucleotide exchange factor 3
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Pollen receptor-like kinase 2
- Rop guanine nucleotide exchange factor 1
Sequence:
MDLASKKNTANVGSKEIDPIKPKSPRSSLSPFSLKLGDNVPRNPHFDPKKMDPLVKHQPPKSLEPPPSTRGTNSEGDLKHNTYSSDGDSLAMRKNAPKNLHYDPKKIVPLTTSETYSPSARNHHHHRTKSPDKKRAPRHNGDYAYGDNLVGPSAQPFKPHTGGDVRWDAINSIASKGPQIGLDNFRLLKRLGYGDIGSVYLADLRGTNAVFAMKVMDKASLASRNKLLRAQTEREILSLLDHPFLPTLYSYFETDKFYCLVMEFCSGGNLHSLRQKQPSRRFTEEAARFYASEVLLALEYLHMLGVVYRDLKPENILVRDEGHIMLSDFDLSLRCTFNPTLVKSSSVCSGGGAILNEEFAVNGCMHPSAFLPRLLPSKKTRKAKSDSGLGGLSMPELMAEPTDVRSMSFVGTHEYLAPEIIRGEGHGSAVDWWTFGIFLYELLHGTTPFKGQGNRATLHNVVGQPLKFPDTPHVSSAARDLIRGLLVKDPHRRIAYTRGATEIKQHPFFEGVNWALVRSAAPPHIPDPVDLGPYAAARGKTKSHGGGDHCNSMKPEPLVACAAGPTDDTAYIDFEYF
Protein: Uncharacterized protein (Q57XT5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MELLGNASLEPQDLQSQQLQWEEEASGKETKVLQKPLPSSAQRELEAKLTEALAIVAADAATRFCEDMRRLWVMYFAHLQGKVREIFQKLHKAFDRFESSPDEETLADFLFLHRTMQPLLSELLGIHDAVVENGEEGKEKVECEEHVHNIGSNDGSACCSNNRDVALPPGTPLEKEHVLVQHLSLCIAEATTPVLAFTLCEMNKFVGVKMNGDTDRNEKELTREKGSSACGRTEQCAGLSNEEKEGILGDFSAERDLQPSRQQSESRDVMSEHSHVCADTARPSVDNSITPNIIHDLPIEDTIDVEIVDDGTSDCGGDVSSENGGQSDYYYHHYNPLMEAMSIEGDWGSSARPTSSPHADEATIRKKMSSVRTSRSAPTFIGTPCEAQIGHHYVDHTETYNGDGTHCGPWDGGSSDYKKGNAVRYSRSNSGVHLKPPAWRDDRTDSAGLMDEWEERDILTNRTLDPERRLQLLKGQEQLLLQSYPVNDERLWRREDGGEARCYALKKRLARLRSAILRGEREMEQLQRIKVERELIRQMRAEKERRLLEGRPSRGRIVHSI
Protein: Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP) (Q9QZE5)
Organism: Mus musculus (Mouse)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit zeta-1
- Coatomer subunit epsilon
- ADP-ribosylation factor GTPase-activating protein 2
- Coatomer subunit zeta-2
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Transmembrane emp24 domain-containing protein 10
Sequence:
MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMAEQRPESTATAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPARSLPYNQPGTCYTLVALPTEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG
Protein: Ubiquitin-like modifier-activating enzyme 5 (Ubiquitin-activating enzyme 5) (P91430)
Organism: Caenorhabditis elegans
Function: E1-like enzyme which activates ufm-1. Required for interaction between ufm-1 and ufc-1.
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- E3 UFM1-protein ligase 1 homolog
- Ufm1-specific protease
- DDRGK domain-containing protein 1
- E1 ubiquitin-activating enzyme
- RING-type domain-containing protein
- Molybdopterin synthase catalytic subunit
- NEDD8-conjugating enzyme ubc-12
- Ubiquitin-like protein NEDD8
Sequence:
MSDEQIDKLVSRLDGALNRLGNVKKDHPLESSSNSKPTHQPKSPAPYRQKIEKLSAEVVDSNPYSRLMALQRMGIVNEYERIREKTVAVVGVGGVGSVVAEMLTRCGIGKLILFDYDKVEIANMNRLFYQPNQAGLSKVEAARDTLIHVNPDVQIEVHNFNITTMDNFDTFVNRIRKGSLTDGKIDLVLSCVDNFEARMAVNMACNEENQIWMESGVSENAVSGHIQYIEPGKTACFACVPPLVVASGIDERTLKRDGVCAASLPTTMAVVAGFLVMNTLKYLLNFGEVSQYVGYNALSDFFPRDSIKPNPYCDDSHCLQRQKEYEEKVANQPVDLEVEVPEEETVVHEDNEWGIELVNESEPSAEQSSSLNAGTGLKFAYEPIKRDAQTELSPAQAATHDFMKSIKDKLVEEAQNKGK
Protein: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase (HQNO methyltransferase) (HQNO-MTase) (EC 2.1.1.374) (Heterocyclic toxin methyltransferase) (P9WKL5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs (Probable). Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ). Can also methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4-hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one. In addition, N-methylates and abolishes the mycobactericidal activity of 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile (compound 14), an inhibitor of DprE1. Also methylates and reduces the inhibitory effect of TPSA (2-[5-(2-{[4-(2-thienyl)-2-pyrimidinyl]sulfanyl}acetyl)-2-thienyl]acetic acid), an inhibitor of GlmU acetyltransferase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A5TZU0}.
Interaction partners:
- Uncharacterized protein Rv0559c
- Menaquinone reductase
- HTH-type transcriptional repressor Rv2887
- Conserved protein
- Possible transcriptional regulatory protein
- Probable transcriptional regulatory protein
Sequence:
MSTVLTYIRAVDIYEHMTESLDLEFESAYRGESVAFGEGVRPPWSIGEPQPELAALIVQGKFRGDVLDVGCGEAAISLALAERGHTTVGLDLSPAAVELARHEAAKRGLANASFEVADASSFTGYDGRFDTIVDSTLFHSMPVESREGYLQSIVRAAAPGASYFVLVFDRAAIPEGPINAVTEDELRAAVSKYWIIDEIKPARLYARFPAGFAGMPALLDIREEPNGLQSIGGWLLSAHLG
Protein: Uncharacterized protein C1734.10c (O74751)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized RING finger protein P8B7.15c
- Endoribonuclease ysh1
- Glucosamine 6-phosphate N-acetyltransferase
- tRNA-specific adenosine deaminase 1
- Uncharacterized protein C630.07c
- Small ribosomal subunit protein uS15
Sequence:
MLAEYLVHVGRVNVFLDPETKDIPKCVADLKFPLPLTLSRSTPINPIIRSDTIQLVISCPPVTYSDEIQVPWKAIDLNKDDAVKSTIKCKQCQSFLTSISSWKDLPSANWMEMLDCWSCHTDYPTVLSKRGGPSMFQPTDDCAYLGTSYVLIRLQSLEGKVAYGPNFKLHCSFCNAELGLPNNKDSSNGVRLDKSSICIDDQKIHPSFIVASEILTLRDMYATHKFVIVDGERSIWTWCFVPHLPISFQKSPFSSIEFANSPISTIKLLYQLEVPPDFTKSSEDWMDIPVSSHAFDEISHVLEKGNLSFPVSAQKFGPWKVGLLPKFHKQMI
Protein: Fibrinogen-like protein 1 (HP-041) (Hepassocin) (HPS) (Hepatocyte-derived fibrinogen-related protein 1) (HFREP-1) (Liver fibrinogen-related protein 1) (LFIRE-1) (Q08830)
Organism: Homo sapiens (Human)
Function: Immune suppressive molecule that inhibits antigen-specific T-cell activation by acting as a major ligand of LAG3. Responsible for LAG3 T-cell inhibitory function. Binds LAG3 independently from MHC class II (MHC-II). Secreted by, and promotes growth of, hepatocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:11470158, ECO:0000269|PubMed:30580966}. Note=Secreted in the blood plasma. {ECO:0000269|PubMed:30580966}.
Interaction partners:
- Lymphocyte activation gene 3 protein
- Fibrinogen gamma chain
- Fibrinogen alpha chain
- Fibrinogen beta chain
- Beta-2-glycoprotein 1
- Alpha-2-antiplasmin
- Thrombospondin-1
- Fibroleukin
- Fibronectin
Sequence:
MAKVFSFILVTTALTMGREISALEDCAQEQMRLRAQVRLLETRVKQQQVKIKQLLQENEVQFLDKGDENTVIDLGSKRQYADCSEIFNDGYKLSGFYKIKPLQSPAEFSVYCDMSDGGGWTVIQRRSDGSENFNRGWKDYENGFGNFVQKHGEYWLGNKNLHFLTTQEDYTLKIDLADFEKNSRYAQYKNFKVGDEKNFYELNIGEYSGTAGDSLAGNFHPEVQWWASHQRMKFSTWDRDHDNYEGNCAEEDQSGWWFNRCHSANLNGVYYSGPYTAKTDNGIVWYTWHGWWYSLKSVVMKIRPNDFIPNVI
Protein: Leptin receptor gene-related protein (Endospanin-1) (OB-R gene-related protein) (OB-RGRP) (O89013)
Organism: Mus musculus (Mouse)
Function: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18042720}; Multi-pass membrane protein {ECO:0000269|PubMed:18042720}. Endosome membrane {ECO:0000269|PubMed:18042720}.
Interaction partners:
- Transmembrane protein 50A
- Transmembrane protein 50B
Sequence:
MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLIFYVISPIPYFIAKRVTYDSDATSSACRELAYFFTTGIVVSAFGLPVVLARVDVIKWGACGLVLAGNAVIFLTIQGFFLVFGRGDDFSWEQW
Protein: Cytohesin 3a (Cytohesin-3) (E7F2Q0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor-like 4, like.
- ADP-ribosylation factor-like protein 4A
- FERM domain-containing protein 4A
- E3 ubiquitin-protein ligase UNKL isoform X1
- DMgamma1
- Par-3 family cell polarity regulator beta b.
Sequence:
MNMDEDNRVPEDLSFEERDELSNIRRRKRELLDDIERLKLEISEVMTEIEHLTCVRETKSTQRSKQIAVGRKKFNMDPKKGIQFLLENDLLQHTPEDIAQFLYKGEGLNKTVIGDYLGERDDFNIRVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAYAARYCQCNPGVFQSTDTCYVLSFSVIMLNTSLHNPNVRDKPSVERFISMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEEPRKPNCFELYNPSHKGQVIKACKTEADGKVVEGNHVVYRISAPTPEEKEEWIKSIKASISRDPFYDMLATRKRRVATKK
Protein: Complement component 6 (Q9QXT7)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTRHLTLCFILLVMLIDKSEACFCDHYPWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLCIKQETRECNLQTCPINCVLGDYGTWSDCDPCTEKQVKVKSVLRPSQFGGQPCTEPLVTFQPCVPSKLCKIEETNCKNKFLCDSGRCIPSKLECNGENDCGDNSDERNCGRTKPVCTRIYTPIPSVQLMGTGFHFLAGEPRGEVLDNSFTGGICKLVKTSRASNPYRVSANLENVNFEVQTIEDDLKTEFYKNLISFEKNKNEDSLSVDERTKFFPIPIFHFSEKNEHSHYSSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKATDLQLSDVFLKALVHLPLEYNSAVYSRIFDDFGTHYFTSGSLGGKYDLIYQFSRQELQNSGLTEEEAQNCVQYETKKLKFLYMEIHKEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSQQAAALAWEKGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLVRNIPCAVTKRNNLRRALQEYAAKFDPCQCAPCPNNGRPRLSGTECLCVCQSGTYGENCERRSPGYKSDAVDGNWGCWSSWSACNAAYRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVSIMENVGQPCINDDEEMTEVDLAEPEAESGCSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQRTSCLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDSWTPPISNSLTCEQGVRDHP
Protein: Chloroplast stem-loop binding protein of 41 kDa a, chloroplastic (CSP41-a) (Q9LYA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds and cleaves RNA, particularly in stem-loops. Associates with pre-ribosomal particles in chloroplasts, and participates in chloroplast ribosomal RNA metabolism, probably during the final steps of 23S rRNA maturation. May enhance transcription by the plastid-encoded polymerase and translation in plastid via the stabilization of ribosome assembly intermediates. Required for chloroplast integrity. Involved in the regulation of the circadian system.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:18431481}. Note=Present in stromules. {ECO:0000250}.
Interaction partners:
- Chloroplast stem-loop binding protein of 41 kDa b, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic
- Rho-N domain-containing protein 1
- Ribonuclease J
- Protein TRAUCO
- Protein RBL
- Multiple organellar RNA editing factor 1, mitochondrial
- NAD
- Ribonuclease E/G-like protein, chloroplastic
- ATP synthase subunit delta, chloroplastic
Sequence:
MAALSSSSLFFSSKTTSPISNLLIPPSLHRFSLPSSSSSFSSLSSSSSSSSSLLTFSLRTSRRLSPQKFTVKASSVGEKKNVLIVNTNSGGHAVIGFYFAKELLSAGHAVTILTVGDESSEKMKKPPFNRFSEIVSGGGKTVWGNPANVANVVGGETFDVVLDNNGKDLDTVRPVVDWAKSSGVKQFLFISSAGIYKSTEQPPHVEGDAVKADAGHVVVEKYLAETFGNWASFRPQYMIGSGNNKDCEEWFFDRIVRDRAVPIPGSGLQLTNISHVRDLSSMLTSAVANPEAASGNIFNCVSDRAVTLDGMAKLCAAAAGKTVEIVHYDPKAIGVDAKKAFLFRNMHFYAEPRAAKDLLGWESKTNLPEDLKERFEEYVKIGRDKKEIKFELDDKILEALKTPVAA
Protein: Probable Ufm1-specific protease 2 (UfSP2) (EC 3.4.22.-) (Q9VUR0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- E3 UFM1-protein ligase 1 homolog
- Ubiquitin-like modifier-activating enzyme 5
- Protein odr-4 homolog
Sequence:
MLPKLKISAFLLKRLERTKQQCSGCLFGVFYGEGTLLLLSFNIESSLGQLNYEQIQHRFPAELDLCGLVKFGGCTDGEAHLNEVIKSVDITDNPILLQCELGTLVGLRASFFVHGKLEEVPYEVMEAHQLYNDFCFTRLQCGFFLQTAATPESVAREMHVLRKRVADGNLVFNVPQTKIFINNYGPLDKQFSGDSQIQDLIDVIPTPGHEKETASVDKKKLKGQNTPVKRLAPTGCDYEVIPIDVMRSRSRDPVSGEPPHPALSIAVTNEEQIRVQVPLEIEAMAILCRKTKLQRLYDVLIESICRGLRLFELSLIEHLTESGSGKLLVPASYHFYPQEFGHFVSCAYLEGLSDDTPSMLMRRKRLHRQFALPISRPYFRRANQMLFLGETEDAPWTPLLNTHIGLRPSGVVDGKEYLVNGNYHYYHYLQQQVQDKGWGCAYRSLQTICSWFVLQGYTNAPIPTHLEVQEYLHKINDKPAAFVGSSQWIGSTEISMCLQGFLNVDSKILHVASGAELATIASELAMHFQTQGTPVMIGGGVLAHTIIGVDYCVQTGQVKFLILDPHYTGADDLATIQIKGWCGWKGMDFWAKGSYYNLCMPQRPILY
Protein: Cytochrome c oxidase subunit 7A, mitochondrial (Cytochrome c oxidase subunit VIIa) (Q9VHS2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P10174}; Single-pass membrane protein {ECO:0000250|UniProtKB:P10174}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5B, isoform A
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cyclope, isoform A
- Cytochrome c oxidase subunit 5B-like
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 8
- Levy, isoform A
- GEO09626p1
- Cytochrome c oxidase subunit 4
Sequence:
MMNLSRAVVRSFATTAGRRSAAVPKDQIEKGYFEIRKVQEHFQKKDGKPVFLKGSVVDNVLYRVTVALALVGIGGMGKLFYELSVPKKE
Protein: Keratin-associated protein 9-8 (Keratin-associated protein 9.8) (Ultrahigh sulfur keratin-associated protein 9.8) (Q9BYQ0)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 4-3
- Keratin-associated protein 17-1
- Keratin-associated protein 9-4
- Keratin-associated protein 9-3
- Keratin-associated protein 3-1
- Keratin-associated protein 4-1
- Keratin-associated protein 4-5
- Keratin-associated protein 1-1
- Keratin-associated protein 1-5
- Keratin-associated protein 4-8
Sequence:
MTHCCSPCCQPTCCRTTCWKPTTVTTCSSTPCCQPSCCVSSCCQPCCRPTCCQNTCCQPICVTSCCQPSCCSTPCCQPTCCGQTSCGSSCGQSSSCAPVYCRRTCYHPTTVCLPGCLNQSCGSNCCQPCCRPACCETTCCRTTCFQPTCVSSCCQPSCC
Protein: Receptor for gonadotropin-inhibitory hormone (Q5KSL3)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MQALRHQEPSGDTFNGSWDNASESQILKENYTFLAYYQHSSPVAVMFILAYTFIFLMCMIGNILVCFIVVKNRQMRTVTNMFILNLAISDLLVGIFCMPTTLVDNLITGWPFDNAMCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALVTIAIIWVLALLIMCPSAITLTVTREEHHFMLDTYNNSYPLYSCWEAWPETEMRKIYTTVLFSHIYVAPLALIVIMYARIAFKLFKSAAPARSTRPEEPEGRKVSRRKAKVINMLIIMALFFTLSWLPLWTLMLLTDYGHLSEHQLHLVTGYIFPFAHWLAFFNSSANPIIYGYFNENFRRGFQEAFRAPFWLPPCRQHRGPYGARNRVFTQPQASDSPPHSESRPLASRRAGIPAWNG