wanglab/gogpt-training-data huggingface dataset:
Protein: Conserved protein (O53356)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- NAD
- Glycerol-3-phosphate dehydrogenase 2
- RNA pseudouridylate synthase
- Possible esterase lipoprotein LpqC
Sequence:
MPLYAAYGSNMHPEQMLERAPHSPMAGTGWLPGWRLTFGGEDIGWEGALATVVEDPDSKVFVVLYDMTPADEKNLDRWEGSEFGIHQKIRCRVERISSDTTTDPVLAWLYVLDAWEGGLPSARYLGVMADAAEIAGAPSDYVHDLRTRPARNIGPGTIA
Protein: Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase (EC 2.1.1.-) (P9WIN3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the methylation of the lipid moiety of the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycoserosates to form phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL).
Interaction partners:
- Trans-acting enoyl reductase
- Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase
Sequence:
MAFSRTHSLLARAGSTSTYKRVWRYWYPLMTRGLGNDEIVFINWAYEEDPPMDLPLEASDEPNRAHINLYHRTATQVDLGGKQVLEVSCGHGGGASYLTRTLHPASYTGLDLNQAGIKLCKKRHRLPGLDFVRGDAENLPFDDESFDVVLNVEASHCYPHFRRFLAEVVRVLRPGGYFPYADLRPNNEIAAWEADLAATPLRQLSQRQINAEVLRGIGNNSQKSRDLVDRHLPAFLRFAGREFIGVQGTQLSRYLEGGELSYRMYCFTKD
Protein: Uridine nucleosidase (EC 3.2.2.3) (Uridine ribohydrolase) (Q04179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Also acts on cytidine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Purine nucleoside phosphorylase
- Uridine kinase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Cytidine deaminase
- IMP-specific 5'-nucleotidase 1
- Suppressor of disruption of TFIIS
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-dependent histone deacetylase SIR2
- Nicotinamide riboside kinase
- Nicotinamidase
Sequence:
MTVSKIPIWLDCDPGHDDAIAILLGCFHPAFNLLGISTCFGNAPPENTDYNARSLLTAMGKAQAIPVYKGAQRPWKREPHYAPDIHGISGLDGTSLLPKPTFEARTDKTYIEAIEEAILANNGEISFVSTGALTTLATVFRCKPYLKKSVKYISIMGGGLHGLGNCNPNLSAEFNVWIDPDAANYIFRDPDVKDKCIVVPLNLTHKAIATYKVNEMIYNEKNNSKLRELFLELFQFFAHTYKDMQGFESGPPIHDPVALMPLLEFYGWDPSSAVGFRYKRMDISCIDDVFNENSGKIIIEKEYPNDSDVGTIIGLDLNIQYFWDQIFEALNRADKMSTIG
Protein: LD36719p (Q960T1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRKYRVCNVTRRPAQMQSFPLQLENGQTVECTVAKYFLDKYRMKLRYPHLPCLQVGQEHKHTYLPLEVCNIVAGQRCIKKLTDMQTSTMIKATARSAPDREREINNLVKRADFNNDSYVQEFGLTISNSMMEVRGRVLPPPKLQYGGRVSTGLTGQQLFPPQNKVSLASPNQGVWDMRGKQFFTGVEIRIWAIACFAPQRTVREDALRNFTQQLQKISNDAGMPIIGQPCFCKYATGPDQVEPMFRYLKITFPGLQLVVVVLPGKTPVYAEVKRVGDTVLGMATQCVQAKNVNKTSPQTLSNLCLKINVKLGGINSILVPSIRPKVFNEPVIFLGADVTHPPAGDNKKPSIAAVVGSMDAHPSRYAATVRVQQHRQEIIQELSSMVRELLIMFYKSTGGYKPHRIILYRDGVSEGQFPHVLQHELTAIREACIKLEPEYRPGITFIVVQKRHHTRLFCAEKKEQSGKSGNIPAGTTVDVGITHPTEFDFYLCSHQGIQGTSRPSHYHVLWDDNHFDSDELQCLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVEKEHDSGEGSHQSGCSEDRTPGAMARAITVHADTKKVMYFA
Protein: Sodium/glucose cotransporter 1 (Na(+)/glucose cotransporter 1) (High affinity sodium-glucose cotransporter) (Solute carrier family 5 member 1) (P13866)
Organism: Homo sapiens (Human)
Function: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump. Has a primary role in the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception. Acts as a water channel enabling passive water transport across the plasma membrane in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity, comparable to aquaporins, and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:26945065}; Multi-pass membrane protein {ECO:0000269|PubMed:34880492, ECO:0000269|PubMed:37217492}.
Interaction partners:
- Epidermal growth factor receptor
- Taste receptor type 1 member 3
- Taste receptor type 1 member 2
- PDZK1-interacting protein 1
- Solute carrier family 2, facilitated glucose transporter member 2
- Guanine nucleotide-binding protein G
- Solute carrier family 2, facilitated glucose transporter member 1
- Solute carrier family 2, facilitated glucose transporter member 5
- Pro-glucagon
- Regulatory solute carrier protein family 1 member 1
Sequence:
MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMPMFIMVMPGMISRILYTEKIACVVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYAKVRKRASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFWKRVNEPGAFWGLILGLLIGISRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFAISFITIVVISLLTKPIPDVHLYRLCWSLRNSKEERIDLDAEEENIQEGPKETIEIETQVPEKKKGIFRRAYDLFCGLEQHGAPKMTEEEEKAMKMKMTDTSEKPLWRTVLNVNGIILVTVAVFCHAYFA
Protein: Tumor protein p53 binding protein 1 S homeolog (p53-binding protein 1) (Q98U15)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPSRNPLDPDFSQQDTPCLIVEDSQPESGVAEDVMDRARFGLLAHHLPDLQAPVESPVLEFVPGCQSIKHAAADKEGLNFCESLNENNLETSRMPDTDDALSQVIERVTCPSNIKSRLECDHDHDQERDAECTTQSLQPEDSGTSQLGFGALELSQSQDLEGHSSYNKDASRLQLQITHPTSQCNQEDCCDSGEVLKDTPAKNTFEKDPERKQEKVVEDKTSSDSSGEKICLAANVDIDMDLQKGSPVKHDDEYKERSGCLQTKEQDMEGSDIPSTQEDLFGQEDVTDSQTHPLTYKVVSTPPADSLRLLHPSGQASLLPGNASKIFSDLVSPSQDAVQPTPIIIPSSPTEQEAENAEVIEKTTPKYDLKRKLQEEPNEPKDSSFLTVPQVSTPLCQSVPAFVPSSFVVPSQPDLSHDNFMATPSLETNLSRDKTKTPVFPDDEKPKEPELIQEVTELDSMISQSMTGDLSNLELSTSEPSEVTDTDYKKDAEDENRATQIEEDVGHGCQLLKNAKESVAVINIDLKKENTTVSKMSMAAVMEETSISIKESTTVSSATVETKMGNNRPECIDLTYDSASQVVLIPSLNSDSSLSILDQNVMEAKLNLTAESQPDASIEEVPETPCDNRVAEDQTMEEGTNLNLALSETQTQHLNVLDVEQSEPEEEPMEVESCAGSSEVSSRKTMNVSHPVPILFNIAQQSGKSECNTDNIDKQIETDHSKVALEKAKRQEDQTVLGEHFDKKRNTEDLKSDYSKPVILFAPLLSASLDEGNVPLAPKKIHISIGEKEDAVHFISNVCQSVAQEQQVAVVGNNPDINLVQNNSKILPVPLENNKCTHSGMQKEKVVPITLEGKTDFAVFPVENKLKQMPQDKCNECFKVQLGDGSQALPSLEVTECSAQMKENIIVSDDLQLNKQQNVEVVEESENVSGIIDDTQQQPPTLKVLANDMRPLEERKQECIEKTISVAKWSDHIESPVLEGNKNEELGILQKCEPQIREEINYPQPSHGENFDTTTHKSEKLLSQQIADDVPQLIQTSTREVNISVDNSAEEAREADSTLQEKTVEQSTHSLCDSSSETPFHFTLPKEGDLIQPISTVTPPMVAQLKRGPRRHSTPIVVGGCPDSTLATSDVTAESTSDITVESAMVTTDVSEASERANSESASNVNEKLCLRMKLITPVNEESEGAPQFNLEKPDAAKRPKEAADVAVNVASVPESTSVFERVCEAHEEEVCPTTSLREKSFQNKEVDEMSAGVNTVLQNVKDTGEHDTNSQTTQNLPEEPIQEHSSSLEDDDMEVEPSQEENIFCVQPDRGKKSELKPTDTASTQNKYGDENMTSSHRHKEVQTASVLEPRMLVVSSATQTDVETGQRTVTSNGQKNVKQDSSKATEKDQEKSENVTKSMQGDDTDSVHSQGEEDFNLQHPPLGRQLHRHVRTIREVRTVVTRVITDVYYVNGTEVERKVVEEAEDPIIECHEYENDVSSSRTAGSSLTSGDLADISSFSSKASSLQRTSSGASSGLSAAQSISGSSTEKGKVYATQRGKSGLLESGEFAVPSGRGTFGKLSPRKVASQPVSPHRSGGQIGVQGSEDDADISPGNRSKATLTPRGRGRRGRPPARGAGTRDNTANTNMEDPADATSDEERFTRLNVYHPGAERSEPGTPTVRRSDSPEIPFRAAAKNESSDSSGSSFVGLRVVAKWSSNGYFYSGKITQDAGGGKYKLLFDDGYECDVLGKDILLCDPIPLDSEVTALSDDEYFSAGVVKAHKKDSEELYYCIERILEWHESRHPFQGMRFLVVSGKRKLISSDEDKSPAKRGRKSVLAKAGAAKGGDFMSPSESGDNDGDQVMVEETHGPLPQSKSIFMGYAFLITSATSSDKQNNRQKSQAFPCISSEEEEEYIENMPYDRKYTEKQLQAGGGYILEDFNEAQCKAAYQCILIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANELQNFRNYLLPAGYSLQEEKILEWHDSQHPFQDLRFLVVSDQKENFLEMWTEILMIGGAASAKQHNSTELKKDNALGIFDVVVTDGSCPESMLKCAQALDLPVVSQEWVIQCLISGKQLKHNTHPKYKHNHVSD
Protein: Protein transport protein Sec31A (ABP125) (ABP130) (SEC31-like protein 1) (SEC31-related protein A) (Web1-like protein) (O94979)
Organism: Homo sapiens (Human)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10788476, ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27716508}; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:17428803}. Note=Associates with membranes in a GTP-dependent manner (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:17428803, PubMed:25201882, PubMed:28442536). {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
Interaction partners:
- Programmed cell death protein 6
- Protein transport protein Sec23B
- Protein transport protein Sec23A
- Protein SEC13 homolog
- Protein transport protein Sec24B
- Small COPII coat GTPase SAR1A
- Protein transport protein Sec24A
- Protein transport protein Sec24C
- Small COPII coat GTPase SAR1B
- Protein transport protein Sec24D
Sequence:
MKLKEVDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPYKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQNDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRISVYSIMGGSTDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTAQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVRMPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKKIDASQTEFEKNVWSFLKVNFEDDSRGKYLELLGYRKEDLGKKIALALNKVDGANVALKDSDQVAQSDGEESPAAEEQLLGEHIKEEKEESEFLPSSGGTFNISVSGDIDGLITQALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLARTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGTRLENEGDSLLQTQACLCYICAGNVEKLVACWTKAQDGSHPLSLQDLIEKVVILRKAVQLTQAMDTSTVGVLLAAKMSQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPASQRTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYDKLREQTLSPTITSGLHNIARSIETRNYSEGLTMHTHIVSTSNFSETSAFMPVLKVVLTQANKLGV
Protein: Eukaryotic translation initiation factor 4E, putative (Q383A4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable eukaryotic initiation factor 4A
- MIF4G domain-containing protein
- MIF4G domain-containing protein
- MIF4G domain-containing protein
- MIF4G domain-containing protein
- MIF4G domain-containing protein
Sequence:
MNPEAEEFVPKGNRTPGSGGRRGNGGGSRQIPVRGERQQPPPPPPPPQQQQQQVAPSSQTTLRASAEPFQPKGSQGFGLVGQVLPYVAGPPGGVPQAWESVEPVPPLSVWKSDSVQQAGAKPLSLSATPYTPTNPKISSKFPATPEAQRGPSTEFKDTTPASLQPQEKEVVEVGEKAVAIASPPEEDAVAANGGSVDASGAPSTQNFTVGEIVENDFSGSMLPSLFQVEVLDKPAPAEPVRFNTVWALYADEHPTPFGAPLAYHPVLVHLVGDVECFWRLWRHLPPPSTLLPAFTYHWFRRDIRPNWEHTRNKNGGTITFVIFDRDKPGLNNKQTMDDAFMAMLMACSGESLAESTTNLNGVMLKVRQNKPTTLQIWTASSDELKLRSLARSLRTLLEKVIGPKPLQKLEYFSHQRTQVGAPGSLAGRMKGKPSRITPDFTL
Protein: Ecdysteroid-phosphate phosphatase (EPPase) (EC 3.1.3.-) (EC 3.1.3.48) (Q7YTB0)
Organism: Bombyx mori (Silk moth)
Function: Steroid phosphatase which catalyzes the conversion of inactive phosphorylated ecdysteroids into their active forms. Shows high activity towards ecdysone 22-phosphate (E22P). Has lower activity towards other ecdysteriod phosphates including 20-hydroxyecdysone 22-phosphate (20E22P) and 2-deoxyecdysone 22-phosphate (2dE22P). Also has protein tyrosine phosphatase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12721294, ECO:0000269|PubMed:15738639}. Note=In 72 hr non-diapause eggs, detected mainly in the cystol surrounding the nucleus of yolk cells. {ECO:0000269|PubMed:15738639}.
Interaction partners:
Sequence:
MANLPPRKVTSASKSKQDVSPLQILLQMGFRRQRALKALAATGNRSVQLASDWLLTHVSDSNIDADDPREYIFYASPTGPLLSQLLEFWDKSKSTCGWNGAHNFLPHITLVSFFKAPDDTSLNLAKAVRQVVENVGDPPKCTLKLEPYVSHNFMGLFISEEHAEYLKKIAVQYVKQVSSVSSINLEAHVKSLHITLAYHFEESSYEDLKTLVEEMQPVEHSSWELRLYSRDPRFANHQVYKVTQGYSPQASDELELVLGDYIYIEEKEFDISPDGWVHGTSWLTGLNGYLPAVYTRRTAETDAWTLLKAVSLGNNCSDCKSESGSNTDSEMAGTYPHEDAADLAYKKSEETYQEWDKYWSEVMNSRSDSILTITQGLPMNWELSKAAEEMKNNITNGTSKSRRWVFALRHGERVDLTYGPWVPHCFENDTYVRKDLNLPLKLAHRAGGKGGYVKDTPLTRLGWFQAQLVGEGMRMAGVSIKHVYASPALRCVETAQGFLDGLRADPSVKIKVEPGLFEFKNWHMPKGIDFMTPIELCKAGLNVDMTYKPYVEMDASAETMDEFFKRGEVAMQAAVNDTEKDGGNVIFIGHAITLDQMVGALHRLRDDMEDVQPYEIGRNLLKVPYCALGAMRGKPWDVVSPPCPPSINSSSGRFDWRILIK
Protein: SAP domain-containing protein (Q4FKQ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein phosphatase 2C, putative
- Tyrosine phosphatase
Sequence:
MRKPGRKIVYVPDDDAQFLGSMSDPLPPRVSDLLRLKSPSMSDNGHAETGSNGTTGSPGYESIGNELLVSYGGYTLADGSGTLHPPTTRRNGAQLYKSLRKCCRFLRASLSDSMAPKLETDSESSWSCPSFCSSDPTSSSEYSDVSPQRGRRRAAKQANEQTGYNAMIVVQLRRLLHKRGLSTCGIKKVLVARLEQSDMQLSKSKEEGEEQKEQEELDGSAGECTKTERSEDVCSASCGNVSGRVTAAGPTSMLSSLLSFGSRLFRASTGSVSEGGHVSGLKRRRSV
Protein: Acetylcholinesterase (AChE) (EC 3.1.1.7) (P22303)
Organism: Homo sapiens (Human)
Function: Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis.
Subcellular location: Synapse {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1748670}. Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform T]: Nucleus. Note=Only observed in apoptotic nuclei.; SUBCELLULAR LOCATION: [Isoform H]: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.
Interaction partners:
- Acetylcholinesterase collagenic tail peptide
- Amyloid-beta precursor protein
- Choline O-acetyltransferase
- Glycerophosphocholine phosphodiesterase GPCPD1
- Choline kinase alpha
- Amine oxidase [flavin-containing] B
- Choline/ethanolamine kinase
- Phosphoethanolamine/phosphocholine phosphatase
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Protein Dok-7
Sequence:
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL
Protein: Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (Macrophage NOS) (MAC-NOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) (P29477)
Organism: Mus musculus (Mouse)
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity). Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}.
Interaction partners:
- Calmodulin-4
- Calmodulin-1
- Calmodulin 5
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Arginase-1
- Arginase-2, mitochondrial
- RAC-alpha serine/threonine-protein kinase
- Argininosuccinate lyase
- Argininosuccinate synthase
Sequence:
MACPWKFLFKVKSYQSDLKEEKDINNNVKKTPCAVLSPTIQDDPKSHQNGSPQLLTGTAQNVPESLDKLHVTSTRPQYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYYQIEPWKTHIWQNEKLRPRRREIRFRVLVKVVFFASMLMRKVMASRVRATVLFATETGKSEALARDLATLFSYAFNTKVVCMDQYKASTLEEEQLLLVVTSTFGNGDCPSNGQTLKKSLFMLRELNHTFRYAVFGLGSSMYPQFCAFAHDIDQKLSHLGASQLAPTGEGDELSGQEDAFRSWAVQTFRAACETFDVRSKHHIQIPKRFTSNATWEPQQYRLIQSPEPLDLNRALSSIHAKNVFTMRLKSQQNLQSEKSSRTTLLVQLTFEGSRGPSYLPGEHLGIFPGNQTALVQGILERVVDCPTPHQTVCLEVLDESGSYWVKDKRLPPCSLSQALTYFLDITTPPTQLQLHKLARFATDETDRQRLEALCQPSEYNDWKFSNNPTFLEVLEEFPSLHVPAAFLLSQLPILKPRYYSISSSQDHTPSEVHLTVAVVTYRTRDGQGPLHHGVCSTWIRNLKPQDPVPCFVRSVSGFQLPEDPSQPCILIGPGTGIAPFRSFWQQRLHDSQHKGLKGGRMSLVFGCRHPEEDHLYQEEMQEMVRKRVLFQVHTGYSRLPGKPKVYVQDILQKQLANEVLSVLHGEQGHLYICGDVRMARDVATTLKKLVATKLNLSEEQVEDYFFQLKSQKRYHEDIFGAVFSYGAKKGSALEEPKATRL
Protein: Cyclin 5 (Q8IEW5)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MTLSVDTAIGDTAICMERSCDAPTPTYAVKTRAMVLSGGSGCTLSRCRRLGRSARQRSPSNKRFSGRMSAASVTPSGGPVMDRSGTGYVDVCRGGECAPMLCRSGGCDHGVSIFAAAATPAAAVPLLDGTVAAECTNGAGGMPADGSRCVTQLYDAGASLRNESGRRYRNNYSCHYSNSGGSGYCCCSASYRGQKGHKGGQSQVFHNSPLFMGNGGNLPPNRGVISNYHYHHHPPCGASHHHHQRCAVRSHRRRGFGAAAVEAIRSRFQAGATMSHHAPPLSAVKCNRQTKQTASNGDQEPRQAFQVPLPRSKAAAGVTQPSATSCDAGVVRPSKGDFRIEMDTPFSATDSMNDPVNGSSRLSGIAPLFDLAIQQLILECDRRVANASGTACASAHSPSNSCNSQKQSSAHFSVNTHSFDMPTASHTKTTFAQTPKESSFATFAVEQAPLEGGQLESPHRDAEAEVMARDGACTTKLHRVEPRLEERVTARRENHVGNVVGRLFRDQSEDAVDLGSDCSKLQLLIVSVGLTVSFGESAPLVLIGTLIYLFRIVKRCDSEYSSVTAANWYRLTAVALLVATKMYVDGSGSWNECFSNATDIPLKELNKLEIDFLFLLDFDALITEEEVEARADWMDSVASRHDMMTPLRTFVLGSSCAPSCVATPLSPAADEAFRSVPLGSSSNMPSTPLSLTPSNMTPVNCFSTPFTQSRPIRNQCVGSLVSGVDASDKQQQQTRPSSMRRLSSSLCPCDRMSPLPLSVSSLSLTERLFSVVHAPAEPETPPSLRRFARQDDEPVSPLTPPDQERMSPVFFFCNATRGRRCNAMAAVGEKTNKTSPAGSAVQYRVSAGVAGDAWKGDEMDEEGGTPPHPRRCILSPPTQEAAPLPPLGMTDFHHRLPRK
Protein: Surfactant-associated protein 3 (Surfactant-associated protein H) (SP-H) (P0C7M3)
Organism: Homo sapiens (Human)
Function: Putative surfactant protein. May be involved in wound healing and in the reduction of the surface tension at the ocular surface.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24743970, ECO:0000269|PubMed:29955092}. Secreted {ECO:0000269|PubMed:24743970, ECO:0000269|PubMed:29955092}.
Interaction partners:
- Homeobox protein Nkx-2.1
- Lysosomal acid glucosylceramidase
- Pulmonary surfactant-associated protein B
- Pulmonary surfactant-associated protein A1
Sequence:
MRAGFSDFQLIRDQVLFLQDQAQRLTEWLQLSGFENPVSESTTLCLREREKRIPTCVAVCVPSPGTVHTALLHPTTLSQSRSSSEAKMLIIHTA
Protein: Chromatin-remodeling ATPase INO80 (EC 3.6.4.-) (F4J277)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368001}.
Interaction partners:
Sequence:
MDPSRRPPKDSPYANLFDLEPLMKFRIPKPEDEVDYYGSSSQDESRSTQGGVVANYSNGSKSRMNASSKKRKRWTEAEDAEDDDDLYNQHVTEEHYRSMLGEHVQKFKNRSKETQGNPPHLMGFPVLKSNVGSYRGRKPGNDYHGRFYDMDNSPNFAADVTPHRRGSYHDRDITPKIAYEPSYLDIGDGVIYKIPPSYDKLVASLNLPSFSDIHVEEFYLKGTLDLRSLAELMASDKRSGVRSRNGMGEPRPQYESLQARMKALSPSNSTPNFSLKVSEAAMNSAIPEGSAGSTARTILSEGGVLQVHYVKILEKGDTYEIVKRSLPKKLKAKNDPAVIEKTERDKIRKAWINIVRRDIAKHHRIFTTFHRKLSIDAKRFADGCQREVRMKVGRSYKIPRTAPIRTRKISRDMLLFWKRYDKQMAEERKKQEKEAAEAFKREQEQRESKRQQQRLNFLIKQTELYSHFMQNKTDSNPSEALPIGDENPIDEVLPETSAAEPSEVEDPEEAELKEKVLRAAQDAVSKQKQITDAFDTEYMKLRQTSEMEGPLNDISVSGSSNIDLHNPSTMPVTSTVQTPELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLPYWGGLQERTILRKNINPKRVMFFSTWIISFDPWAVRQICICKRACNVVRFQTLSDMDAGFHILITSYQLLVTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEHGGTLNEHQLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIKNKISLAELFDSNRGQFTDKKVLNLMNIVIQLRKVCNHPELFERNEGSSYLYFGVTSNSLLPHPFGELEDVHYSGGQNPIIYKIPKLLHQEVLQNSETFCSSVGRGISRESFLKHFNIYSPEYILKSIFPSDSGVDQVVSGSGAFGFSRLMDLSPSEVGYLALCSVAERLLFSILRWERQFLDELVNSLMESKDGDLSDNNIERVKTKAVTRMLLMPSKVETNFQKRRLSTGPTRPSFEALVISHQDRFLSSIKLLHSAYTYIPKARAPPVSIHCSDRNSAYRVTEELHQPWLKRLLIGFARTSEANGPRKPNSFPHPLIQEIDSELPVVQPALQLTHRIFGSCPPMQSFDPAKLLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQHRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKETVEEKILHRASQKNTVQQLVMTGGHVQGDDFLGAADVVSLLMDDAEAAQLEQKFRELPLQVKDRQKKKTKRIRIDAEGDATLEELEDVDRQDNGQEPLEEPEKPKSSNKKRRAASNPKARAPQKAKEEANGEDTPQRTKRVKRQTKSINESLEPVFSASVTESNKGFDPSSSAN
Protein: Melectin (MEP) (P86170)
Organism: Melecta albifrons (Cuckoo bee) (Melecta punctata)
Function: Antimicrobial activity against the Gram-positive bacteria B.subtilis (MIC=0.8 uM) and S.aureus (MIC=6.8 uM), and against the Gram-negative bacteria E.coli (MIC=2.0 uM) and P.aeruginosa (MIC=18.5 uM). Stimulates degranulation from rat peritoneal mast cells with an EC(50) of 19.4 uM. Has very weak hemolytic activity towards rat erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:18942691}.
Interaction partners:
Sequence:
GFLSILKKVLPKVMAHMK
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (A0A0H2UPM2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MYQALYRKYRSQNFSQLVGQEVVAKTLKQAVEQEKISHAYLFSGPRGTGKTSVAKIFAKAMNCPNQVGGEPCNNCYICQAVTDGSLEDVIEMDAASNNGVDEIREIRDKSTYAPSLARYKVYIIDEVHMLSTGAFNALLKTLEEPTQNVVFILATTELHKIPATILSRVQRFEFKSIKTQDIKEHIHYILEKENISSEPEAVEIIARRAEGGMRDALSILDQALSLTQGNELTTAISEEITGTISLSALDDYVAALSQQDVPKALSCLNLLFDNGKSMTRFVTDLLHYLRDLLIVQTGGANTHHSSVFVENLALPQKNLFEMIRLATVSLADIKSSLQPKIYAEMMTVRLAEIKSEPALSGAVENEIATLRQEVARLKQELSNVGAVPKQVAPAPSRPATGKTVYRVDRNKVQSILQEAVENPDLARQNLIRLQNAWGEVIESLGGPDKALLVGSQPVAANEHHAILAFESNFNAGQTMKRDNLNTMFGNILSQAAGFSPEILAISMEEWKEVRAAFSAKAKSSQTEKEVEESLIPEGFEFLADKVKVEED
Protein: Serine/threonine-protein kinase ppk23 (EC 2.7.11.1) (O60145)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized cyclin-L1-like protein C1296.05c
Sequence:
MAGSKWETEETNQFAIENQKLEEEWRKKRRLEKKRKRKILEEEEKAEERNIDACRLYLMGNTPELKSCNSIDDYEILEKIEEGSYGIVYRGLDKSTNTLVALKKIKFDPNGIGFPITSLREIESLSSIRHDNIVELEKVVVGKDLKDVYLVMEFMEHDLKTLLDNMPEDFLQSEVKTLMLQLLAATAFMHHHWYLHRDLKPSNLLMNNTGEIKLADFGLARPVSEPKSSLTRLVVTLWYRAPELLLGAPSYGKEIDMWSIGCIFAEMITRTPLFSGKSELDQLYKIFNLLGYPTREEWPQYFLLPYANKIKHPTVPTHSKIRTSIPNLTGNAYDLLNRLLSLNPAKRISAKEALEHPYFYESPRPKDPKFFPTFPSKAKGESKEKNVFQSFRSASPKK
Protein: carboxylesterase (EC 3.1.1.1) (Q95U30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMSKESLETCELTLPVGQIKGVKRLSLYDDPYFSFEKIPFAKPPLGELRFRAPVPADPWSGVLDCTHYAEKPTQRGLLTREIEGGEDCLYLNVYSKQLKSEKPLPVMVYIYGGAFTVGEATRELYGPDYFMTKDVVLVTLNYRVDCLGFLSLKDPSLKVPGNAGLKDQVLALKWVKQYISNFNGDDSNITVFGESAGGCSTHFMMCTEQTRGLFHKAIPMSGTVHNYWANNPAEDFAFRLAQQNGFTGENDDAKVLEYLQGVPARDLVNHNLLTPEHRRNGLLFAFGPTVEAYVGEDCVVPKPPVEMARDAWSNNFPVMLGGTSFEGLFMYPAVSANLKALDSLSQDPTRLVPVDVRTVSSEKENLEYSQRLMKAYFGYSPPSSELLLNMLDFYSYKIFWHGFNRTFNARLTYAKAPTYYYRFDFDSPNFNFYRAKFCGDKIKTGVAHADDLSYLFRNAGSWKLDKTSAEYRTIERMIGIWTAFAATSNPNCPEIGHLEWKPSTKNDPKRVINISSDVTIIDLPEYEKLQIWDNLYKPNQLI