wanglab/gogpt-training-data huggingface dataset:
Protein: Carboxylesterase 1D (Carboxyesterase ES-10) (Carboxylesterase 3) (EC 3.1.1.1, EC 3.1.1.67) (ES-HVEL) (Fatty acid ethyl ester synthase) (FAEE synthase) (Liver carboxylesterase 10) (pI 6.1 esterase) (P16303)
Organism: Rattus norvegicus (Rat)
Function: Major lipase in white adipose tissue (By similarity). Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. Hydrolyzes retinyl esters.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8VCT4}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VCT4}. Lipid droplet {ECO:0000250|UniProtKB:Q8VCT4}. Microsome {ECO:0000269|PubMed:12230550}.
Interaction partners:
- Cytochrome P450 2E1
- Arylamine N-acetyltransferase 2
- Carboxylesterase 1C
- Arylamine N-acetyltransferase 1
- Beta-glucuronidase
- arylamine N-acetyltransferase
- Cytidine deaminase
- Carboxylic ester hydrolase
- UDP-glucuronosyltransferase 2B1
- UDP-glucuronosyltransferase
Sequence:
MRLYPLVWLFLAACTAWGYPSSPPVVNTVKGKVLGKYVNLEGFAQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWNFVKNTTSYPPMCSQDAVGGQVLSELFTNRKENIPLQFSEDCLYLNVYTPADLTKNSRLPVMVWIHGGGLVVGGASTYDGQVLSAHENVVVVTIQYRLGIWGFFSTGDEHSQGNWGHLDQVAALHWVQDNIANFGGNPGSVTIFGESAGGFSVSALVLSPLAKNLFHRAISESGVVLTSALITTDSKPIANLIATLSGCKTTTSAVMVHCLRQKTEDELLETSLKLNLFKLDLLGNPKESYPFLPTVIDGVVLPKTPEEILAEKSFNTVPYIVGINKQEFGWIIPTLMGYPLSEGKLDQKTAKSLLWKSYPTLKISEKMIPVVAEKYFGGTDDPAKRKDLFQDLVADVMFGVPSVMVSRSHRDAGAPTFMYEFEYRPSFVSAMRPKTVIGDHGDELFSVFGSPFLKDGASEEETNLSKMVMKYWANFARNGNPNGGGLPHWPEYDQKEGYLKIGASTQAAQRLKDKEVAFWSELRAKEAAEEPSHWKHVEL
Protein: Protein muscleblind (Protein mindmelt) (O16011)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for terminal differentiation of photoreceptor cells. Vital for embryonic development.
Subcellular location: Nucleus {ECO:0000269|PubMed:9334280}.
Interaction partners:
- CCHC-type zinc finger nucleic acid binding protein
- Bruno 3, isoform A
- Purine-rich binding protein-alpha, isoform B
- TAR DNA-binding protein 43
- Double-stranded RNA-specific editase Adar
Sequence:
MANVVNMNSLLNGKDSRWLQLEVCREFQRNKCSRQDTECKFAHPPANVEVQNGKVTACYDSIKGRCNRDKPPCKYFHPPQHLKDQLLINGRNHLALKNALMQQMGIAPGQPVISGQVPAVATNPYLTGIPANSYSPYYTTGHLVPALLGPDPVTSQLGPVVPQTVQVAQQKIPRSDRLETSPLAAHHHQQQQQLQHQLNNINNNNNHSTAGAAATSTTATTTTNNAAAAAAAAAAAAAAAVMGHHTLEVGKKRAADTTDMFPLVFFCSFPSPCVFAFLNCSIFGFLRLWFSLFNLRH
Protein: Zormin, isoform G (Q0E8J4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MERRQALDSSMSSLYSVASSSNPNPRQPHTGHQLQTQQSQQSQQSQLDAFNYSATMSSSSPTPSQAMSTAMSTGTGTGTGTTHTTPPSSSSLRATTIGTVVVRCGPIQLVIALLQSPEKIYIKVVELEPKITALGENLDESLRMQREHDETLRNLQSLPGPMDEFVQKADKLLASKRISSELVNAMADTLNIIWQDILNLLQDRQHLLILCTQFHDKMTQCFRKMDQLELACEETLHPPDVPRVQEFLNRFKQLRIDMLTGVMAALKDGNELLAQLEELEKLETLDTRPEHIKRDATRAVHQVQQWLEALHDRRNSLELAWQTRKIQMEQCLALALLGRELVDLEAALQQARMELNTMYSLGECEHTANEMLTKYREWKQQALLLRDRALKITRAKEKVQSAGHFTEEDACARAYAVLSGCTEHLDLVDQREHWLHQSREFFAKAEHTVSVLEKLELELTSVKLPPHSPESYAMFSKVDRDVRNFTEEPLRLGYGILDEVGRTQPETQGVKRVLDELENRKVYIQGICANSSEDQQKVQRALSEFLNHHNELLAWLRASGQHQLQQSVDMGGNLQQAKQFLLQHHELMQDLEIKGELINLLLESIKVHLESLSPQERYDVDSKAESLHKHWIELKDLVLKRVDYVSLLIDFFELANELSSQLDNLQRQLQQTPDEHKLQFLQATWTGIASTFGELKSRGQRFINLKIVDPYLETKSSAQAVQETLNDFSKRQVDVTSSLENWTTSIAEKREVEYLLEKVMSDNEETVAKSTQVDTQLYPVFTSQSVDSKQLLISTREKLTNVIQDIERAQDEIQQRIQTTLGIQTKDQPSLAKIEQVINNLRMLKAKLDGIKYDYRTLVESVIQFLENIVQLRREIDDYFARQQKEPASGADRSIAEHEKFRDQCMDKFRSLITQSELLIDRVRVLEPPGAREIDTDRILKLLENLRLHFESNSSARMSTLERLEKIEQFRSDLEDIDRSLDSVSQQLHEINNQSVDSLAAAKTTSLAFEYFERTIELLEKRIEKFTESTSQQLFITNPESERYVKDELRKLNEKWQSFKDQVKQKRKSLNQATDFFEVVEKIDAEYREISYFYTSVSNKVPYLRDSVEAGNLVNDIENYVTSREAALRSKLDSASQCAHDMNKVSSLYNDVMNIFQSFIKLKMDINVVQERLKQEQRQKEQRERDARDQAEREKAIKEAEAKERLHREEQSRLENQRQQAAIEQAQRELAARELALREQAVREEEARLQAIREQATREQLAREQAAREEELRIQSLRDIARREEEVRLQNIRDEETRIRREEEERIRRENESRSKREEEARIQREEITRLQTLRDQVDQQRIVTENIRKDIQVNSIFTELRYASPLFTRPLKDAVSREGDRFVFECEVTGTPEPAVEWFKDGISIQTNSDYKTTFDKGICRLVIEETFAADSARFSCRASNLVGTCDTNATLSVRENAAEVQLVPPRILRFLQSGKATEGSSFQFACVVAGVPLPTVQWFKNDKCIDDSPDYVISYNNGEATLKFEEVFLEDDAVYTCSASNPAGIEHCSASLIVEPLEPTELPSFKVPLSNAMARVGQKIKLEAIVGGIPRPEVYWLHNGKPFQPRDSKYEYGRVTLIIPQAYPNDAGSYVLSAKNLAGEAYTSCNVIVKGRLPNETSDSEMASDIEPIKPAVHLPLKDVSIFEGKPVRLDCVIVGQPEPEVIWYHNERPVKESADVQLLFQGDRCSLIIQEVYQEDAGHYKVVAINSAGEASSSCELKVTPLNQAEPATRAQAERQSLPKDSQPKFERLLSDVLADEGEQVVLEVQASGDQPLTAQWFLTNKELQLDQRITTQSDSELGVFKLILNNVSGDDKGVYTVKVTNPAGDAKCFSHLIVKSVNAPENRRSSQSSVEIIERHQCPEFKELFSDKQGEIDEVIKFECIVKGKPTPKVHWFFNDQPVHGHNFLVSTSGERQVLTIQKLTHDAVGKISCVAENEAGKATCVAFLNIRGSGLPASSDVQTVSQEHNTESSRVTIKKQTFTTTSTSQVNSYEGNAPQTEVHHSSAHIDQSLKQLGQQRPEIVESHHYQELHKSKEMSSPTVQQKSFSFIQSSGANGQSAVAIPDSPTRLRREIAPRFTTPLSGKIVDQGADVSMEAIYDGFPSPEIKVEKNGGQLFEDAHTRISNKCNRVTIELKQVGVGDAGRYAVTASNTVGQSTSTADLVVKKTIFPPVFGRRLQAQVSKKGEKLTMEVEVTGLPEPTVTWLKDDKPLKDAGISEHRLLAQGNSYRLIIEKAQTTDSGKYMVRATNAGGEAKSIADCAILEPSPERLQEVVKTIVYETGPVAPASEFKTEGYKYTSSSMTSNYSHNMQSSSSSSHHETKFSSTSAPPPVVTYPSPIPAQRKTPAAEFSDYSSEIDERFRSVSRANESDAEIKGYRVVFPPTPTPRTNIATNGHKSPVVVITPSPMEFEPTPQDYARPKFEPISKEIRHEIKTETSSKQSKFMQNQQQNQPVFKPKPVAAKFIAATQQQQQKQPQATSRPTMYYNAVAGAPMHVAKVATETKNVMQMHESTESSQRVVNMQQTKRIIHFDSPQEQRDQQILEPFPYSPATSRTPSRQSHLPPPATPTKFVPGEFRESDYESEIDGARIQPLWSPYGDGMTKGFRRVAPPQGAGRSCSLPRTYERVLSPMEFDRGPEMPSKIHVDINTLRKEQRGGSTVTTQNRTQSLNRNTTMRQQQQQQQQQSMDQIDRAGTLPRYGYSSLQQQAENQGRRMGSTFLQKSHQFVDDVSREIRSSASNGIRPGFKRAPSEGSSQQPQAFRDESRVSQYGTKCVDPNTGLIYFKYDFGYEFGILFPGEGHKFVSSQWNSSGSSNSNAKPIQNGRHSPYPLKLPPGNELVIPVQHERSAQGYSSDNEVQRRSQTRNWSTTKPMAPRTINSHKRYSLPSGHSLDIHLDRLHAQAPRLPPDQMIRTVPELPNTEPVNAHLSRDELAQRQPLFITPLKDIAVGVGGTARFECIVQAHPQPQVNWTHNGGLLESGSRHCIEYRNGVCRLTLPQAYPDDNGSYACTAINPLGAATTSGNLTVSSTNRGFRY
Protein: Limostatin, isoform B (A0A0B4K762)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pyrokinin-1 receptor
Sequence:
MFAYTWQFPSLHSFLVPSLQLAPLILVILATTMTTTMAAPQQQEVPHALLDIETPNQFNYSPSPLAQPDSLRSKPYFDFLSTLYAHDTAKSNLFRPYSVRQRRDADVQKLSRPRRAIVFRPLFVYKQQEIRKQEIRDRNAQRRHDLNRLQRV
Protein: Malate dehydrogenase, cytoplasmic (EC 1.1.1.37) (Aromatic alpha-keto acid reductase) (KAR) (EC 1.1.1.96) (Cytosolic malate dehydrogenase) (P40925)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:8786100}.
Interaction partners:
Sequence:
MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKDLLKANVKIFKSQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTANDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFVTTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKESAFEFLSSA
Protein: AT5g11850/F14F18_20 (Protein kinase superfamily protein) (Q8S9K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKMKHLLRKLHIGGSSGVGGGFADHHRLDDSTRPMIDPSPILSTSPSPASTSSVSSSGFGNASTTMPRLDTFEPVGRDLTAVDGVDFNLMEEEYQVQLAMAISVSDPDPRENADTAQLDAAKRISLGVSAPVTDADSAVDFLSLRYWGHKVINYDQKVRDGFYDVYGITSNSLSQGKMPLLVDLQAISISDNVDYEVILVNRLIDPELQELERRVFALASECPDFAPGQVSSDLTQKIANIVVEQMGGPVENADEALRRWMLRSYELRNSLNTTILPLGRVNVGLARHRALLFKVLADRINLPCMLVKGSYYTGTDDGAVNLIKLDDKSEYIIDLMGAPGALIPSEVPSSFLPVSCTDTRVFPENLDSLQHSSPVLEKEIETPAFSVSKEADSRSGMVANFFTGNQEENSDRCAVEKHQTERFEHDFGKLMHSQQISGENMPPFSGKPTCAQKVKVKNVSKYVISAAKNPEFAQKLHAVLLESGASPPPDLFMDINPHNLRGKNLLQELRQESSNSMVSGIPCYPEKVAEQLRESERNPTAESYQQSVEVDLSMKRNFDLDNTGKASSSENMEVGTADGESAVCDSHDQGINPLLGEAAKWEIMWEDLQIGERIGIGSYGEVYRAEWNGTEVAVKKFLDQDFSGDALTQFKSEIEIMLRLRHPNVVLFMGAVTRPPNFSILTEFLPRGSLYRLLHRPNHQLDEKRRMRMALDVAKGMNYLHTSHPTVVHRDLKSPNLLVDKNWVVKVCDFGLSRMKHHTYLSSKSTAGTPEWMAPEVLRNEPANEKCDVYSFGVILWELATSRVPWKGLNPMQVVGAVGFQNRRLEIPDDIDLTVAQIIRECWQTEPHLRPSFTQLMQSLKRLQGLNISNRANTSESLM
Protein: Carboxynorspermidine/carboxyspermidine decarboxylase (CANS DC/CAS DC) (CANSDC/CASDC) (EC 4.1.1.96) (Q8D8D2)
Organism: Vibrio vulnificus (strain CMCP6)
Function: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Carboxynorspermidine is decarboxylated 20-fold more efficiently than carboxyspermidine. Exhibits some activity with L-ornithine, but shows no activity with L-arginine, L-lysine or meso-diaminopimelate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MNKEQLKTPFFMIDEAKLIQNLEIAKQLKEISGVKLVLALKCFSTWGVFDIIKPYLDGTTSSGPFEVKLGYEKFGGETHAYSVGYSEDDVREVADLCDKIIFNSQSQLAAHRHIVEGKASIGLRLNPGVSYASQDLANPARQFSRLGVQADHIDPAVFDSINGVMFHMNCENKDVDAFIALLDSISERFGAYLNKLDWVSMGGGVFFTWPGYDVEKLGLALKAFSEKHGVQMYLEPGEAIITKTTDLVVTVVDLVENGMKTAIVDSATEAHRLDTLIYKEPASVLEASENGEHEYVIGSCSCLAGDQFCVAKFDQPLHVGQRLHILDSAGYTMVKLNWFNGLKMPSVYCERTNGEIQKLNEFGYEDFKRSLSLWSVQ
Protein: Transcription attenuation protein MtrB (Trp RNA-binding attenuation protein) (TRAP) (Tryptophan RNA-binding attenuator protein) (P19466)
Organism: Bacillus subtilis (strain 168)
Function: Required for transcription attenuation control in the trp operon. This trans-acting factor binds to trinucleotide repeats (GAG or UAG) located in the trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.
Interaction partners:
- Tryptophan RNA-binding attenuator protein inhibitory protein
- Anthranilate synthase component 1
- Aminodeoxychorismate/anthranilate synthase component 2
- Probable tryptophan transport protein
- Uncharacterized transporter YcbK
- GTP cyclohydrolase 1
- Heptaprenyl diphosphate synthase component 1
Sequence:
MNQKHSSDFVVIKAVEDGVNVIGLTRGTDTKFHHSEKLDKGEVIIAQFTEHTSAIKVRGEALIQTAYGEMKSEKK
Protein: Mak-prov protein (Male germ cell associated kinase L homeolog (EC 2.7.1.-)) (Q6DCJ4)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MNRYTTMKQLGDGTYGSVIMGRSNESGELVAIKRMKRKFYSWEECMNLREVKSLKKLNHANVVKLKEVIRENDHLYFVFEYMKENLYQLMKDRNKLLPESVIRNIMYQILQGLAFIHKHGFFHRDMKPENLLCMGPELIKIADFGLVRELRSQPPYTDYVSTRWYRAPEVLLRSSSYSSPIDLWAVGSIMAELYTLRPLFPGTSEVDQIFKICQVLGTPKKNDWPEGYQLAASMNFRFPQCIPINLKTLIPNASEDALNLMRDTMQWDPKKRPTASQALRHPYFQVGQELGPPTQYAEHKKTLNKALQPKEPQPMYVTKMQSSSTSERSEKTSPDTPPATNRPLQQIQVPQSTGDTQLPSKTQQVTLPSISKTISPKFVANGPQTSAVSIKHGRRRWGQSVVKDSWDEIDTDFGISYSKKPSMALAKENKPEDSLFGLPDSISIGEENKGSSLAGTKRIDTSQTTSAKQHYLRQSRYLPGMNPKNAGLISANKDGKHATWNSALTTKPLGPIGGGIGYNRTNGGILGGFVGPSYNSTVAYIPSFNKKEVGSAGQRLQLAPIGAATTAPVISDAMNGKLKLTKPKSTTQRILPDNTADYDAWKPKAVRSQMPAPPFKPAAGNLSILNRPQPLQPVHGRTDWAAKYGGHR
Protein: Guanylate-binding protein 3 (EC 3.6.5.-) (GTP-binding protein 3) (GBP-3) (Guanine nucleotide-binding protein 3) (Q61107)
Organism: Mus musculus (Mouse)
Function: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H0R5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H0R5}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H0R5}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP5, at the Golgi apparatus. {ECO:0000250|UniProtKB:Q9H0R5}.
Interaction partners:
- Guanylate-binding protein 2
- Immunity-related GTPase family M protein 3
- Immunity-related GTPase family M protein 2
- Immunity-related GTPase family M protein 1
- Guanylate-binding protein 7
- Interferon-inducible GTPase 1
- Interferon-induced protein with tetratricopeptide repeats 3
- 2'-5'-oligoadenylate synthase-like protein 2
- Receptor-transporting protein 4
- GTP-binding protein
Sequence:
MEAPICLVENWKNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSSPREDKVKDSSEFVGFFPDFIWAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQLERNFQVESEKFCSYIFTNGKTKTLRGGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMERTRRKPSLFGQILDTIGNAFIMILPGAGKLFGVGLKFLGSLSS
Protein: Cyclic AMP-responsive element-binding protein 3-like protein 2 (cAMP-responsive element-binding protein 3-like protein 2) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 2] (A1L224)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/mbtps1 and S2P/mbtps2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis. May protect neuroblastoma cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BH52}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8BH52}. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 2]: Nucleus {ECO:0000250|UniProtKB:Q8BH52}. Note=Upon ER stress, translocated into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.
Interaction partners:
- cAMP-responsive element-binding protein 3-like 3 like.
- Creb1 protein
- Cyclic AMP-responsive element-binding protein 3-like protein 3-B
- Cyclic AMP-responsive element-binding protein 3-like protein 3-A isoform X1
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-responsive element-binding protein 5
- Cyclic AMP-dependent transcription factor ATF-4
- Ribosomal protein S6 kinase
- Cyclic AMP-responsive element-binding protein 5
- Zgc:112054
Sequence:
MEIMDSGEPFLQWDKNLSELSEAGENDILYSTHFTDLLDDLSQEALLGQLLSDPFLSGRGDAMDTEEELTRASPVPPHIQAEHSYSLCGDSRPQSPLSHLPGEPGSDAADSESDEWPMEQEDKGIKMEPLLCVPLPALTLTVTPAGSAPEPVIDSCDSAQSLSLPQVKEDSNSPQIKLEPHEVDQFLNLSPKGLECLQMPPTPPSSVGSDSEGSQSPVHPCAPASPTQTPAVLKVAPRAPSSLSSSPLLTAPHKLQGSGPLLLTEEEKRTLIAEGYPVPTKLPLSKAEEKALKKIRRKIKNKISAQESRRKKKEYVDALEKKVETCSNENHELRRKVENLECTNKSLLQQLHSLQAVVAGKVPRSCRVTGTQTSTCLMVVVLCFSLFLGSFYPGLSPCSSITKADLSREISIHDSYTTTVKSRSLLSIQEPGGLDEPHPIGLGGEYPEWDRQADVMAAWRFEQQHKEEEAELHKAEHRPLLLSTNETHAQKAILIDLHTHRSNETAKVIQLDRTVNETS
Protein: Uncharacterized protein (Q38CY1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase complex I subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Peptidyl-prolyl cis-trans isomerase
- NADH dehydrogenase subunit NI8M
- Uncharacterized protein
- Adrenodoxin reductase, putative
- NB-ARC domain-containing protein
Sequence:
MAVQTRFKWRHKETDRWRRLMDATCVPLDWIGQTRGPSFTQYSGHWTHLLTCAHVITPWDYPNFYPPKGPTRFVSRITLADTMTQVRLVSLQGNAVYKHFTSNQHVFVHSNPRLDLCVLHPEQNLRRSGEMKMLWMQNEGHVTRPRLELVKPLEVGDHVWVYGMTAHESLFDEEGGPEPLMIPTGIRARVHALTREHFFIDTKSIEGAERGCVGMGMCGSAVMRNGRCVGMLTATVHEESDCKELAGTAMCTYASDIFEFLLEVERQMKALPPSLNRQETMFQQRRRGEGSEEYEKQRETEGKEWDLDHTRLARHIPVPVSLWHMEEKWITEEDYMTNKVFGRGGPFNQETQENILGYDMNSSKSYGERPGDIASVSTATQDGKPTMQGERKDYSPTGIYADHEDFKTSDVWDYNVSSELRSLFDKGVDAKDAHSLNMMRKSLENIRAQRAMEKMKETVMKAPGHSEDPLNVGSMGRYDVNMEESSAQAFTPDMDDEVRAAARKEEKYHEELRRRHGNKARPFGDEDLRGLWEPH
Protein: SRBC-64 (Serpentine Receptor, class BC (Class B-like)) (G5ECV4)
Organism: Caenorhabditis elegans
Interaction partners:
- Serpentine receptor class gamma
- G-protein coupled receptor daf-37
- Serpentine receptor class gamma
- G-protein coupled receptor daf-38
- Guanine nucleotide-binding protein alpha-3 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
- 7TM GPCR serpentine receptor class x
- Serpentine receptor class X-43
Sequence:
MPEIVIILNNFLSVVFSQTTCILNFYLLFSIFYSKRIAWKSELSLIYTRFAFDMFYTFFVPHNKIYYIIRQIFPGFVVKNLSFYLIWPTIPLGCIRATLVFLITLDRVIALFFPISYHNHRFKISLSAIIISVSCFGASDHLILFGYCRYTVDVPLECDNFNCVIKTCFYSYWVSRDQIQYILTGTFSVILLFRLVIWNNFVASQRNQNLSRATRIALLESIVIICFSIIPSLIFSTFPSLNFVSVGPWTIVLKHAGFMIEALIICKFLLKRKSKNGIGRNSTVLTWSQ
Protein: Zinc finger protein 572 (Q7Z3I7)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEQEKKLLVSDSNSFMERESLKSPFTGDTSMNNLETVHHNNSKADKLKEKPSEWSKRHRPQHYKHEDAKEMPLTWVQDEIWCHDSYESDGKSENWGNFIAKEEEKPNHQEWDSGEHTNACVQQNSSFVDRPYKCSECWKSFSNSSHLRTHQRTHSGEKPYKCSECAKCFCNSSHLIQHLRMHTGEKPYQCGECGKSFSNTSHLIIHERTHTGEKPYKCPECGKRFSSSSHLIQHHRSHTGEKPYECSVCGKGFSHSYVLIEHQRTHTGEKPYKCPDCGKSFSQSSSLIRHQRTHTGEKPYKCLECEKSFGCNSTLIKHQRIHTGEKPYQCPECGKNFSRSSNLITHQKMHTGEKSYESSEYEESLGQNCNVIEECRIQLGEKPYRCCECGKSFGLSSHLIRHQRTHTGEKPYRCSECWKTFSQSSTLVIHQRTHTGEKPYKCPDCGESFSQSFNLIRHRRTHIGEKPYKCTSCEKCFSRSAYLSQHRKIHVEKPFESPDVGDFPHEWTWKNCSGEMPFISSFSVSNSSS
Protein: Nigerose phosphorylase (EC 2.4.1.279) (A9KT32)
Organism: Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans)
Function: Catalyzes the reversible phosphorolysis of nigerose. Also shows a weak activity on kojibiose.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:21808968}.
Interaction partners:
- Beta-phosphoglucomutase
- Beta-phosphoglucomutase
- Beta-phosphoglucomutase
Sequence:
MNWTLTNSSLDKDSITSNGNRFLIGNGYLGIRGTLEEYRKEYFPAINLAGIYDQVGEGWREPLNAPNALYTRIEVDEVEYQLPKIEPRYHELSLDYRHGILDRQTVWASNKGTIIVKSSRFASMKEKHLVVLNYSITADYDCEIIVYTGIDGSVWDIHGPHYDKVEFQKQLLRHNETEILNEKYLLESESKWNGHRLSIAAQTHENKDIVYVTEDIICNKEAKIELIESDKECLRKLTFHGKAKEEINFTKYITVFTSKDCVDYKEQSIKIVNHAKDTGYERLQEEHKNVWEQLWNISEVTIEGDDEANDALNYSLYHLHCIAPRHSKSLSIAARGLSGQTYKGAVFWDTEMFMLDFFLYTQPEVAKTLLRYRIDTLEGAKKKAKLYGYEGAFYAWESQEGGYDACSDYNVTDVFTKRPMRTYFKDKQVHISSAIVYGIRSYLNYTNDFSILAEGGAETILECAKFYYSLLEKKIGKEYYEIHDVIGPDEYHERVNNNAYTNRMAKLTFETAIDILDHEKNKDEEFYIKLLKQYEIKDLLDKLKDACNKLYIPKPKDNSDLIEQFDGFFELEDVSLEEVRSRLLHEKEYWGGAYGVASHTQVIKQADVVTMLVLFKEEYQREVLQQNLNYYEPRTEHGSSLSACMYSLLYCMCDQPQYAYPFFMKSALADWNGKGKEWAGLVYIGGTHPAAAGGAYMTAIKGFGGFQIENGVIKATPRLPKHWVRLKYRVLYQGAIYEIDASKEQVSISKIEM
Protein: Protein YLS7 (Protein TRICHOME BIREFRINGENCE-LIKE 17) (Protein YELLOW-LEAF-SPECIFIC GENE 7) (Q9FHM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Small ribosomal subunit protein uS3x
- At5g50410
- Probable metal-nicotianamine transporter YSL7
- NDR1/HIN1-like protein 10
- Metal-nicotianamine transporter YSL1
- NAC domain-containing protein 17
Sequence:
MTLASPRVSNSKTTVLLFPRKVSSIAFAIGGLTSFVIFASLLLFTYPIGSSVTDYFYRTETTQNVQFHHSIHDPDRNPSPVSSSESPPVLTQDSDDKVLPKGSHDSNDVRLGEETNSGKSSNVSIDEEATQDHVETECDLYHGNWFYDPMGPLYTNNSCPLLTQMQNCQGNGRPDKGYENWRWKPSQCDLPRFDAKKFLELMRGKTLAFIGDSVARNQMESMMCLLWQVETPVNRGNRKMQRWYFRSSSVMIARMWSSWLVHQFNEPFGFATDGVTKLKLDQPDERIIEALPNFDVVVLSSGHWFAKQSVYILNDQIVGGQLWWPDKSKPEKINNVEAFGISVETIIKAMAKHPNYTGLTILRTWSPDHYEGGAWNTGGSCTGKVEPLPPGNLVTNGFTEIMHEKQATGFHRAVADDKLGNRSKKLKLMDITEAFGYRHDGHPGPYRSPDPKKITKRGPDGQPPPQDCLHWCMPGPVDTWNEMVLEIIRRDFEGRQSSPSS
Protein: ABC transporter C family member 5 (ABC transporter ABCC.5) (AtABCC5) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 5) (Glutathione S-conjugate-transporting ATPase 5) (Multidrug resistance-associated protein 5) (Q7GB25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates. Involved in regulation of K(+) and Na(+) cell content. Mediates resistance to NaCl and Li(+), confers sensitivity to sulfonylurea drugs such as glibenclamide (inducer of stomatal opening), and required for stomatal opening regulation by auxin, abscisic acid (ABA) and external Ca(2+). Transports oestradiol-17-(beta-D-glucuronide) (E(2)17G). Involved in the root auxin content regulation that controls the transition from primary root elongation to lateral root formation. Plays a role in ABA-mediated germination inhibition. High-affinity inositol hexakisphosphate transporter that plays a role in guard cell signaling and phytic acid storage. Required for phytic acid accumulation in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Phosphatidylinositolglycan-like protein
- Inositol-pentakisphosphate 2-kinase
- Probable sugar phosphate/phosphate translocator At3g11320
- Dem protein
- Inositol-tetrakisphosphate 1-kinase 1
- GDSL esterase/lipase At5g08460
- Inositol-tetrakisphosphate 1-kinase 2
Sequence:
MDFIEISLIFREHLPLLELCSVIINLLLFLVFLFAVSARQILVCVRRGRDRLSKDDTVSASNLSLEREVNHVSVGFGFNLSLLCCLYVLGVQVLVLVYDGVKVRREVSDWFVLCFPASQSLAWFVLSFLVLHLKYKSSEKLPFLVRIWWFLAFSICLCTMYVDGRRLAIEGWSRCSSHVVANLAVTPALGFLCFLAWRGVSGIQVTRSSSDLQEPLLVEEEAACLKVTPYSTAGLVSLITLSWLDPLLSAGSKRPLELKDIPLLAPRDRAKSSYKVLKSNWKRCKSENPSKPPSLARAIMKSFWKEAACNAVFAGLNTLVSYVGPYLISYFVDYLGGKEIFPHEGYVLAGIFFTSKLIETVTTRQWYMGVDILGMHVRSALTAMVYRKGLKLSSIAKQNHTSGEIVNYMAVDVQRIGDYSWYLHDIWMLPMQIVLALAILYKSVGIAAVATLVATIISILVTIPLAKVQEDYQDKLMTAKDERMRKTSECLRNMRVLKLQAWEDRYRVRLEEMREEEYGWLRKALYSQAFVTFIFWSSPIFVAAVTFATSIFLGTQLTAGGVLSALATFRILQEPLRNFPDLVSMMAQTKVSLDRISGFLQEEELQEDATVVIPRGLSNIAIEIKDGVFCWDPFSSRPTLSGIQMKVEKGMRVAVCGTVGSGKSSFISCILGEIPKISGEVRICGTTGYVSQSAWIQSGNIEENILFGSPMEKTKYKNVIQACSLKKDIELFSHGDQTIIGERGINLSGGQKQRVQLARALYQDADIYLLDDPFSALDAHTGSDLFRDYILSALAEKTVVFVTHQVEFLPAADLILVLKEGRIIQSGKYDDLLQAGTDFKALVSAHHEAIEAMDIPSPSSEDSDENPIRDSLVLHNPKSDVFENDIETLAKEVQEGGSASDLKAIKEKKKKAKRSRKKQLVQEEERVKGKVSMKVYLSYMGAAYKGALIPLIILAQAAFQFLQIASNWWMAWANPQTEGDESKVDPTLLLIVYTALAFGSSVFIFVRAALVATFGLAAAQKLFLNMLRSVFRAPMSFFDSTPAGRILNRVSIDQSVVDLDIPFRLGGFASTTIQLCGIVAVMTNVTWQVFLLVVPVAVACFWMQKYYMASSRELVRIVSIQKSPIIHLFGESIAGAATIRGFGQEKRFIKRNLYLLDCFVRPFFCSIAAIEWLCLRMELLSTLVFAFCMVLLVSFPHGTIDPSMAGLAVTYGLNLNGRLSRWILSFCKLENKIISIERIYQYSQIVGEAPAIIEDFRPPSSWPATGTIELVDVKVRYAENLPTVLHGVSCVFPGGKKIGIVGRTGSGKSTLIQALFRLIEPTAGKITIDNIDISQIGLHDLRSRLGIIPQDPTLFEGTIRANLDPLEEHSDDKIWEALDKSQLGDVVRGKDLKLDSPVLENGDNWSVGQRQLVSLGRALLKQAKILVLDEATASVDTATDNLIQKIIRTEFEDCTVCTIAHRIPTVIDSDLVLVLSDGRVAEFDTPARLLEDKSSMFLKLVTEYSSRSTGIPEL
Protein: Translocator protein 2 (Peripheral-type benzodiazepine receptor-like protein 1) (Q9CRZ8)
Organism: Mus musculus (Mouse)
Function: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum. Required to meet cholesterol demands during erythropoietic differentiation. May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-mediated ATP export, and import of the heme precursors protoporphyrin IX and 5-aminolevulinic acid (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19729679}; Multi-pass membrane protein {ECO:0000269|PubMed:19729679}. Cell membrane {ECO:0000250|UniProtKB:Q5TGU0}; Multi-pass membrane protein. Note=Localizes to the plasma membrane and intracellular membranes in developing and mature erythrocytes. {ECO:0000250|UniProtKB:Q5TGU0}.
Interaction partners:
- Glycophorin-A
Sequence:
MQLQGPVFVGVPLLGPILICMLIHQPSSRCEDERKLPWCPPHKVILLVWVTIYSVMGYASYLVWKELGGGFRWPLALPLGLYSFQLALSWTFLVLFLAADSPGLALLDLLLLYGLVASLVFIWQPINKLAALLLLPYLAWLTVTTAITYRLWRDSLCPTYQP