wanglab/gogpt-training-data huggingface dataset:
Protein: Prostate and testis expressed protein 2 (PATE-like protein M) (PATE-M) (Q6UY27)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Prostate and testis expressed protein 3
- Prostate and testis expressed protein 4
- Prostate and testis expressed protein 1
Sequence:
MLVLFLLGTVFLLCPYWGELHDPIKATEIMCYECKKYHLGLCYGVMTSCSLKHKQSCAVENFYILTRKGQSMYHYSKLSCMTSCEDINFLGFTKRVELICCDHSNYCNLPEGV
Protein: Malate dehydrogenase (EC 1.1.1.37) (B3H560)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEFRGDANQRIARISAHLTPQMEAKNSVIGRENCRAKGGNPGFKVAILGAAGGIGQSLSLLMKMNPLVSLLHLYDVVNAPGVTADVSHMDTGAVVRGFLGAKQLEDALTGMDLVIIPAGIPRKPGMTRDDLFKINAGIVKTLCEGVAKCCPNAIVNLISNPVNSTVPIAAEVFKKAGTYDPKKLLGVTTLDVARANTFVAEVLGLDPREVDVPVVGGHAGVTILPLLSQVKPPSSFTPQEIEYLTNRIQNGGTEVVEAKAGAGSATLSMAYAAAKFADACLRGLRGDANVVECSFVASQVNLENSFTLFHCFNGFNLKWQLTTGDRISFLCNKSAPWPYRSRGSVSAWTLKRIRKDWSGESKR
Protein: Seizure 6-like protein (Acupuncture-induced protein 1-L) (Brain-specific receptor-like protein B) (BSRP-B) (Q6P1D5)
Organism: Mus musculus (Mouse)
Function: Candidate tumor suppressor gene. May contribute to specialized endoplasmic reticulum functions in neurons.
Subcellular location: Cell membrane {ECO:0000305|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000305|PubMed:16814779}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16814779}; Single-pass type I membrane protein {ECO:0000269|PubMed:16814779}. Note=In cerebellar predominantly localized to the endoplasmic reticulum.
Interaction partners:
Sequence:
MPVARPQAAGPDRISLFLVAFLLGSPAAAQAEDGGPEGEMHPSTAYLLPSASLESSLEEGVTSAAPGLLPSQEALEAMEESLPPALPDEASVQHTPALRKGLPSLKQLNSARRQLRPLATPTTLQRLGSPASATTKLREPEDPEQPTAPAPLQIAPFTALATTLPHSPQPAQAPDDSSPGSPLDKGDNELTGSASEESQETTTSTIVTTTIITTEQAPALCGVSFSDPEGYIDSSDFPPQPYSSFLECTYNVTVYTGYGVELQVKSVNLSEGELLSIRGVDGPTLTVLANQTLLVEGQVIRSPTNTISVYFRTFQDDGLGTFQLHYQAFMLSCPFPRRPDAGEVTVMDLHSGGVAHFHCHLGYELQGAKTLTCINASKPHWSSQEPVCSAPCGGAVHNATIGRVLSPSFPGTANGSQLCVWTIEAPEGQKLHLHLERLLLHEKDRMIVYSGRTNTSALLYDSLRTESVPFEGLLSEGSSIRIEFTSDQGQAASAFNIRFEAFEKGHCYEPYIQNGNFTTSDPTYNIGTIVEFTCDPGHSLEQGPAVIECVNVRDPYWNDTEPLCRAMCGGELSAVAGVVLSPNWPEPYAEGEDCVWKIHVGEEKRIFLDIQFLNLSNSDILTIYDGDEVVPHVLGQYFGHSSPQKLYSSTPDLTIQFHSDPAGLIFGKGQGFIMNYIEVSRNDSCSDLPEIQNGWKTTSHTELVRGARITYQCDPGYDIVGSDTLTCQWDLSWSSDPPFCEKIMYCTDPGEVEHSTRLISDPVLLVGTTIQYTCSPGFVLEGSSLLTCYSRETGTPIWTSRLPHCVSEESLACDNPGLPENGYQILYKRLYLPGESLTFMCYEGFELMGEVTIRCILGQPSHWSGPLPICKVNQDSFEHALEAEAAAESSLEGGNMALAIFIPVLLISLLLGGAYIYVTRCRQYSSLRLPLMYSHPYSQITVETEFDNPIYETGETREYEVSI
Protein: Minichromosome maintenance 10 (Q5XVE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- Origin of replication complex subunit 2
- DNA replication licensing factor MCM5
- Cell division cycle 45
- DNA replication licensing factor MCM3
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM6
- Cell division control protein 6 homolog
- DNA polymerase epsilon subunit B
Sequence:
MENDQEDLELLLSLDDRVLETPPGSPSAAPGYLTDDESPKRRGHSDLSDFRSVVQDCIDYNPKPIAKNTKPKGSNNSNTNDIEKFSGLRIRNQLLSPAEISDLFSDIRFVRLPTIKNLLMGDKLSGCWATMGVITEKGQPKTSSIGQAYGIWKIGSLNENNVSLFLFGDAYKKNETEKAGTVFGLFNCSLRKDNGGREFSLSVNSAKQMVKLGVSADYGVCTAKRKDGTTCTSVVNKRQGAFCKIHKLNASDKFATMRTELKGGNLRTAFRDLKSQGIYTVEPPADRSGNKKTTQPVRVLSVEGLRKALSGADKVTPNVHSQGIRFLNEMARQKASKNVNKKSEAVNKSTEKRKASTKETQVNGEPKRKKTEHRKETPEISTGKMMLLDFCSSDEE
Protein: Protein moonraker isoform X1 (Si:dkey-243i1.1) (X1WC30)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- rRNA methyltransferase 3A, mitochondrial
- Centriole and centriolar satellite protein ofd1
- 2-
- Centrosomal protein 120.
- Centrosomal protein of 63 kDa
Sequence:
MISDFHRASTMTTADLGSLNRQWIKKGSSVSQIAGLQTQLQFNSAVLPSVLNRATRVGPPSPIVIEKLLPHTERQDDMESCSSSLRLSVLSEERLQAAVRLAKRDLQRKRQESINRSSLEQEETQEIIIPERTNTDNVPRVVSPKMAGTRKQIKTGAHVLVYTPQKPNSPIKQTQTPIKNTIVNSSEPQLTQEIRKLQKELSTYVQRVEQLANKECVVEALEPNEKQRIEIRRQEQAARSARMIYVLQQQVKEIKQDLDKLRCQNIKPTKKSRPMERLAAAHRGAVRAMQVFINQLSDPAENRVPTHCKELGQLIRQLSLCSAKVEVGQGSVVPETALDILQKLEMLDSALSKQETTKKRDVYLQNVNPVEKTSIQVRARSMSPPRPARAPAERNSRRPRKPADAKKPASSRLAGKSHRTSQALLKERNDVLKAGLESLIHHQKLREAEAQKTNKTTSAISQDHVKQASHVRDAKFQQPTVSSRLRENQVPQKESTVPWIPTSPHSPSRLRAVPNRPEPRCLFSPHKNPEKQKPQTTSSTQLSASSPDRKQAQNEALRQAWLDRVTADRLRELNRLSKEEADRIKKLRTTVGSPTQWAERAERAAKERIQPLLDQAQRVAGAGSDRLRARLKVTDKAEGKTDLLTETLLEDLQEDTAQALWVTQREQVAETDAERKLQGPTLESMLLRMEEMERDQDEVRRRLAMISYSDPLIWERGTDATRNNSSSRPISPQPIRLTKPALNAPPTADILLQKPVEIGAASDMPILDDESLTPNDSSNPVPAGGGSTRGVYLTVPASMQRRIQKYRENHDAFLRLISHEALGSFNPWAIADSLADELMSEALAEVAAEFQDVCEEYAEAVFTSEFLQPVQSPSTSMS
Protein: Centromere protein O (Q8GUP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At5g10060
- ENTH/VHS family protein
- AT5g05210/K2A11_8
- Nucleic acid-binding protein
- Serine/Threonine-kinase
- AT5g57120/MUL3_6
- Cytomatrix protein-like protein
- Protein BIG GRAIN 1-like B
- Protein GID8 homolog
- Uncharacterized protein
Sequence:
MGEMIVSMDQDIRLDTTRARLSNLLKRHRELSDRLTRDSDKTMLDRLNKEFEAARRSQSQEVFLDGEEWNDGLLATLRERVHMEADRKADNGNAGFSLVCHPEERITYRVGNKVICCLDGSRIGIQFETSTAGETYEVYHCVLESKSFLEKMIVLEHTIPFFLPLSDLENDLLFSNAKKFIDNVGDLLQAYVDRKEQVRLIKELFGHQISEIYHSLPYHMIEFSMDDCDCKFVVSLRYGDLLCELPTKVRILVWPMHHLSKKQCTSPGSPAIPVRLPFAEDAFRIQSLPEAYAEIMPNMPNEIRQLFQTSPS
Protein: CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) (P13242)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Interaction partners:
- Large ribosomal subunit protein uL2
- DNA-directed RNA polymerase subunit beta
- GMP synthase
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL5
- Nucleoside diphosphate kinase
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL14
Sequence:
MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKFSNVTTGKIYSTVLKKERRGDYLGGTVQVIPHITNELKDRVYRAGKETNADVVITEIGGTVGDIESLPFLEAIRQMKSDIGRENVMYIHCTLVPYIKAAGELKTKPTQHSVKELRSLGIQPNIIVVRTEMPISQDMKDKIALFCDIDTKAVIECEDADNLYSIPLELQKQGLDKLVCEHMKLACKEAEMSEWKELVNKVSNLSQTITIGLVGKYVELPDAYISVVESLRHAGYAFDTDVKVKWINAEEVTENNIAELTSGTDGIIVPGGFGDRGVEGKIVATKYARENNIPFLGICLGMQVASIEYARNVLGLKGAHSAEIDPSTQYPIIDLLPEQKDVEDLGGTLRLGLYPCKLEEGTKAFEVYQDEVVYERHRHRYEFNNEFRQQMEEQGFVFSGTSPDGRLVEIIELKDHPWFVASQFHPEFKSRPTRPQPLFKGFIGASVEAANQK
Protein: Ribonucleoside-diphosphate reductase small subunit (EC 1.17.4.1) (Ribonucleotide reductase small subunit) (Q4JQV7)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Host membrane {ECO:0000255|HAMAP-Rule:MF_04028}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04028}.
Interaction partners:
Sequence:
MDQKDCSHFFYRPECPDINNLRALSISNRWLESDFIIEDDYQYLDCLTEDELIFYRFIFTFLSAADDLVNVNLGSLTQLFSQKDIHHYYIEQECIEVVHARVYSQIQLMLFRGDESLRVQYVNVTINNPSIQQKVQWLEEKVRDNPSVAEKYILMILIEGIFFVSSFAAIAYLRNNGLFVVTCQFNDLISRDEAIHTSASCCIYNNYVPEKPAITRIHQLFSEAVEIECAFLKSHAPKTRLVNVDAITQYVKFSADRLLSAINVPKLFNTPPPDSDFPLAFMIADKNTNFFERHSTSYAGTVINDL
Protein: Coiled-coil domain-containing protein 70 (Q6NSX1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSFKVSRWMGLACFRSLAASSPSIRQKKLMHKLQEEKAFREEMKIFREKIEDFREEMWTFRGKIHAFRGQILGFWEEERPFWEEEKTFWKEEKSFWEMEKSFREEEKTFWKKYRTFWKEDKAFWKEDNALWERDRNLLQEDKALWEEEKALWVEERALLEGEKALWEDKTSLWEEENALWEEERAFWMENNGHIAGEQMLEDGPHNANRGQRLLAFSRGRA
Protein: RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1) (Q96D71)
Organism: Homo sapiens (Human)
Function: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000269|PubMed:20946875}. Note=Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits.
Interaction partners:
- RalA-binding protein 1
- AP2-associated protein kinase 1
- SH3-containing GRB2-like protein 3-interacting protein 1
- RalBP1-associated Eps domain-containing protein 2
- BMP-2-inducible protein kinase
- AP-2 complex subunit beta
- Epidermal growth factor receptor substrate 15
- Intersectin-1
- AP-2 complex subunit alpha-1
- AP-2 complex subunit mu
Sequence:
MEGLTLSDAEQKYYSDLFSYCDIESTKKVVVNGRVLELFRAAQLPNDVVLQIMELCGATRLGYFGRSQFYIALKLVAVAQSGFPLRVESINTVKDLPLPRFVASKNEQESRHAASYSSDSENQGSYSGVIPPPPGRGQVKKGSVSHDTVQPRTSADAQEPASPVVSPQQSPPTSPHTWRKHSRHPSGGNSERPLAGPGPFWSPFGEAQSGSSAGDAVWSGHSPPPPQENWVSFADTPPTSTLLTMHPASVQDQTTVRTVASATTAIEIRRQSSSYDDPWKITDEQRQYYVNQFKTIQPDLNGFIPGSAAKEFFTKSKLPILELSHIWELSDFDKDGALTLDEFCAAFHLVVARKNGYDLPEKLPESLMPKLIDLEDSADVGDQPGEVGYSGSPAEAPPSKSPSMPSLNQTWPELNQSSEQWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPVPIRMTPSKIHMQEMELKRTGSDHTNPTSPLLVKPSDLLEENKINSSVKFASGNTVADGYSSSDSFTSDPEQIGSNVTRQRSHSGTSPDNTAPPPPPPRPQPSHSRSSSLDMNRTFTVTTGQQQAGVVAHPPAVPPRPQPSQAPGPAVHRPVDADGLITHTSTSPQQIPEQPNFADFSQFEVFAASNVNDEQDDEAEKHPEVLPAEKASDPASSLRVAKTDSKTEEKTAASAPANVSKGTTPLAPPPKPVRRRLKSEDELRPEVDEHTQKTGVLAAVLASQPSIPRSVGKDKKAIQASIRRNKETNTVLARLNSELQQQLKDVLEERISLEVQLEQLRPFSHL
Protein: Putative sulfate transporter YPR003C (P53394)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possible sulfate transporter.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GTP-binding protein YPT1
- Protein ISD11
Sequence:
MTSNNSLLGRGRMSYSSTAPPRFKRSVDQRDTFSDNFDYDKDSSNRGRTYIAASNSTTGVPPPNNSRSGCTNNTNNTNNTSNTSNTNNNDSVDENTVFETLPYYLPCFSWLPEYTFNKLWGDVIAGISVASFQIPLALSYTTSIAHVPPLCGLYSLAISPFVYGILGSVPQMIVGPESAISLVVGQAVESITLHKENVSLIDISTVITFVSGTILLFSGISRFGFLGNVLSKALLRGFISSVGLVMIINSLISELKLDKFLVSLPQHYHTPFEKILFLIDYAPAQYHIPTAIFSGCCLIVLFLTRLLKRKLMKYHKSAIFFPDILLVVIVTILISMKFNLKHRYGISIIGDFSMDNFDELKNPLTRPRRKLIPDLFSASLIVAMLGFFESTTASKSLGTTYNLTVSSNRELVALGFMNIVISLFGALPAFGGYGRSKINALSGAQSVMSGVFMGVITLITMNLLLQFVHYIPNCVLSVITTIIGISLLEEVPGDIKFHLRCGGFSELFVFAVTFCTTIFYSIEAGICIGCVYSIINIIKHSAKSRIQILARVAGTSNFTNLDDYMMNMKRNSLDVEGTEEIEGCMIVRIPEPLTFTNSEDLKQRLDRIERYGSSKIHPGRKSLRSKDSIKYVIFDLGGMTSIDSSAAQVLEEIITSYKRRNVFIYLVNVSINDKVRRRLFKAGVAASVERAQANNNENNTSNTFSDAGETYSPYFDSIDAALYEIEKMKIKGNNVPNNDSESFMSNTLFNSSLV
Protein: Heme oxygenase 4, chloroplastic (EC 1.14.14.18) (Q9LQC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19860740}.
Interaction partners:
- Ferrochelatase-2, chloroplastic
- Ferrochelatase-1, chloroplastic/mitochondrial
- Frataxin, mitochondrial
- Phytochromobilin:ferredoxin oxidoreductase, chloroplastic
- Heme oxygenase 3, chloroplastic
- Heme oxygenase 1, chloroplastic
- Protoheme IX farnesyltransferase, mitochondrial
- ELM2 domain-containing protein
Sequence:
MATSRLNASCRFPASRRLDCESYVSLRAKTVTIRYVRTIAAPRRHLVRRANEDQTLVVNVVAAAGEKPERRYPREPNGFVEEMRFVVMKIHPRDQVKEGKSDSNDLVSTWNFTIEGYLKFLVDSKLVFETLERIINESAIQAYAGLKNTGLERAENLSRDLEWFKEQGYEIPESMVPGKAYSQYLKNIAEKDPPAFICHFYNINFAHSAGGRMIGTKVAEKILDNKELEFYKWDGQLSELLQNVSEELNKVAELWTREEKNHCLEETEKSFKFYWEIFRYLLS
Protein: 3-ketoacyl-CoA thiolase, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase) (Peroxisomal 3-oxoacyl-CoA thiolase) (P27796)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs).
Subcellular location: Peroxisome {ECO:0000269|PubMed:7754706, ECO:0000269|PubMed:8125978}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Peroxisomal targeting signal 2 receptor
- Hydroxymethylglutaryl-CoA synthase
- Acyl-coenzyme A oxidase
- Peroxisomal membrane protein PEX18
- Peroxisomal hydratase-dehydrogenase-epimerase
- Peroxisomal protein PEX21
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Citrate synthase, peroxisomal
- 3,2-trans-enoyl-CoA isomerase
Sequence:
MSQRLQSIKDHLVESAMGKGESKRKNSLLEKRPEDVVIVAANRSAIGKGFKGAFKDVNTDYLLYNFLNEFIGRFPEPLRADLNLIEEVACGNVLNVGAGATEHRAACLASGIPYSTPFVALNRQCSSGLTAVNDIANKIKVGQIDIGLALGVESMTNNYKNVNPLGMISSEELQKNREAKKCLIPMGITNENVAANFKISRKDQDEFAANSYQKAYKAKNEGLFEDEILPIKLPDGSICQSDEGPRPNVTAESLSSIRPAFIKDRGTTTAGNASQVSDGVAGVLLARRSVANQLNLPVLGRYIDFQTVGVPPEIMGVGPAYAIPKVLEATGLQVQDIDIFEINEAFAAQALYCIHKLGIDLNKVNPRGGAIALGHPLGCTGARQVATILRELKKDQIGVVSMCIGTGMGAAAIFIKE
Protein: Mast/stem cell growth factor receptor (EC 2.7.10.1) (B8A5K6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000311}.
Interaction partners:
- Kit ligand b.
- Kit ligand
- Mast/stem cell growth factor receptor kita
- HRas proto-oncogene, GTPase a.
- small monomeric GTPase
- GTPase NRas
- small monomeric GTPase
- Colony-stimulating factor 1a
- Growth factor receptor-bound protein 2
- Growth factor receptor-bound protein 2a
Sequence:
MGHSWFLRTVLLLFALPEGWSKPVITPDAPHLVILKGKQLYLRCHDDADVNAGRVRWLRDKGRRIEGELKDDEASVILLNITETQHMGNYTCENTETEEKSSIYIYVKDLGSAFVRRMVNDLQVRKGEEITLPCLVTDPAVSHLSLQTCNGSALPAALTFITHPQGGITIRNVSKAFEGCYFCAGQLDQKPVKSREYNLVVRLAPESVPAISLSRNENVILIQDQEFKLSCSAVNINHDFHLRWTIPSEATALESHKSNIQPGSREYQRSITLWIQSVKINDTGSYRCNARNEKGVSMAAVNLEVYERGFINLTEGENRVVEVREGESLTLSVEITSYPKPNDVLWTYNNQELQNTSEHVITLHNQQYRYISELRLVRVHGSEGGIYTFSANHKYESVNQSFTVHVICKPVIVSQEGPVDGQVRCVASGYPVPKISWYYCEPPHTRCSHLLNATQADEEFAVITVSGSEFGRSEVESRLNISKGKFHTLECVASAQGEQAYTLFSISERTVPHKLFTPLLSGVVSTSVLLSFILVVLLYKYMQKPKYEIHWKVIDSFDGNNYTYIDPTQLPYDPKWEFPRERLRFGKILGSGAFGKVVAATAYGLCSADTVTTVAVKMLKPSAHSTEKEALMSELKVLSYIGNHINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDAFFSSKTGDGYYKNLLSQTQPSIEGTDNGYMPMRSYQKRSNQTEWCDDKDDLSLDTEDLLSFSYQVAKGMDFLTSKNCIHRDLAARNVLLTQGRVAKICDFGLARDITRDSNYVLRGNARLPVKWMSPESLFACVYTFESDVWSYGILLWEIFSLGNTPYPGIPVGSTFYKMIQDGYRMSEPEFAPSEIYEVMRWCWSADPLKRPPFKKLVERTELLLSETTKHDYLNLSTSGSCEAFVPPGLQRPQRLSSVGSSTASTQPLLQATNDVFLEHQSI
Protein: Neuropeptide S receptor (G-protein coupled receptor 154) (G-protein coupled receptor PGR14) (G-protein coupled receptor for asthma susceptibility) (Q6W5P4)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for neuropeptide S (NPS). Promotes mobilization of intracellular Ca(2+) stores. Inhibits cell growth in response to NPS binding. Involved in pathogenesis of asthma and other IgE-mediated diseases.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15947423, ECO:0000269|PubMed:16790440}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:15947423}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:15947423}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:15947423}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:15947423}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:15947423}.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000269|PubMed:15947423}.; SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm {ECO:0000269|PubMed:15947423}.
Interaction partners:
- Neuropeptide S
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL5
Sequence:
MPANFTEGSFDSSGTGQTLDSSPVACTETVTFTEVVEGKEWGSFYYSFKTEQLITLWVLFVFTIVGNSVVLFSTWRRKKKSRMTFFVTQLAITDSFTGLVNILTDINWRFTGDFTAPDLVCRVVRYLQVVLLYASTYVLVSLSIDRYHAIVYPMKFLQGEKQARVLIVIAWSLSFLFSIPTLIIFGKRTLSNGEVQCWALWPDDSYWTPYMTIVAFLVYFIPLTIISIMYGIVIRTIWIKSKTYETVISNCSDGKLCSSYNRGLISKAKIKAIKYSIIIILAFICCWSPYFLFDILDNFNLLPDTQERFYASVIIQNLPALNSAINPLIYCVFSSSISFPCREQRSQDSRMTFRERTERHEMQILSKPEFI
Protein: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (D-alanyl-glycyl endopeptidase) (N-acetylmuramoyl-L-alanine amidase) (Q08JW9)
Organism: Staphylococcus phage phiMR11
Interaction partners:
Sequence:
MQAKLTKKEFIEWLKTSEGKQFNVDLWYGFQCFDYANAGWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDRIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSETAPRSIQSPTQASKKETAKPQPKAVELKIIKDVVKGYDLPKRGGNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQLGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKQLQLKDYFIKQIRVYMDGKIPVATVSNESSASSNTVKPVASAWKRNKYGTYYMEENARFTNGNQPITVRKIGPFLSCPVAYQFQPGGYCDYTEVMLQDGHVWVGYTWEGQRYYLPIRTWNGSAPPNQILGDLWGEIS
Protein: Ccp84Ad (Cuticle protein) (O97061)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD29420p
Sequence:
MAFKFIALFALIAAASAGVLPVQQVYHAAPAVATYAQAPVAVAHAQPVLAKAAEEYDPHPQYKYAYDVQDSLSGDSKSQVEERDGDVVRGEYSLIDADGYKRTVQYTADPINGFNAVVNREPLVKAVAVAPVVKTVAAPVAHYAAPAVAHYAAPAVVKTVAPVAHYAAPAVVKTVAPVAHYAAPATYTSYAAPAVAYHH
Protein: Hydrophobic dipeptide epimerase (EC 5.1.1.-) (C0BK17)
Organism: Flavobacteria bacterium (strain MS024-2A)
Function: Catalyzes the epimerization a variety of hydrophobic dipeptides. Epimerase activity is highest with L-Ala-L-Tyr, and lower with L-Ala-L-Met, L-Ala-L-Phe, L-Tyr-L-Ala, L-Tyr-L-Met and L-Tyr-L-Trp (in vitro).
Interaction partners:
- PFAM: protein of unknown function DUF1611
Sequence:
MKFTFHKVTLKKRFPLAISRGVRYNSENLFVCYEKDGHIGWGEAAPGNSEGAATAEAVQEALENFIATGIEGFSIQELYDRAREMKIPPCAYVALDTAFWDWTAKKAQLPLRQLLGFSKPHTPTSVTIGINPPEVIKERVPLLLEGTTVQSLKIKLGSPEGIDADKTMFEQVVESTKKYPVKLRVDANGGWDVNQAQHMMQWLADRKVDYIEQPLKEGDEAGLKTLFKSRPLPIYVDESCRFSQNIPSFAAHVDGVNMKLMKCGGITEALRIIGTARAHGLKTMIGCMSESSVAIAAAAAMTGGIDHIDLDSHYNLAPDPAHGAPLINGVTLPPEIPGHGAYLKEEFYA
Protein: Carbonic anhydrase 2, isoform A (EC 4.2.1.-, EC 4.2.1.1) (LD26647p) (Q9VTU8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyrosine-protein phosphatase 99A
Sequence:
MRRCRNTPFAIVIAPILICASLVLAQDFGYEGRHGPEHWSEDYARCSGKHQSPINIDQVSAVEKKFPKLEFFNFKVVPDNLQMTNNGHTVLVKMSYNEDEIPSVRGGPLAEKTPLGYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSVNMTNPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTANDDHLKNNFRPIQPLNDRTLYKNYIEIPIHNMGSIPLVDAENAAGKWRAQAAAVLLPLVVLAALSRTSIFRGF
Protein: Neurexin-3-beta (Neurexin III-beta) [Cleaved into: Neurexin-3-beta, soluble form; Neurexin-3-beta, C-terminal fragment (NRXN3-CTF)] (Q9HDB5)
Organism: Homo sapiens (Human)
Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity).
Subcellular location: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8C985}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHLRIHARRSPPRRPAWTLGIWFLFWGCIVSSVWSSSNVASSSSTSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTIIETTKDSLSMTSEAGLPCLSDQGSDGCDDDGLVISGYGSGETFDSNLPPTDDEDFYTTFSLVTDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQQSSKSGHKKQKNKDREYYV
Protein: L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2) (Dactylomelin-P) (P86163)
Organism: Aplysia dactylomela (Spotted sea hare)
Function: Catalyzes the oxidative deamination of positively charged L-amino acids L-Lys and L-Arg but not of amino acids L-His, L-Asp or L-Glu. Has antibacterial activity against the Gram-positive bacterium S.aureus (MIC=15 ug/ml). This antibacterial activity is bacteriostatic in the absence of amino acids L-Lys or L-Arg but bactericidal in their presence. The antibacterial effect is largely dependent on H(2)O(2) produced in the oxidative deamination of substrates. Has hemagglutinating activity towards rabbit erythrocytes. Hemagglutinating activity is inhibited by the glycoprotein fetuin, but not by glucose, mannose, galactose, N-acetylglucosamine, N-acetylgalactosamine or sialic acid.
Subcellular location: Secreted {ECO:0000269|PubMed:10758276, ECO:0000269|PubMed:16354780, ECO:0000269|Ref.1}.
Interaction partners:
Sequence:
DGVCSNRRQCNKEVCGSSYDVAIVGA
Protein: Long chain acyl-CoA synthetase 4 (EC 6.2.1.3) (Q9T0A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 3, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Acyl-coenzyme A oxidase 4, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Long chain acyl-CoA synthetase 9, chloroplastic
Sequence:
MSQQKKYIFQVEEGKEGSDGRPSVGPVYRSIFAKDGFPDPIEGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVYDIVMKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGADAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANEALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLAELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFIFDSAFSYKFGYMKKGQSHVEASPLFDKLVFSKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELGMLGTVGPPVPNVDIRLESVPEMEYDALASTARGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPDGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLIAIANPNQHILERWAAENGVSGDYDALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTINAKFASRG
Protein: Paxillin-like protein 1 (P36166)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Cytokinesis protein 2
- Cytokinesis protein 3
- GTP-binding protein RHO1
Sequence:
MYNSIYGSPFPKINPKVRYKTALERAGFDTKPRNPFSSQRNASTGSLQASVKSPPITRQRNVSAAPSVPVTMKSAYTASSKSAYSSVKGESDIYPPPVLENSERRSVTPPKNSNFTSSRPSDISRSISRPSERASQEDPFRFERDLDRQAEQYAASRHTCKSPANKEFQAADNFPFNFEQEDAGNTEREQDLSPIERSFMMLTQNDTASVVNSMNQTDNRGVLDQKLGKEQQKEESSIEYESEGQQEDENDIESLNFEPDPKLQMNLENEPLQDDFPEAKQEEKNTEPKIPEINVTRESNTPSLTMNALDSKIYPDDNFSGLESSKEQKSPGVSSSSTKVEDLSLDGLNEKRLSITSSENVETPYTATNLQVEQLIAQLDDVSLSRNAKLDMNGNCLNAVDRKASRFKKSSAYLSGYPSMDIPVTQQTSIVQNSNTNLSRQTILVDKGDVDEDAPSESTTNGGTPIFYKFKQSNVEYSNNEGMGSQETFRTKLPTIEALQLQHKRNITDLREEIDNSKSNDSHVLPNGGTTRYSSDADYKETEPIEFKYPPGEGPCRACGLEVTGKRMFSKKENELSGQWHRECFKCIECGIKFNKHVPCYILGDEPYCQKHYHEENHSICKVCSNFIEGECLENDKVERFHVDCLNCFLCKTAITNDYYIFNGEIPLCGNHDMEALLKEGIDNATSSNDKNNTLSKRRTRLINFN