wanglab/gogpt-training-data huggingface dataset:
Protein: Pleckstrin homology domain containing, family A member 5 (A0A0N4SUV0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTSEDKKERPISMINEASNYNMASDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIAMLTAEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKITTDSASTKETNNIPNHRVLIRPEVQNHQKNKEISKIEEKRALEAERYGFQKDGQDRPLTKINSVKLNSLLSEYESGPDCPPQNVHYRPINVNSSDGKAVNVSLADVRGGSHPNAGPLATEADRVIQRTNSMQQLEQWIKVQKGRGLEEEPRGVISYQTLPRNMPSHRAQILARCPEGYRTLPRNSKTRPESICSVTSSGHEKTGPGAEEKRRSMRDDTMWQLYEWQQRQFYHKQSTLPRHGCLSSPKAMVQVSDQTMHSIPTSPSHGSAAAYQGFSPQRTYRSEVTSPIQRGDVTIDRRHRPHHPKHVYVADRRSMPAGLTLQAVSPQSLQGRTVSVMTLLIICLLYLLPRKT
Protein: Late embryogenesis abundant (LEA) hydroxyproline-rich glycoprotein family (O82354)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADSEHVRPLAPATILPVSDESASNIKNTHRSRNRIKCSICVTATSLILTTIVLTLVFTVFRVKDPIIKMNGVMVNGLDSVTGTNQVQLLGTNISMIVDVSVKNPNTASFKYSNTTTDIYYKGTLVGEAHGLPGKARPHRTSRMNVTVDIMLDRILSDPGLGREISRSGLVNVWSYTRVGGKVKIMGIVKKHVTVKMNCTMAVNITGQAIQDVDCKKKIDL
Protein: Peptide methionine sulfoxide reductase A2 (AtMSRA2) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (Q9LY15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Prevents cellular oxidative damage in long nights. MSRA family specifically reduces the MetSO S-enantiomer.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Peptide methionine sulfoxide reductase B8
- Peptide methionine sulfoxide reductase B9
- Peptide methionine sulfoxide reductase B4
- Peptide methionine sulfoxide reductase B3
- Peptide methionine sulfoxide reductase B6
- Peptide methionine sulfoxide reductase B5
- Molybdenum cofactor sulfurase family protein
- Peptide methionine sulfoxide reductase B1, chloroplastic
- At1g21440
- Peptide methionine sulfoxide reductase B7
Sequence:
MDSSLKTQEPQVVETSPSPVAQEPPQVADKPAIVPSPIAQEPDNDVPAPGNEFAEFAAGCFWGVELAFQRIPGVTVTEVGYTHGISHNPSYEDVCTNTTNHAEVVRVQYDPKECTYETLLDLFWSRHNPTTLNRQGELLGAQYRSGIYFYTPEQEKLARESLEKEQKKLEDKIVTEILPAKKFYKAEEYHQQYLVKGGMHGNAQSPAKSCKDPIRCYG
Protein: Protein kinase C (EC 2.7.11.13) (H9G2Y7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKFFSSRTISSGGFWGKNKNKYALNGKVSPKDSVLLRKRRKIISRRYRRPSDERVVMLFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQVRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTRIAFDQLKIGSANDIWVDLEPHGQLHVVVEMHGTNVEDVHSHNKTRVFKERTNAFNDRQRRGAMRRKIHEVTGHKFMALFLRQPTFCAHCKEFIWGIGKQGYQCQICTVVVHKRCHEDVVWKCPGNKADAVEELGKEIQETGAGRFNINMPHRFSVHSYKRPTFCDHCGSMLYGLINQGLQCSTCKLNVHKRCQRNVANNCGINAKQMAAELAQLGLTGDKMSIRSKKKPSIMTDTSTDISGSSNSENSGYLQQISEDDSGTTSSRSASKVPGGTLSIHDFTFMKVLGKGSFGKVMLAERKGTDEVYAIKILKKDVIVQDDDVECTMCEKRILSLAAKHPFLTALHSSFQTSDRLFFVMEYVNGGDLMFQIQRARKFDESRARFYAAEVTCALQFLHRNDVIYRDLKLDNILLDAEGHCRLADFGMCKEGINKDNLTSTFCGTPDYIAPEILQEMEYGVSVDWWALGVLMYEMMAGQPPFEADNEDDLFEAILNDDVLYPVWLSKEAVNILKAFMTKNAGKRLGCVVSQGGEDAIRAHPFFREIDWDALESRQVKPPFKPKIKSKRDANNFDSDFTKEEPVLTPSDPAVVRAINQDEFRGFSFINPHFTY
Protein: Protein cereblon (Protein PiL) (Q8C7D2)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (By similarity). Maintains presynaptic glutamate release and consequently, cognitive functions such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus {ECO:0000250|UniProtKB:Q96SW2}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Cullin-4A
- DNA damage-binding protein 1
- E3 ubiquitin-protein ligase RBX1
- DNA-binding protein Ikaros
- Zinc finger protein Aiolos
- Cullin-4B
- E3 ubiquitin-protein ligase ZFP91
- Bromodomain-containing protein 4
- DDB1- and CUL4-associated factor 15
- Casein kinase I isoform alpha
Sequence:
MAGEGDQQDAAHNMGNHLPLLPADSEDEDDEIEMEVEDQDSKEARKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPEVLMILIPGQTLPLQLSHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQEFGIEVVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQVFPSKPISWEDQYSCKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPENPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTVHSWFPGYAWTIAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPETEDEISPDKVILCL
Protein: histone acetyltransferase (EC 2.3.1.48) (Q91XT0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGPTQSTAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQSHKMGMMSNPTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMPNMGQQPTPSVQQPGLVNPVAPGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQ
Protein: TBC1 domain family member 21 (Male germ cell Rab GTPase-activating protein) (Q8IYX1)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase-activating protein for Rab family protein(s). Essential for the establishment of male fertility, and is required for both the production of normal sperm number and sperm function (By similarity). Plays an important role in the formation of intact mitochondria, outer dense fibers and axoneme within the sperm tail (By similarity). Essential for sperm mitochondrial sheath formation and for the interactions of ARMC12 with VDAC2 and VDAC3 (By similarity). May be involved in acrosome formation and cytoskeletal reorganization during spermiogenesis, possibly by regulating RAB3A activity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9D9D3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9D9D3}. Note=Located at the edge of the acrosomal region, neck and annulus during spermiogenesis. Colocalizes with RAB3A at the acrosome-acroplaxome and neck regions of spermatids. Colocalizes with ACTB at the neck region in elongated spermatids. {ECO:0000250|UniProtKB:Q9D9D3}.
Interaction partners:
Sequence:
MTTLSPENSLSARQSASFILVKRKPPIDKTEWDSFFDESGHLAKSRDFICVNILERGLHPFVRTEAWKFLTGYFSWQSSQDERLTVDSMRRKNYKALCQMYEKIQPLLENLHRNFTETRNNIARDIQKIYDKDPLGNVLIDKKRLEKILLLSYVCNTQAEYQQGFHEMMMLFQLMVEHDHETFWLFQFFLQKTEHSCVINIGVAKNLDMLSTLITFLDPVFAEHLKGKGAGAVQSLFPWFCFCFQRAFKSFDDVWRLWEVLLTGKPCRNFQVLVAYSMLQMVREQVLQESMGGDDILLACNNLIDLDADELISAACVVYAELIQKDVPQTLKDFFL
Protein: ADAM metallopeptidase with thrombospondin type 1 motif A, isoform E (EC 3.4.24.-) (Q7KSH7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MSTHWRQNACLYACCIAFLLGMLIMFHLGLRSAHKGQEELPQSTHPLANSPPATPATLHPRRLDNDTSTDHEPPDGLDDLDEEEHSAFVMPTKVYNYSLSEADLIYESKRNSDINSFLKESASAFAMTGTYRNMSNEIWDPHPQYNLNVFGRQLHLVLRQDASFVHNHSMTHIRILKEGEEHPGPETEAEAEQRHLGCFYSGYVEDDPHSMVSVSLCGGMTGYIKTSFGALLIQPVNRTSSDEVLHRVFRKSQRNARHAVSKFELGLDDFMSKLEQVQEEEQKSKSRKLNRKKRHYADVDNQVYTLEVLIAVDNSMKQFHGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPNINDQTHSSNEMLKHFCQFINQSGYERDTAMLITREPICGSVPGKICHMLGLAELGTVCSSSSCSIVQDTGLPTAFTMAHELGHILNMNHDDDDKCMPYVTRQNNNKVLHIMSSVMGIHMHPWSWSKCSRHFVSEFLEKTDKSCLETSVGAHIPYGTERLPGEIYSLDAQCQLSFGNDFGYCPTDEECKRLWCNRTSGNSNEQCASSNLPWADGTPCGSSGHWCQRGKCVSNKHGYGRQVNGGWGPWTPFTPCSLTCGGGVQESRRECNQPVPENGGKYCTGSRKKYRSCNTHQCPPGSMDPREQQCYAMNGRNMNIPGVNPDTKWVPKYEKDACKLFCRMDMKVTYFMLKSMVTDGTSCAVDSFDKCVNGICRPAGCDNELNSIAKLDKCGVCEGRNDTCHEVTGNLLVSNLLGLNDGNEPNKTLYYVTRIPKGASNIIITQRGYPDQNFIVLTDDRDNELLNGKFLKTYPLKFVYAGVTMQYTGSSSVVEQVNTTYSWKLSRDLIVQIISLDVSPSKRQDTVLLSYSYTIDKPPDYEAEVEIYRWEMQAPSNCDSLCEGRSHRLPACISTTQGVKVAPQFCDKSAMPKIDDRACNTDCRLNLTVTSISECSAACGELGTREKTYACVQTFTNMQRSNIVDMSYCKLKFDVAYHEECREGCWVLSEWSTCSKSCGTGSQQREAHCYLHNSRVSDDLCNPRTKPHLNTLIGICNTESCPTYTKSPNALAVSNWVIGEWGECNEWCEKTRSVSCSHPYGIGCGSRKPKDVRKCCHIKYTSDWTDCSVQCGEGVKRKKQSCTRVYKPDVPGTRKRRVYVDESYCISRKVHRPKLRTTTKSCRINCKWNASDWRRCPADCSEEYQTRDVRCESFQGDGVEDKHCDAKKRPSKRRICNNCVRRQSRVISQCNCEGVEKRRDFCFNSHKGRIACPTRARVERHSCTPPPHCRRRSAIGSSISSRPRGTGVSSSRSLNSIGGSRNRGTPRSCADLKEMHGYNKDGNYQLEVRSRMVHIYCHGMNSRTPQEYVNVDPQENYSIYYEYRTKQTNSCPPESRGHEYYNDQNSGRTHFRKLRLNITDLRIMDNDFKFADSRGLAQKLGSAGDCYNRIGQCPQGDFSINMKDTDFSIRPGTVWRMHGQYSVMKRISEFDTTTQMRRGFCGGYCGGCYIAPDSGLYLDVL
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FTU1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Cell division control protein 42
- High osmolarity signaling protein SHO1
Sequence:
MKTAVLLSLLSAALAAPVANRFDDAINNYQNNADLGLASNSTNSDNANANANANANSGNIDVDANKVSSYLNSIASKAFVTTKSSKSNDYDDTYNSKFSTIDLSSSKSSDKNDFDWLSSSVVQSTPSISSIYSSNAYDTQIPSQVVSSNDFQLNSEIVSSVPSAEQISSDTISSVPSAEQISSDTISSVPSAEQIPSNVISVPSSIDSSFSVTPLSSSSSSSEEPTQYPISSSISSQIEQSSVIPSPVESVSSQIESDSSSSISDYLSSSTPTPIPSPPAESTERSELESSISISIPPIVPPTTSSEIVSSLEPSSVPFQSSSEDNTSTYISSQAQVVPSSVESIEPSSVPSEVPISTTTTSSPSQISSEYLSPTPSIFESPISQESTISSGSSFVESVISSELPKPPQPIISSDTSTESSILPQPSPSSVESNTISFPSSAVVTTTPQPPPVVESSESPLASSSSSSQIIVSSVDVPPSASVPVASSIPSVSVSSDPVAPSSVIPVDIPSSSSSSPPYVTPSPSTIISVPSPLPIDSSDTITSSQIIPSPEVPSPSSAIPSSSVSQPPIEIPSSSSESSSSSTSSNSNAWIPTSLIIAPTETESESTPTESNDGTQLSSLPKVIYGSAYSESVPEGYSVITIGFKKPLNYPFVVSESKSSAQIMYYLPKLLNANFESIFSDIKTVQLMPLEIQDSGYLSTVALLFFPTSEIQSLSNMVKNTSSSLYSTQYETITQSLSALIDPRIPVTGLTDTKTNNAGSSSSSSSNSNGRSSNSNQDTEHSSSFGNINSGSLDYIPSSKSASSDGTQSKTKKRIIPIIVGTIAGGMAVIIMLFLFFRYHAMKRREQLNQERLARLNFERASSCSDDSIERYNNEKQQYSDDVSSLSPSMKINKWMNDNHNVEHSTTTTDVNGSKKIIKISMPIATQNSLGWNDI
Protein: Endoprotease bli (EC 3.4.21.75) (Blisterase) (A0A044RE18)
Organism: Onchocerca volvulus
Function: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif.
Subcellular location: Secreted {ECO:0000305|PubMed:12855702}.
Interaction partners:
- G_PROTEIN_RECEP_F1_2 domain-containing protein.
- RING-type domain-containing protein.
- RING-type domain-containing protein.
- Uncharacterized protein.
- RING-type domain-containing protein.
- RING-type domain-containing protein.
- Uncharacterized protein.
- RING-type domain-containing protein
- RING-type domain-containing protein.
- RING-type domain-containing protein.
Sequence:
MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV
Protein: Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (P0A988)
Organism: Escherichia coli (strain K12)
Function: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases, repair factors and other proteins. Initially characterized for its ability to contact the alpha subunit (dnaE) of DNA polymerase III (Pol III), tethering it to the DNA and conferring very high processivity. Pol III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; it also exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication. A single clamp can bind both Pol III and IV, allowing the repair Pol IV to access DNA when it is damaged and needs to be fixed, a process the replicative polymerase cannot perform; when DNA is repaired Pol III takes over again. Serves as a processivity factor for DNA polymerases II, IV and V. A shorter protein beta* may be important for increasing survival after UV irradiation, and stimulates DNA synthesis with increased processivity in the presence of core Pol III plus the clamp loader complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23994470}. Note=Localizes to midcell position when chromosomes are condensed during DNA replication (PubMed:23994470). {ECO:0000269|PubMed:23994470}.
Interaction partners:
- Chromosomal replication initiator protein DnaA
- DnaA regulatory inactivator Hda
- DNA polymerase III subunit delta'
- DNA polymerase III subunit delta
- DNA polymerase IV
- DNA polymerase III subunit alpha
- DNA polymerase III subunit epsilon
- DNA polymerase III subunit tau
- Protein UmuC
- DNA polymerase I
Sequence:
MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALVQPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLDDWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVCSMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYVVMPMRL
Protein: Major pollen allergen Art v 1 (Defensin-like protein 1) (allergen Art v 1) (Q84ZX5)
Organism: Artemisia vulgaris (Mugwort)
Subcellular location: Secreted {ECO:0000305|PubMed:12475905}.
Interaction partners:
Sequence:
MAKCSYVFCAVLLIFIVAIGEMEAAGSKLCEKTSKTYSGKCDNKKCDKKCIEWEKAQHGACHKREAGKESCFCYFDCSKSPPGATPAPPGAAPPPAAGGSPSPPADGGSPPPPADGGSPPVDGGSPPPPSTH
Protein: Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) (ARF guanine-nucleotide exchange factor BIG1) (F4JSZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Soluble and partially membrane-bound. {ECO:0000250}.
Interaction partners:
- Nucleolar GTP-binding protein 1
- Nucleolar GTP-binding protein 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Villin-4
- Gamma-secretase subunit APH1-like
- Fatty acyl-CoA reductase 1
Sequence:
MSSSQNLGGATRCGRVIGPSLDKIIKNAAWRKHTFLVSACKSVLDKLEALSDSPDPSSPLFGLTTSDADAVLQPLLLSLDTGYAKVIEPALDCSFKLFSLSLLRGEVCSSSPDSLLYKLIHAICKVCGIGEESIELAVLRVLLAAVRSPRILIRGDCLLHLVRTCYNVYLGGFNGTNQICAKSVLAQIMLIVFTRSEANSMDASLKTVNVNDLLAITDKNVNEGNSVHICQGFINDVITAGEAAPPPDFALVQPPEEGASSTEDEGTGSKIREDGFLLFKNLCKLSMKFSSQENTDDQILVRGKTLSLELLKVIIDNGGPIWLSDERFLNAIKQLLCLSLLKNSALSVMSIFQLQCAIFTTLLRKYRSGMKSEVGIFFPMLVLRVLENVLQPSFVQKMTVLSLLENICHDPNLIIDIFVNFDCDVESPNIFERIVNGLLKTALGPPPGSSTILSPVQDITFRHESVKCLVSIIKAMGTWMDQQLSVGDSLLPKSLENEAPANNHSNSNEEDGTTIDHDFHPDLNPESSDAATLEQRRAYKIERQKGVTLFNRKPSKGIEFLISSKKVGNSPDEVVSFLRNTTGLNATMIGDYLGEREDFPMKVMHAYVDSFDFKEMNFGEAIRFFLRGFRLPGEAQKIDRIMEKFAERFCKCNPNSFSSADTAYVLAYSVIMLNTDAHNIMVKEKMTKADFIRNNRGIDDGKDLPEEYLGALYDQVVINEIKMSSDSSAPESRQSNGLNKLLGLDGILNLVYWTQTEEKAVGANGLLIKDIQEKFRSKSGKSESAYHVVTDVAILRFMVEVSWGPMLAAFSVTLDQSDDRLAAVECLRGFRYAVHVTAVMGMQTQRDAFVTSMAKFTNLHCAGDMKQKNVDAVKAIISIAIEDGNHLQDAWEHILTCLSRIEHLQLLGEGAPSDASYFASTETEEKKALGFPNLKKKGALQNPVMMAVVRGGSYDSSTIGPNMPGLVKQDQINNFIANLNLLDQIGSFQLNNVYAHSQRLKTEAIVAFVKALCKVSMSELQSPTDPRVFSLTKLVEIAHYNMNRIRLVWSRIWSILSDFFVSVGLSENLSVAIFVMDSLRQLSMKFLEREELANYNFQNEFLRPFVIVMQKSSSAEIRELIVRCISQMVLSRVSNVKSGWKSVFKVFTTAAADERKNIVLLAFETMEKIVREYFSYITETEATTFTDCVRCLITFTNSTFTSDVSLNAIAFLRFCALKLADGGLVWNEKGRSSSPSTPVTDDHSPSTQNFMDADENISYWVPLLTGLSKLTSDSRSAIRKSSLEVLFNILKDHGHIFSRTFWIGVFSSVIYPIFNSVWGENDLLSKDEHSSFPSTFSSHPSEVSWDAETSAMAAQYLVDLFVSFFTVIRSQLSSVVSLLAGLIRSPAQGPTVAGVGALLRLADELGDRFSENEWKEIFLAVNEAASLTLSSFMKTLRTMDDIPDEDTLSDQDFSNEDDIDEDSLQTMSYVVARTKSHITVQLQVVQVVTDLYRIHQQSLLASHVTVILEILSSISSHAHQLNSDLILQKKVRRACSILELSEPPMLHFENDTFQNYLDILQAIVTNNPGVSLELNVESQLMTVCMQILKMYLKCTLFQGDELEETRQPKNWILPMGAASKEEAAARSPLVVAVLKALRELKRDSFKRYAPNFFPLLVELVRSEHSSSQVPQVLSTVFHTCMGAMMDE
Protein: Phosphotransferase (EC 2.7.1.-) (A2R0H3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSSALLDEAARIARQFDYPAAEVQRGVTEYIREIDEGLSKEHTTLSQIPTYVTAVPNGTEKGLYLAVDLGGTNFRVCSIDLHGDTTFSLTQSKIMIPRETMASGTAKDLFLFLARQIESFLRIHHNDHFEAHLRRRNEKNGNCEEDLFDLGFTFSFPVRQLGINKGTLIRWTKGFNIPDAVGKDVCALLQNAIDDLGLPVRVAALVNDTVGTLMARSYTSPGETGTFLGAIFGTGTNGAYVEKLDRITKLQTIEHSEYDKTTGEMIINAEWGSFDNHLSVLPNTIYDQQLDADSNNPGIQMFEKRVSGMFLGEILRRVMLDMQRNESLGFLRAGGASTVSVPQESSLYRQWGIDTSLLSLVEADKTENMEQIKVALKDHLKIERPTTDDCKAIQTVVHAIGKRAARLSAVPLAAILLSTGKLQKDDLVDIGVDGSLVEFYPNFEGYMRDALREVPEVGEAGNKKIRIGISKDGSGVGAALIALVASKEEARRKSQ
Protein: Neuroblastoma suppressor of tumorigenicity 1 (N03) (Zinc finger protein DAN) (Q61477)
Organism: Mus musculus (Mouse)
Function: Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process.
Subcellular location: Secreted {ECO:0000269|PubMed:23063586}.
Interaction partners:
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Bone morphogenetic protein 7
- Growth/differentiation factor 5
- Bone morphogenetic protein 6
- Growth/differentiation factor 7
- Growth/differentiation factor 6
- Muellerian-inhibiting factor
- Bone morphogenetic protein 5
- Bone morphogenetic protein 8B
Sequence:
MLWVLVGAVLPVMLLAAPPPINKLALFPDKSAWCEAKNITQIVGHSGCEAKSIQNRACLGQCFSYSVPNTFPQSTESLVHCDSCMPAQSMWEIVTLECPGHEEVPRVDKLVEKIVHCSCQACGKEPSHEGLNVYVQGEDSPGSQPGPHSHAHPHPGGQTPEPEEPPGAPQVEEEGAED
Protein: protein-secreting ATPase (EC 7.4.2.8) (A0A0H3NB84)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKNELMQRLRLKYPPPDGYCRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEVCGPELLIEKLHQILTE
Protein: EG:163A10.1 protein (O97174)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKRMRSSRLLVLPLILVLILTLLLQPIAVHAKSKKNKSSQSSHHGDSSSSSSSSSSSSGSSSAAASSANDESKPKGGDNGGQHFAMEPQDQTAVVGSRVTLPCRVMEKVGALQWTKDDFGLGQHRNLSGFERYSMVGSDEEGDFSLDIYPLMLDDDAKYQCQVGPGPQGEQGIRSRFAKLTVLVPPEAPKITQGDYLVTTEDREIELECVSQGGKPAAEITWIDGLGNVLTKGIEYVKEPLADSRRITARSILKLAPKKEHHNTTFTCQAQNTADRTYRSAKLLLEVKYAPKVIVSVVGGALAGGKIPEGAEVILSCQADANPHELSYRWFINDELMTGDFTTKMIIHNVSRQYHDAIVKCEVVNAVGKSEQSKKLDISCKYSMAISDDIFRQRPVSVEADLGATVSMRCDVAGNPEPEIEWISENSDQVVGVAAELKLKVSSETAGRYFCKAVVNGFPEIGAEATLYVKRAPIITSHKVQFGGVGGRVKIDCLAFSIPKAEHILWSFEGKIINMSSADPDIYIFEEHHLPEGVRAALIIRDSKATHFGKYNCTVLNSYGGDSLVITLLREPGNIPVLLVVMGSMFCVAIILMIVMIIIVYRKRRSRKKPMPADVIPEASRGGDKLNELKSELRSKAYDVEYSEAGGDGLAINLTQSPMPDVQMKGATLGVPLAGPVKFDERFSGDFGGDRYNRQCHIKNLKNQQETAYKGSPQANGYAHYFEYALDYSPPGGEGAAVVVGSGGVGKLKNGGMNSATLPHSAAATVNGGGAGNGGGASLPRNQRHEIQQSQQSNGFLGNETDVISTTFAGQPLLQNGIDSRFSAIYGNPYLRTNSSLLPPLPPPSTANPAATPAPPPYHAARHGHAHHANGGLKHFVGGAVITTSPVGNVNINGGGGGGSTPSGGGGVGVGVAAGGSVSGSSSNLTASSNTLAATPLAGGGVGNSGQCAQSPSGQFILSNNGKGHTQKGPLATHV
Protein: G protein alpha q subunit (Guanine nucleotide-binding protein G(q) subunit alpha) (Guanine nucleotide-binding protein alpha-q) (dGQalpha) (P23625)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Could be the transducin analog, an amplifier and one of the transducers of a visual impulse that performs the coupling between opsin and cGMP-phosphodiesterase. Could mediate a subset of olfactory and gustatory responses.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:10608815}. Cell projection, rhabdomere {ECO:0000269|PubMed:10608815}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Guanine nucleotide-binding protein subunit gamma-e
- Guanine nucleotide-binding protein subunit beta-2
- Opsin Rh1
- Inactivation-no-after-potential D protein
- G protein beta subunit 5
- Neither inactivation nor afterpotential protein C
- Protein kinase C, eye isozyme
- Transient-receptor-potential-like protein
- Guanine nucleotide-binding protein subunit beta-1
Sequence:
MECCLSEEAKEQKRINQEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGYIKLVFQNIFMAMQSMIKAMDMLKISYGQGEHSELADLVMSIDYETVTTFEDPYLNAIKTLWDDAGIQECYDRRREYQLTDSAKYYLSDLARIEQADYLPTEQDILRARVPTTGILEYPFDLDGIVFRMVDVGGQRSERRKWIHCFENVTSIIFLVALSEYDQILFESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPKQDHAAAKQFVLKKYLACNPDPERQCYSHFTTATDTENIKLVFCAVKDTIMQNALKEFNLG
Protein: Vanillin dehydrogenase (EC 1.2.1.67) (O05619)
Organism: Pseudomonas sp. (strain HR199 / DSM 7063)
Function: Catalyzes the NAD-dependent oxidation of vanillin to vanillic acid.
Interaction partners:
Sequence:
MFHVPLLIGGKPCSASDERTFERRSPLTGEVVSRVAAASLEDADAAVAAAQAAFPEWAALAPSERRARLLRAADLLEDRSSEFTAAASETGAAGNWYGFNVYLAAGMLREAAAMTTQIQGDVIPSNVPGSFAMAVRQPCGVVLGIAPWNAPVILGVRAVAMPLACGNTVVLKSSELSPFTHRLIGQVLHDAGLGDGVVNVISNAPQDAPAVVERLIANPAVRRVNFTGSTHVGRIIGELSARHLKPAVLELGGKAPFLVLDDADLDAAVEAAAFGAYFNQGQICMSTERLIVTAVADAFVEKLARKVATLRAGDPNDPQSVLGSLIDANAGQRIQVLVDDALAKGARQVVGGGLDGSIMQPMLLDQVTEEMRLYREESFGPVAVVLRGDGDEELLRLANDSEFGLSAAIFSRDVSRAMELAQRVDSGICHINGPTVHDEAQMPFGGVKSSGYGSFGSRASIEHFTQLRWLTIQNGPRHYPI
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (M9PE88)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein decapentaplegic
- Protein 60A
- Mothers against decapentaplegic homolog
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Serine/threonine-protein kinase receptor
- Dorsal-ventral patterning protein Sog
- Fibroblast growth factor
- receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
Sequence:
MNWAIYLLLALISLGRATPVPNRQYSCMSYQEDDNSFHDDDGDQDSSGELQEQQVESTPIPSEPHRRTCPDGYTFCFTIWNQTANGARVVKQGCWKDNTDRTSICSQSECTSSAPTSKTSSLYYCCCSGGVCNAQYSVVEPAPLELGSNEGRTSITNRATEKQHQSFLASTMLGLAGGLTALTIGIFLAVQYCRTAKEKPEPEESPLAPSGPGYSSNLRNVDNMNLIGMLGSGKYGTVMKGLLHDQEVAVKIYPEEHHQYYVNERNIYALPLMECPALLSYFGYDERCTMDGRMEYQLVLSLAPLGCLQDWLIANTLTFSECCGMLRSITRGISHLHTELRLGDQHKPCVAHRDINTRNVLVQADLSCCIADFGFALKVFGSKYEYKGEVAMAETKSINEVGTLRYMAPELLEGAVNLRDCETSLKQMDVYALGLVLWEVATRCSDFYAPGQATPPYKAPYEQEVGSHPSFDQMQALVVRHKARPLFPTGWGGGAAAKVVRDTCEDCWDHDADARLTSLCAEERMQEMSTLRPRAQAQPSSPLLNTNNLVASPTAEQGINIIATTTTAAAVHHQMSSDTTGLIQPPPNQQIPLAALEREKNHLSYPQQQLQPYQGRNPCQERNLAPLTMRTPPVLVERSKKHSFQTQPQENSLSCLEHDVSVEELIASHQHQQQKNTIVSTGGNGNSCLGQGFPKQQNTDQKLRGWHGVRALIHKKLFRKEHAEELCRQLQLGEEKSNLVTALRRPNNLDLNPRLDKPPPDQLRSAEQRMGTPAHIVPRSLSSSLIKHINGTTNNNSIQSHGSELQTLTRPASKRRPGHLRTNSLMATTGQGPPTEQQMRRQHSLEVFREVFSGRGSSERLRDPSERVKTPGDVPPSVRKARASKTLSLYDDRMMDSSLLNILXHEEVLLLEL