wanglab/gogpt-training-data huggingface dataset:
Protein: Albumin (P08835)
Organism: Sus scrofa (Pig)
Function: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Beta-lactoglobulin-1A/1C
- Lactoperoxidase
- Plasminogen
- Insulin
- Alpha-lactalbumin
- Lactotransferrin
- Alpha-2-HS-glycoprotein
- Prothrombin
- Ovalbumin isoform X1
- SPARC
Sequence:
MKWVTFISLLFLFSSAYSRGVFRRDTYKSEIAHRFKDLGEQYFKGLVLIAFSQHLQQCPYEEHVKLVREVTEFAKTCVADESAENCDKSIHTLFGDKLCAIPSLREHYGDLADCCEKEEPERNECFLQHKNDNPDIPKLKPDPVALCADFQEDEQKFWGKYLYEIARRHPYFYAPELLYYAIIYKDVFSECCQAADKAACLLPKIEHLREKVLTSAAKQRLKCASIQKFGERAFKAWSLARLSQRFPKADFTEISKIVTDLAKVHKECCHGDLLECADDRADLAKYICENQDTISTKLKECCDKPLLEKSHCIAEAKRDELPADLNPLEHDFVEDKEVCKNYKEAKHVFLGTFLYEYSRRHPDYSVSLLLRIAKIYEATLEDCCAKEDPPACYATVFDKFQPLVDEPKNLIKQNCELFEKLGEYGFQNALIVRYTKKVPQVSTPTLVEVARKLGLVGSRCCKRPEEERLSCAEDYLSLVLNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYKPKEFVEGTFTFHADLCTLPEDEKQIKKQTALVELLKHKPHATEEQLRTVLGNFAAFVQKCCAAPDHEACFAVEGPKFVIEIRGILA
Protein: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 (EC 1.14.11.33) (EC 1.14.11.54) (Alkylated DNA repair protein alkB homolog 3) (hABH3) (DEPC-1) (Prostate cancer antigen 1) (Q96Q83)
Organism: Homo sapiens (Human)
Function: Dioxygenase that mediates demethylation of DNA and RNA containing 1-methyladenosine (m1A). Repairs alkylated DNA containing 1-methyladenosine (m1A) and 3-methylcytosine (m3C) by oxidative demethylation. Has a strong preference for single-stranded DNA. Able to process alkylated m3C within double-stranded regions via its interaction with ASCC3, which promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3. Can repair exocyclic 3,N4-ethenocytosine adducs in single-stranded DNA. Also acts on RNA. Demethylates N(1)-methyladenosine (m1A) RNA, an epigenetic internal modification of messenger RNAs (mRNAs) highly enriched within 5'-untranslated regions (UTRs) and in the vicinity of start codons. Requires molecular oxygen, alpha-ketoglutarate and iron.
Subcellular location: Nucleus {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:29144457}. Cytoplasm {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:17979886}. Note=Colocalizes with ASCC2 and ASCC3 in nuclear foci when cells have been exposed to alkylating agents that cause DNA damage (PubMed:29144457). Predominantly localizes to the nucleus. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:29144457}.
Interaction partners:
- Nucleic acid dioxygenase ALKBH1
- Activating signal cointegrator 1 complex subunit 3
- Activating signal cointegrator 1 complex subunit 2
- Activating signal cointegrator 1 complex subunit 1
- Activating signal cointegrator 1
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- tRNA
- RNA demethylase ALKBH5
- tRNA
Sequence:
MEEKRRRARVQGAWAAPVKSQAIAQPATTAKSHLHQKPGQTWKNKEHHLSDREFVFKEPQQVVRRAPEPRVIDREGVYEISLSPTGVSRVCLYPGFVDVKEADWILEQLCQDVPWKQRTGIREDITYQQPRLTAWYGELPYTYSRITMEPNPHWHPVLRTLKNRIEENTGHTFNSLLCNLYRNEKDSVDWHSDDEPSLGRCPIIASLSFGATRTFEMRKKPPPEENGDYTYVERVKIPLDHGTLLIMEGATQADWQHRVPKEYHSREPRVNLTFRTVYPDPRGAPW
Protein: Interleukin-1 (A0A060Z0U0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
- Ig-like domain-containing protein
- Interleukin 1 receptor accessory protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Caspase a
- Caspase-1
- Iceberg protein
- Uncharacterized protein
- CARD domain-containing protein
Sequence:
MEFESNCSLMKNTSASVAWSSKLPQGLDVEISHHPITLRCVANLIIAMERLNGGKGFTLGRDEGLLNFLLESAVEVLELESARTEASSRAAFSSKGEYECSVTDSENKCWVLNEGSMELHAIMLQGGSSYHKVHLNLSTYITPVPSETKARPVALGIKGSNLYLSCITSEGTPTLHLEEVADKEQLKSINHESDMVRFLFYKQDTGVDISTLESAHYRNWFISTALQQDNTKMVNMCQRATLNRNTTFTVQRHN
Protein: Transmembrane ascorbate ferrireductase 1 (EC 7.2.1.3) (Cytochrome b561) (Artb561-1) (AtCytb561) (Protein b561A.tha5) (Tonoplast Cyt-b561) (TCytb) (Q8L856)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent trans-membrane ferric-chelate reduction. Able to use dihydrolipoic acid (DHLA) as an alternative substrate to ascorbate.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14730083}; Multi-pass membrane protein {ECO:0000269|PubMed:14730083}.
Interaction partners:
- Cytochrome b561 and DOMON domain-containing protein At3g07570
- At1g52870/F14G24_14 family protein)
- Actin cross-linking protein
- At1g80480
- Electron carrier/ protein disulfide oxidoreductase
- At3g13062
- Mitotic-spindle organizing protein 1A
- Metallo-beta-lactamase family protein
Sequence:
MAVRINAMAVTFVAHALAVIAAIMVLVWSISYRGGLAWEATNKNLIFNLHPVLMLIGFIILGGEAIISYKSLPLEKPVKKLIHLILHAIALALGIFGICAAFKNHNESHIPNLYSLHSWIGIGVISLYGFQWVYSFIVFFFPGGSTNLKSGLLPWHAMLGLFVYILAVGNAALGFLEKLTFLENGGLDKYGSEAFLINFTAIITILFGAFVVLTASAESPSPSPSVSNDDSVDFSYSAI
Protein: transketolase (EC 2.2.1.1) (Q7KSU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNNLRKIDSDLEGHPTPRLNFIDVGTGSLGQGVAVGAGMAYVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAEVVKHLEGLIVNKNVKLTPKPVPKTGAAPDVDINNIKLSSPPAYKLGDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTCVIYDNEEPFTIGRGKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCGGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEILKD
Protein: UDP-glycosyltransferase 73C5 (EC 2.4.1.-) (Cytokinin-O-glucosyltransferase 3) (Deoxynivalenol-glucosyl-transferase 1) (Zeatin O-glucosyltransferase 3) (AtZOG3) (Q9ZQ94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically catalyzes 23-O-glucosylation of brassinosteroids, resulting probably in their inactivation. Also, involved in the O-glucosylation of trans-zeatin and dihydrozeatin. Active in vitro on cis-zeatin, dihydrozeatin-9-N-Glc, and olomoucine. Also involved in the detoxification of the Fusarium mycotoxin deoxynivalenol by the transfer of glucose from UDP-glucose to the hydroxyl group at C-3. Possesses low quercetin 7-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytosolic sulfotransferase 10
- BAHD acyltransferase BIA1
- Cytochrome P450 72C1
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90D1
Sequence:
MVSETTKSSPLHFVLFPFMAQGHMIPMVDIARLLAQRGVIITIVTTPHNAARFKNVLNRAIESGLPINLVQVKFPYLEAGLQEGQENIDSLDTMERMIPFFKAVNFLEEPVQKLIEEMNPRPSCLISDFCLPYTSKIAKKFNIPKILFHGMGCFCLLCMHVLRKNREILDNLKSDKELFTVPDFPDRVEFTRTQVPVETYVPAGDWKDIFDGMVEANETSYGVIVNSFQELEPAYAKDYKEVRSGKAWTIGPVSLCNKVGADKAERGNKSDIDQDECLKWLDSKKHGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFIWVIRGWEKYKELVEWFSESGFEDRIQDRGLLIKGWSPQMLILSHPSVGGFLTHCGWNSTLEGITAGLPLLTWPLFADQFCNEKLVVEVLKAGVRSGVEQPMKWGEEEKIGVLVDKEGVKKAVEELMGESDDAKERRRRAKELGDSAHKAVEEGGSSHSNISFLLQDIMELAEPNN
Protein: Salt tolerance receptor-like cytoplasmic kinase 1 (EC 2.7.12.1) (Receptor-like cytoplasmic kinase 154) (OsRLCK154) (Q7XR88)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts probably as a dual specificity protein kinase (Probable). Regulates hydrogen peroxide (H(2)O(2)) homeostasis and improves salt tolerance by phosphorylating tyrosine residues of CATC thus activating its catalase activity. Promotes growth at the seedling stage and prevents grain yield loss under salt stress conditions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29581216, ECO:0000269|PubMed:38180963}; Lipid-anchor {ECO:0000269|PubMed:29581216, ECO:0000269|PubMed:38180963}.
Interaction partners:
Sequence:
MFTGCGLFACVRRCDGGDVRKRGEAGAMSSRVAADPAGVEEEGSCKNVAAASARQLAWADVESVTGGFSSRVIGHGGFSTVYLASLSSSRLGAVKVHCSSERLHRAFRQELEVLLSLRHPHIVRLLGYCDERDEGVLVFEYAPNGDLHERLHCSEVAGGVASVLPWARRVAIAFQVAMALEYLHESRHPAVIHGDIKASNVLLDANMNAKLCDFGFAHVGFSATVGCRPSARAVMGSPGYVDPHLIRSGVATKKSDVYSFGVLLLELVTGKEAVCRDTGRRLTAAVGPMLSEGKVADVVDRRLGGEHDGAEAAVMAELAMQCIGDSPGLRPSMADVVRALQEKTSALASAVGSRLDRKMMF
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (G3V9P8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Large ribosomal subunit protein uL14
- Glucose-6-phosphate isomerase
- Poly [ADP-ribose] polymerase
- 40S ribosomal protein S15
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS19
- Ribosomal_L18_c domain-containing protein.
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL5
Sequence:
MDIKGQFWNDDDSEGDNESEEFLYGVQGSCAADLYRHPQLDADIEAVKEIYSENSVSIREYGTIDDVDIDLHINISFLDEEVSTAWKVLRTEPIVLRLRFSLSQYLDGPEPSIEVFQPSNKEGFGLGLQLKKILYMFTSQQWKHLSNDLLKTQQEKRHSWFKASGSIRKFRAGLSIFSPIPKSPSFPIIQDSMLKGKLGVPELRVGRLMNRSISCTMKNPKVEVFGYPPSPQAGLLCPQHVGLPPPARTSPLVSGHCKNIPTLEYGFLVQIMKYAEQRVPTLNEYCVVCDEQHVFQNGSMLKPAVCTRELCVFSFYTLGVMSGAAEEVATGAEVVDLLVAMCRAALESPRKSIIFEPYPSVVDPTDPKTLAFNPKKKNYERLQKALDSVMSIREMTQGSYLEIKKQMDKLDPLAHPLLQWIISSNRSHIVKLPLSRQLKFMHTSHQFLLLSSPPAKEARFRTAKKLYGSTFAFHGSHIENWHSILRNGLVNASYTKLQLHGAAYGKGIYLSPISSISFGYSGMGKGQHRMPSKDELVQRYNRMNTIPQTRSIQSRFLQSRNLNCIALCEVITSKDLQKHGNIWVCPVSDHVCTRFFFVYEDGQVGDANINTQDPKIQKEIMRVIGTQVYTN
Protein: Regulating synaptic membrane exocytosis protein 1 (Rab-3-interacting molecule 1) (RIM 1) (Rab-3-interacting protein 1) (Q99NE5)
Organism: Mus musculus (Mouse)
Function: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Protein unc-13 homolog B
- Ras-related protein Rab-3A
- Protein unc-13 homolog A
- Syntaxin-binding protein 1
- ELKS/Rab6-interacting/CAST family member 1
- Synaptosomal-associated protein 25
- Syntaxin-1A
- Peripheral-type benzodiazepine receptor-associated protein 1
- Synapsin-1
- Complexin-1
Sequence:
MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAESQPHQPPLNIFRCVCVPRKPSSEEGGPDRNWRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQPSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAVSSQDTASHGAPLDRNKGAEPSQQALGPEQKQASRSRSEPPRERKKAPGLSEQNGKGGQKSERKRVPKSVVQPGEGTADERERKERRETRRLEKGRSQDYPDRLEKREDGRVAEDEKQRKEEEGVSTPEYTSCEDVELESESVSEKGDLDYWLDPATWHSRETSPISSHPVTWQPSKEGDRLIGRVILNKRTTMPKESGALLGLKVVGGKMTDLGRLGAFITKVKKGSLADVVGHLRAGDEVLEWNGKPLPGATNEEVYNIILESKSEPQVEIIVSRPIGDIPRIPESSHPPLESSSSSFESQKMERPSISVISPTSPGALKDAPQVLPGQLSVKLWYDKVGHQLIVNVLQATDLPPRVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKLLEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQDEESEFLGEILIELETALLDDEPHWYKLQTHDESSLPLPQPSPFMPRRHIHGESSSKKLQRSQRISDSDISDYEVDDGIGVVPPVGYRASARESKATTLTVPEQQRTTHHRSRSVSPHRGDDQGRPRSRLPNVPLQRSLDEIHPTRRSRSPTRHHDASRSLADHRSRHAESQYSSEPDSELLMLPRAKRGRSAECLHMTSELQPSLDRARSASTNCLRPDTSLHSPERERGRWSPSLARRRPASPRIQIQHASPENDRHSRKSERSSIQKQSRKGTASDADRVLPPCLSRRGYAIPRATDQPVIRGKHTTRSRSSEHSSIRTLCSMHHLAPGGSAPPSPLLTRTHRQGSPTQSPPADTSFGSRRGRQLPQVPVRSGSIEQASLVVEERTRQMKMKVHRFKQTTGSGSSQELDHEQYSKYNIHKDQYRSCDNASAKSSDSDVSDVSAISRASSTSRLSSTSFMSEQSERPRGRISSFTPKMQGRRMGTSGRAIIKSTSVSGEIYTLEHNDGSQSDTAVGTVGAGGKKRRSSLSAKVVAIVSRRSRSTSQLSQTESGHKKLKSTIQRSTETGMAAEMRKMVRQPSRESTDGSINSYSSEGNLIFPGVRVGPDSQFSDFLDGLGPAQLVGRQTLATPAMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQILLEELDLSSMVIGWYKLFPPSSLVDPTLTPLTRRASQSSLESSSGPPCIRS
Protein: Kekkon 1, isoform B (Kekkon 1, isoform C) (Q9VK54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Epidermal growth factor receptor
- Protein gurken
Sequence:
MHIREAVFLVLTLLPGMILGTRYNQLHLYANGGASSSGPGGYRPAPSSQNEVYSIADSQPMTEDGYMPPSQHFPPTHSDLDPPAQQQSTCQTVCACKWKGGKQTVECIDRHLIQIPEHIDPNTQVLDMSGNKLQTLSNEQFIRANLLNLQKLYLRNCKIGEIERETFKGLTNLVELDLSHNLLVTVPSLALGHIPSLRELTLASNHIHKIESQAFGNTPSLHKLDLSHCDIQTISAQAFGGLQGLTLLRLNGNKLSELLPKTIETLSRLHGIELHDNPWLCDCRLRDTKLWLMKRNIPYPVAPVCSGGPERIIDRSFADLHVDEFACRPEMLPISHYVEAAMGENASITCRARAVPAANINWYWNGRLLANNSAFTAYQRIHMLEQVEGGFEKRSKLVLTNAQETDSSEFYCVAENRAGMAEANFTLHVSMRAAGMASLGSGQIVGLSAALVALIVFALGVIMCLLLRVKRQPYVDSKTPNHMEVITSVNHQNSITNKTQPATGNGSIGGVVIANGAVANIIDGGVVQGGTLERKSSGRGGVPHGVHDQRSANPVQKPPRLTDLPYSTQGYDNNGSVLSTASCFISPSGSTGNGGNNPDLINDTKRFGSDEFADLKIPPISGVGVGGSGEYSRANGCDSLYPSGLWEHGAPVGTTSADDLFMKRYTDKTPIIDSTQLYDLHERTAATDYFSKTFPRSHLQQGMMTGGGGGTSTASTVTTNLSGGSSSGYPNDYGLPLVPGAEHQHNHQLQMHPLQQLQQQLTSTLNHQKQEGSSTGSSPHFSSRTLPRLHEGSGGGGSSRSSPTPAVSGGHANQAANPSTSSSSCSILPNGQPINAKTIRVWQKGGVPVLPPVTALKRALISSSRNSPDEGYQEGCGTDV
Protein: Friend of echinoid, isoform F (M9NCR3)
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:
MSTIKLLIIGQLWLSIGLISGDDSLDTREGVDLVLKCRFTEHYDSTDFTFYWARWTCCPTLFENVAIGDVQLNSNYRLDFRPSRGIYDLQIKNTSYNRDNGRFECRIKAKGTGADVHQEFYNLTVLTAPHPPMVTPGNLAVATEEKPLELTCSSIGGSPDPMITWYREGSTVPLQSYALKGGSKNHYTNATLQIVPRRADDGAKYKCVVWNRAMPEGHMLETSVTLNVNYYPRVEVGPQNPLKVERDHVAKLDCRVDAKPMVSNVRWSRNGQYVSATPTHTIYRVNRHHAGKYTCSADNGLGKTGEKDIVLDVLYPPIVFIESKTHEAEEGETVLIRCNVTANPSPINVEWLKEGAPDFRYTGELLTLGSVRAEHAGNYICRSVNIMQPFSSKRVEGVGNSTVALLVRHRPGQAYITPNKPVVHVGNGVTLTCSANPPGWPVPQYRWFRDMDGDIGNTQKILAQGPQYSIPKAHLGSEGKYHCHAVNELGIGKIATIILEVHQPPQFLAKLQQHMTRRVGDVDYAVTCSAKGKPTPQIRWIKDGTEILPTRKMFDIRTTPTDAGGGVVAVQSILRFRGKARPNGNQLLPNDRGLYTCLYENDVNSANSSMHLRIEHEPIVIHQYNKVAYDLRESAEVVCRVQAYPKPEFQWQYGNNPSPLTMSSDGHYEISTRMENNDVYTSILRIAHLQHSDYGEYICRAVNPLDSIRAPIRLQPKGSPEKPTNLKILEVGHNYAVLNWTPGFNGGFMSTKYLVSYRRVATPREQTLSDCSGNGYIPSYQISSSSSNSNHEWIEFNCFKENPCKLAPLDQHQSYMFKVYALNSKGTSGYSNEILATTKVSKIPPPLHVSYDPNSHVLGINVAATCLSLIAVVESLVTRDATVPMWEIVETLTLLPSGSETTFKEAIINHVSRPAHYTTATTSGRSLGVGGGSHLGEDRTMALAETAGPGPVVRVKLCLRSNHEHCGAYANAEIGKSYMPHKSSMTTSALVAIIIASLSFVVFLGLLYAFCHCRRKHAAKKESSSVGGGVGGGNANATANPGSTGAKEYDLDLDASRRPSLSQDPQQSQQQPPPPPPYYPTGTLDSKDIGNGNGGMELTLTALHDPDEQLNMQQQQHHSNHGQYQQPKAILGIYGGVAGSGGNNSGGQHPHSNGYGYHVTSAIGVDSDSYQVLPSVANSAAGSHGHGSGHGHGLGAGEWSSSNSNENNYSNARDLSQEALWRLQMATAQSQQIYVERPPSAFSGLVDYSGYSPHIPTVTSSLSQQSFSPTQQLAPHEMLQAAQRYGTLRKSGKQPPLPPQRKDMQQQAKPPQQMADIIQDLAN
Protein: LD02329p (Q8MRJ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
Sequence:
MAVKVQFEIGHTSKLRSKKTPHPQAFTHDWEIYVQGVNKADISAFVEKVVFVLHESFPKPKRVVKEPPYAIQESGYAGFLLPVEIYFRNRDEPKRIVYQYDLVLQSTGPPQHHVEVKTHIFEAPSEEFRTKLMRGGGVPVFGANIGAGSLARTLSPSVGSGETAHSNEMSGVKAKGVPGTISMNSDLNTGKKHKSRSEDPGKSNAFSALFGPPITKTSVTANNMAQVPVSKHSPEAKSAAVGGKGVFHEGREKASKDRDKSSGGDKPREKDKKDRHGRDKDRKSSKSGDGKHERDKEKSKKDKSRDKEREREQGSGNTTSANALTVATSVGTAGGLVKHTASPKPGKPNEMGAPSPKKTANDSAAGAVAPTSRSKERDEHKSVKSESKDKERSSSKKSKKDKKDKDKQRDESKDKRMPKDERPGQSDSPASGNLQSAHLQQQSQVASTGKATPTSVGSNSSSSMVSNIGKQKEEATGKHSEKAAESKGDKSTSNGNATDTKKSHKHKKKKKK
Protein: WD_REPEATS_REGION domain-containing protein (Q17872)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear Pore complex Protein
- Nuclear pore complex protein 5
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 15
- Nsp1_C domain-containing protein
- Protein SEC13 homolog
- Nucleoporin SEH1
- Nucleoporin_N domain-containing protein
- Nuclear pore protein
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MAVVTITTDTEDSEIPQRTEVGSSTPLVDEIMQHADVKLSKILFTGETSSQIISLGKGRGRCISLWERDDGIDPFKVLATKNSEIDPNDACTMTDNRVCIGYADGSLAVFSTDKDDLALMSRIPSIHSGSASRKICRHGNSILSASSNGSLVAVDVETGMPRTIFTGQAGIRSVCTTFGTNVVMAGDANGQITMWDLRENNEHSNTLDPIKTLIPSKKALDAVTALCSHPAQSNLVCCGTDDGIVGLIDARNVRGANITSTYLVAKKAISQVMFHPKCGDNLLVSSNDGSLIRIDASGAPIAVGPRSTKDTIWLEGDLVNSLRLDPIRNESVHSISSFDIRSDTVVTASSIGLISLYQQLPFFPNSNFGRF
Protein: Nucleotide sugar transporter SLC35D1 (Solute carrier family 35 member D1) (UDP-galactose transporter-related protein 7) (UGTrel7) (UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter) (UDP-GlcA/UDP-GalNAc transporter) (A2AKQ0)
Organism: Mus musculus (Mouse)
Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (By similarity). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D-glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (By similarity). May couple UDP-GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (By similarity). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17952091}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Solute carrier family 35 member C2
- Solute carrier family 35 member E1
- GDP-fucose transporter 1
- Solute carrier family 35 member B1
- Nucleotide sugar transporter SLC35B4
Sequence:
MAEVHRRQHAPVKGEAPAKSSTHRDEEELGMAPAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKTLRVVKFPDFDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGALLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYVFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAMEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNISIAGSLVYSYITFTEEQLSKQSEASNKLDTKGKGAV
Protein: Somatostatin receptor type 1 (SS-1-R) (SS1-R) (SS1R) (SST1) (SRIF-2) (P30872)
Organism: Homo sapiens (Human)
Function: Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuropeptide Y receptor type 5
- Pro-neuropeptide Y
- Somatostatin receptor type 5
- Appetite-regulating hormone
- Pro-opiomelanocortin
Sequence:
MFPNGTASSPSSSPSPSPGSCGEGGGSRGPGAGAADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLSDNFKRSFQRILCLSWMDNAAEEPVDYYATALKSRAYSVEDFQPENLESGGVFRNGTCTSRITTL
Protein: Platelet glycoprotein Ib beta chain (GP-Ib beta) (GPIb-beta) (GPIbB) (CD antigen CD42c) (P56400)
Organism: Mus musculus (Mouse)
Function: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein Ib alpha chain
- Platelet glycoprotein IX
- von Willebrand factor
- Platelet glycoprotein V
- Tyrosine-protein kinase Lyn
- 14-3-3 protein zeta/delta
- Integrin alpha-IIb
- Filamin-A
- Prothrombin
- Guanine nucleotide-binding protein subunit beta-like protein 1.
Sequence:
MGSRPRGALSLLLLLLALLSRPASGCPAPCSCAGTLVDCGRRGLTWASLPAAFPPDTTELVLTGNNLTALPPGLLDALPALRAAHLGANPWRCDCRLLPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYVAEDELRAACAPGLLCWGALVAQLALLVLGLLHALLLALLLGRLRRLRARARARSIQEFSLTAPLVAESARGGAS
Protein: Receptor-type tyrosine-protein phosphatase-like ida-1 (Dense-core vesicle membrane protein ida-1) (Related to islet cell diabetic autoantigen protein) (G5EGJ5)
Organism: Caenorhabditis elegans
Function: Regulates dense-core vesicle (DCV) trafficking and/or secretion. Probably by controlling DCV trafficking, plays a role in the AVG neuron-mediated formation of the right axon tract of the ventral nerve cord. Involved in locomotion by regulating acetylcholine release. Probably by controlling the secretion of FLP neuropeptides, regulates the turning step of male mating behavior. Plays a role in preventing dauer formation.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15180830, ECO:0000305|PubMed:15044551}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell projection, axon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell projection, dendrite {ECO:0000269|PubMed:15180830}. Note=Localizes to dense-core vesicles along axons. {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}.
Interaction partners:
- Neuroendocrine convertase 2
- Carboxypeptidase E
- Neuropeptide-Like Protein
- Calcium-dependent secretion activator
Sequence:
MRFFHSIIVLLFSISTGSAFLLYGCNLSENLCDNDESCYPDGVFGQCYSSESGSPEPTVLDNLDDTQLELLKLELTRLAAKDKDWGDEETQCVLAYFKMSMFYQLQYDPDFCQVRKPANVWALIQLIDTGLTEDPTILDEDVNPENVTDEDMAQIIEQLKEPSLPTEEDIEEALNAQNEDVDDEILDQYVQAVVNNENPDFSELSDGQLNILIGRLVDLKKNVENEEAQLLTGDGEQEMAVPLDDLEERGEQAILKKDIEQVGEINQGLDNTEHKIVKGRKDQVVTRVDANRVYLKVHLKNEDQLMPLIEFLQNTIAIPNNLYFDDFQFENGQLSMRISRFEGAKPKADKRIDSVEGVASAVYKRRKDIARLSGADVRETGIGSGEDGSLPVESSERDWLLMPVLFVCAFTVTALGLVAAVQIARSRRHYKDNIQQIAEQLDGKNSFAYQDLCRQRADGGRASKSSSTSSWCEETAVPTIDISTGHVVLNFLQEYLSEPTKIEAQWNGIKDYRNEERTKTKAEKFASQNRTILPFDDNIVDIDGKTAENEDFYLNASFIYDDDPRQAVYIAAQTPASSQIAAFWQTIWQHGVCLVVNLSTPEECKQEKNYWPDTGSEVHGAFEIHLVSEHIWSDDYLVRSFYLKNLQNSQTRTITQFHYLSWQKESTPTSAKSILEFRRKVNKSYRGRSSAVLVHSWDGSGRTGVYCAVDVLCARLLRGIRQIDVVATVEHLRDQRDGMVATGDQFKLVYGCVAQEVNHLLKSIATK