wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein 176B (Protein LR8) (Q9R1Q6)
Organism: Mus musculus (Mouse)
Function: May play a role in the process of maturation of dendritic cells (By similarity). Required for the development of cerebellar granule cells.
Subcellular location: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Transmembrane protein 176A
Sequence:
MVQSTVTVNGVKVASTHPQSAHISIHIHQKSALEQLLGAVGSLKKFLSWPQARIHYGQLSLGVTQILLGLVSCALGVCLYFGPWTELCAFGCAFWSGSVAILAGVGTIVHEKRQGKLSGQVSCLLLLACIATAAAATVLGVNSLIRQTSVPYYVEIFSTCNPLQSSMDPGYGTVRYSDDSDWKTERCREYLNMMMNLFLAFCIMLTVVCILEIVVSVASLGLSLRSMYGRSSQALNEEESERKLLDGHPAPASPAKEKIPAIL
Protein: Transcription initiation factor TFIID subunit 6 (J3KR72)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDIRHSEFLPCLHCPPFVGPLPVSHVSFSSACPVPLPGSPSLHRGLHPSREEKRDSRMAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGATTADGKGKEKKAPPLLEGAPLRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRAEFGSLGPLLCSQVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSAPSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPSGPGSVQKYIVVSLPPTGEGKGGPTSHPSPVPPPASSPSPLSGSALCGGKQEAGDSPPPAPGTPKANGSQPNSGSPQPAP
Protein: Transposon Ty1-MR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q04214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVQTTQDPLDISASKTEECEKVSTQANSQQPTTPLSSAVPENHHHASPQAAQVPLPQNGPYPQQRMMNTQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFAPSQFLPPWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLATLHYNGSTPADAFEAEVTNILDRLNNNGIPINNKVACQFIMRGLSGEYKFLRYARHRCIHMTVADLFSDIHSMYEEQQESKRNKSTHRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTFNNSPGPDNDLIRGSTTEPIQLKNTHDLHLGQELTESTVNHTNHSDDKLPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQQSNDLNIESDHDFQSDIELHPEQLRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQSNTHESSHASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFENSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Nuclear RNA export factor 1 (E9PIN3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MADEGKSYSVSTSFFKSPTQFSSNFSLMLPSHREGSFLWIGSGVCMEMASVVKHDDERVNFPQRKKKGRGPFRWKYGEGNRRSGRGGSGIRSSRLEEDDGDVAMSDAQDGPRVRYNPYTTRPNRRGDTWHDRDRIHVTVRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYENTRAQFFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNNRLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEELWLDGNSLCDTFRDQSTYISAIRERFPKLLRLDGHELPPPIAFDVEAPTTLPPCKGSYFGTENLKSLVLHFLQQYYAIYDSGDRQGLLDAYHDGACCSLSIPFIPQNPARSSLAEYFKDSRNVKKLKDPTLRFRLLKHTRLNVVAFLNELPKTQHDVNSFVVDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASSEEIQRAFAMPAPTPSSSPV
Protein: Retinol-binding protein 1 (Cellular retinol-binding protein) (CRBP) (Cellular retinol-binding protein I) (CRBP-I) (P02694)
Organism: Bos taurus (Bovine)
Function: Cytoplasmic retinol-binding protein. Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q00915}. Lipid droplet {ECO:0000250|UniProtKB:Q00915}.
Interaction partners:
- Lecithin retinol acyltransferase
- Receptor for retinol uptake STRA6
- Retinol-binding protein 4
- Transthyretin
- Retinaldehyde-binding protein 1
- Retinol binding protein 1
- Retinol-binding protein 3
- Retinol dehydrogenase 5
- Short-chain dehydrogenase/reductase family 9C member 7
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MPVDFTGYWKMLANENFEEYLRALDVNVALRKIANLLKPDKEIVQEGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLECVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVN
Protein: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (EC 1.14.11.4) (Lysyl hydroxylase 1) (LH1) (Q63321)
Organism: Rattus norvegicus (Rat)
Function: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (By similarity).
Subcellular location: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Interaction partners:
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Glycosyltransferase 25 domain containing 1
- Collagen beta
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Calmodulin-lysine N-methyltransferase
- Prolyl 4-hydroxylase subunit alpha 2
- Collagen type V alpha 2 chain
- Prolyl 4-hydroxylase subunit alpha-1
- Collagen alpha-1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
Sequence:
MRSLLLLASLAWLLLAQAKDDAKLEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQSLGLGEDWSAAGGPSAAGGGQKVRLLKKALKKYADKEDLVILFVDSYDVVFASGPRELLKKFQQAKSRVVFSAEELIYPDRRLEAKYPTVPDGKRFLGSGGFIGYAPSLSKLVAEWEGQDNDSDQLFYTKIFLDPEKREQINISLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVVIHGNGPTKLQVNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPFLSLFFRRLLHLRYPQKQMRLFIHNQEQHHKLQVEQFLAEHGGEYQSVKLVGPEVRMANADARNMGADLCRQDQTCTYYFSVDADVALTEPNSLRLLIEQNKNVIAPLMTRHGRLWSNFWGALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRAELRHVDLFHYSKLDPDMSFCANVRQQEVFMFLTNRHTFGHLLSLDNYQTTHLHNDLWEVFSNPQDWKEKYIHENYTKALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHYGQWSLGDNKDNRIQGGYENVPTIDIHMNQITFEREWHKFLVEYIAPLTEKLYPGYYTKAQFDLAFVVRYKPDEQPSLMPHHDASTFTINIALNRVGEDYEGGGCRFLRYNCSVRAPRKGWALMHPGRLTHYHEGLPTTKGTRYIAVSFVDP
Protein: Protein GDS1 (P41913)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nuclear control of mitochondria.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
Sequence:
MALANSRPLQIPTLENEILHNSNSPVFQLNSMGFTTRADTISNPGTDLIGNQPGMALDDNNLAGSSFSSSQEIKATKPKKDFGAPKKDNPLLEISKLIPVTGERPKPENRDSPLDDDVLHAVFLILWEMDPNQQGMTVKQLCDLLLQKHPDMSNLSTKLSNLISAKLNAYVKKIEKGEKTLTYALSREWSNSSPRRMLYIYRGILSPDYKEHAQAVTMQLKQQLETSGDTSDFNSNGKKKRESSSNQLVNNDSYSSSMTDMKNMSSNSSFSKNLNVGNLAFSLSPEFNIPYSTSPVSLNLSPSMSNNQQQLLTPNSASKSKNNNKKRNYMDEDTNESMTEPKKTKTTKPGKQTKSQSLSVLSTPKKGSSASLSTFASSKNISPDSSLSHNASSNTYVTAAAAAPRLSKLLPKNGFKKNSRSSSELAAIHKVISTQTPIESSSESSQYNSSSSSPVNSAAASSAESLSDINSSQDNGRESNPSSQESRNEVTNWMKIVRNGFLTHDIESPESITLDDLENIFN
Protein: Adhesion G-protein coupled receptor G2 (G-protein coupled receptor 64) (Human epididymis-specific protein 6) (He6) (Q8IZP9)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Could be involved in a signal transduction pathway controlling epididymal function and male fertility. May regulate fluid exchange within epididymis.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
Sequence:
MVFSVRQCGHVGRTEEVLLTFKIFLVIICLHVVLVTSLEEDTDNSSLSPPPAKLSVVSFAPSSNGTPEVETTSLNDVTLSLLPSNETEKTKITIVKTFNASGVKPQRNICNLSSICNDSAFFRGEIMFQYDKESTVPQNQHITNGTLTGVLSLSELKRSELNKTLQTLSETYFIMCATAEAQSTLNCTFTIKLNNTMNACAVIAALERVKIRPMEHCCCSVRIPCPSSPEELEKLQCDLQDPIVCLADHPRGPPFSSSQSIPVVPRATVLSQVPKATSFAEPPDYSPVTHNVPSPIGEIQPLSPQPSAPIASSPAIDMPPQSETISSPMPQTHVSGTPPPVKASFSSPTVSAPANVNTTSAPPVQTDIVNTSSISDLENQVLQMEKALSLGSLEPNLAGEMINQVSRLLHSPPDMLAPLAQRLLKVVDDIGLQLNFSNTTISLTSPSLALAVIRVNASSFNTTTFVAQDPANLQVSLETQAPENSIGTITLPSSLMNNLPAHDMELASRVQFNFFETPALFQDPSLENLSLISYVISSSVANLTVRNLTRNVTVTLKHINPSQDELTVRCVFWDLGRNGGRGGWSDNGCSVKDRRLNETICTCSHLTSFGVLLDLSRTSVLPAQMMALTFITYIGCGLSSIFLSVTLVTYIAFEKIRRDYPSKILIQLCAALLLLNLVFLLDSWIALYKMQGLCISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTYIRKYILKFCIVGWGVPAVVVTIILTISPDNYGLGSYGKFPNGSPDDFCWINNNAVFYITVVGYFCVIFLLNVSMFIVVLVQLCRIKKKKQLGAQRKTSIQDLRSIAGLTFLLGITWGFAFFAWGPVNVTFMYLFAIFNTLQGFFIFIFYCVAKENVRKQWRRYLCCGKLRLAENSDWSKTATNGLKKQTVNQGVSSSSNSLQSSSNSTNSTTLLVNNDCSVHASGNGNASTERNGVSFSVQNGDVCLHDFTGKQHMFNEKEDSCNGKGRMALRRTSKRGSLHFIEQM
Protein: Cytochrome P450 710A1 (EC 1.14.19.41) (C-22 sterol desaturase) (O64697)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required to form the C-22 double bond in the sterol side chain. Possesses in vitro C-22 desaturase activity toward beta-sitosterol and produces stigmasterol. No activity with campesterol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- 24-methylenesterol C-methyltransferase 2
- Delta
- Methylsterol monooxygenase 2-1
- Cycloeucalenol cycloisomerase
- Delta
- Methylsterol monooxygenase 2-2
- Cycloartenol-C-24-methyltransferase
- 7-dehydrocholesterol reductase
- Serine carboxypeptidase-like 8
Sequence:
MVFSVSIFASLAPYLISAFLLFLLVEQLSYLFKKRNIPGPFFVPPIIGNAVALVRDPTSFWDKQSSTANISGLSANYLIGKFIVYIRDTELSHQIFSNVRPDAFHLIGHPFGKKLFGDHNLIYMFGEDHKSVRRQLAPNFTPKALSTYSALQQLVILRHLRQWEGSTSGGSRPVSLRQLVRELNLETSQTVFVGPYLDKEAKNRFRTDYNLFNLGSMALPIDLPGFAFGEARRAVKRLGETLGICAGKSKARMAAGEEPACLIDFWMQAIVAENPQPPHSGDEEIGGLLFDFLFAAQDASTSSLLWAVTLLDSEPEVLNRVREEVAKIWSPESNALITVDQLAEMKYTRSVAREVIRYRPPATMVPHVAAIDFPLTETYTIPKGTIVFPSVFDSSFQGFTEPDRFDPDRFSETRQEDQVFKRNFLAFGWGPHQCVGQRYALNHLVLFIAMFSSLLDFKRLRSDGCDEIVYCPTISPKDGCTVFLSRRVAKYPNFS
Protein: Nucleosome assembly protein (Q8I2W3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKRDRSENSVENTDPKHTKIENDDPLMPFMQDFEDIQKDIEQLDIKCAHEQMNIQKQYDEKKKPLFEKRDEIIQKIPGFWANTLRKHPALSDIVPEDIDILNHLVKLDLKDNMDNNGSYKITFIFGEKAKEFMEPLTLVKHVTFDNNQEKVVECTRIKWKEGKNPIAAVTHNRSDLDNEIPKWSIFEWFTTDELQDKPDVGELIRREIWHNPLSYYLGLEEFDEFDDDFDEEFDDDDDDDDDDDDDDDDDDKDDDLDGDDDGNNDDNDD
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit (EC 3.1.3.16) (Abnormal chemotaxis protein 6) (Calmodulin-dependent calcineurin subunit A) (Q0G819)
Organism: Caenorhabditis elegans
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. Dephosphorylates arrd-17. Dephosphorylates daf-16 at 'Ser-319' which regulates daf-16 nuclear translocation. Dephosphorylates calcium permeable cation channel pkd-2 at 'Ser-534'. Regulates male mating behavior including response to hermaphrodite contact and vulva location and localization of pkd-2 to neuronal cilium. Negatively regulates several sensory behaviors including thermotaxis in ADF neurons, osmosensation in ASH neurons, olfaction adaptation in AWC neurons and sensitivity to CO2 levels. Plays a role in modulating temperature-dependent calcium responses in AFD neurons and together with tax-6 inhibitor rcan-1 regulates thermotaxis in AFD neurons. Regulates expression of rcan-1. In response to changes in intracellular calcium levels may also regulate nuclear translocation of transcriptional regulators such as crtc-1. Plays a role in egg-laying, body-size, fertility, growth, movement and cuticle development. Negatively regulates lifespan. Promotes transcription activator crtc-1 nuclear localization, probably by dephosphorylating crtc-1 and thereby negatively regulates lifespan. Regulates expression of chemoreceptor srt-2 in AWC neurons probably downstream of Ser/Thr kinase kin-29. Negatively regulates nicotinic acetylcholine receptor (nAChR) sensitivity to nicotine. Plays a role in several endocytic processes including in coelomocyte endocytosis, intestine apical endocytosis and synaptic vesicle recycling. May negatively regulate excitatory GABA receptor exp-1 during enteric muscle contraction. May negatively regulate autophagy.
Subcellular location: Perikaryon {ECO:0000269|PubMed:12221132}. Cell projection, cilium {ECO:0000269|PubMed:16481400}. Cytoplasm {ECO:0000269|PubMed:12221132}.; SUBCELLULAR LOCATION: [Isoform a]: Perikaryon {ECO:0000269|PubMed:11879652}. Cell projection, dendrite {ECO:0000269|PubMed:11879652}. Cell projection, axon {ECO:0000269|PubMed:11879652}. Cell projection, cilium {ECO:0000269|PubMed:11879652}. Cytoplasm {ECO:0000269|PubMed:11879652}.
Interaction partners:
- Protein phosphatase 2B regulatory subunit cnb-1
- Calmodulin
- Calcipressin-like protein
- Calmodulin-like protein
- Calmodulin-like protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Uncharacterized calcium-binding protein B0563.7
Sequence:
MASTSAGQNSAAKPDTTNTTTTASNNNRERERDLKQFTERFVKTVQFPVSERLTVDQVYDRRTGKPRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAILKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVHILNICSDDELMAECDDTFEGGVGSARKEVIRHKIRAIGKMARAFSVLRHESESVLQLKGLNAGGKLPQGALSEGRTGLNAAYRIEQSVAAESGCDSGHLIQSFEEARRLDKINERMPPTMATPPAQSPSQSPIPSRQTTPQPPQNGPSNS
Protein: Large subunit GTPase 1 (EC 3.6.1.-) (P53145)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase required for the nuclear export of the 60S ribosomal subunit. Acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12773575, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Probable metalloprotease ARX1
- 60S ribosomal export protein NMD3
- Cytoplasmic 60S subunit biogenesis factor REI1
- Eukaryotic translation initiation factor 6
- Tyrosine-protein phosphatase YVH1
- Large ribosomal subunit protein uL18
- Nucleolar GTP-binding protein 1
- Large ribosomal subunit protein uL16
- Ribosome biogenesis protein RLP24
- Large ribosomal subunit protein eL27A
Sequence:
MPPKEAPKKWKAPKGPKPTHRKNKNKLELGRAIKYARQKENAIEYLPDGEMRFTTDKHEANWVKLRSVTQESALDEFLSTAALADKDFTADRHSNVKIIRMDSGNDSATSQGFSMTNEQRGNLNAKQRALAKDLIVPRRPEWNEGMSKFQLDRQEKEAFLEWRRKLAHLQESNEDLLLTPFERNIEVWKQLWRVVERSDLVVQIVDARNPLLFRSVDLERYVKESDDRKANLLLVNKADLLTKKQRIAWAKYFISKNISFTFYSALRANQLLEKQKEMGEDYREQDFEEADKEGFDADEKVMEKVKILSIDQLEELFLSKAPNEPLLPPLPGQPPLINIGLVGYPNVGKSSTINSLVGAKKVSVSSTPGKTKHFQTIKLSDSVMLCDCPGLVFPNFAYNKGELVCNGVLPIDQLRDYIGPAGLVAERIPKYYIEAIYGIHIQTKSRDEGGNGDIPTAQELLVAYARARGYMTQGYGSADEPRASRYILKDYVNGKLLYVNPPPHLEDDTPYTREECEEFNKDLYVFDRLPDTRKEQVQNAAKAKGIDIVDLARDLNQLTFSAHTGGDTQKEAKSVTHGGKQAALYNAAEDLDRDFFKMNNVEGRLSTPFHKVQNSSAGKRHNKKNKSKNAKSKVFSIENN
Protein: Natural killer cells antigen CD94 (Killer cell lectin-like receptor subfamily D member 1) (CD antigen CD94) (O54707)
Organism: Mus musculus (Mouse)
Function: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13241}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Killer cell lectin-like receptor subfamily C, member 1
- H-2 class I histocompatibility antigen, D-37 alpha chain
- TYRO protein tyrosine kinase-binding protein
- Killer cell lectin-like receptor subfamily C, member 2
- Killer cell lectin-like receptor subfamily C, member 3
- KIR-like receptor 2 KIRL2.1
- Histocompatibility 2, Q region locus 1
- Heat shock 70 kDa protein 1B
- Tyrosine-protein phosphatase non-receptor type 11
- Tyrosine-protein phosphatase non-receptor type 6
Sequence:
MAVSRITRWRLMSVIFGIKCLFLMVTLGVLLINSFTIQNIQSTPSPTTTVEFQEVSECCVCLDKWVGHQCNCYFISKEEKSWKRSRDFCASQNSSLLQPQSRNELSFMNFSQTFFWIGMHYSEKRNAWLWEDGTVPSKDLFPEFSVIRPEHCIVYSPSKSVSAESCENKNRYICKKLPI
Protein: Protein Skeletor, isoforms D/E (Q9GPJ1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Provides structural support to stabilize and organize the microtubule spindle during mitosis (within embryonic somatic cells) and meiosis (within spermatocytes). The role in mitosis regulation depends on the Ran pathway.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Nucleus, nucleolus. Chromosome. Note=Part of a macromolecular complex forming the spindle matrix. During mitosis, associated with chromatin at interphase, redistributes to the spindle structure at prophase (preceding the formation of the microtubule spindle) through to anaphase. Extends from one end of the spindle to the other during metaphase and anaphase, coaligns with the microtubule spindle.
Interaction partners:
- Nucleoprotein TPR
Sequence:
MLAMKDKPWLLLFGLLAALSCLASFGDAAYPYYGTKIGALTRLHHGVSGDVYAVDSRTIFIKKFNYDGEAPAAYFYVGNTARPSNEGAARLRDERGGTASLTRRYRNKDVTLSLPEGKTLRDIKWFSVWCDEFAVNFGDVSIPPNLDFPRPQKISALRGVHGVSSDNIVIVDAQTLLVPNFSYDGEAPDAKFWVGRGQRPTSDGLRIPDENGKENPLRRYERKTIVLTLPEDLTIFDIGHFGVWCEAFTVDFGHVRLPEGLNVPPSLKMLGISPQSKLNCEVLYDDLAFEVRWAVAGESIVVQLVAKLEPNHYMSFGISPNKNISQMIGADAVVAWVDPQTGNGFATDYFLEGKAQCSGGRGACPDTKISEKTNSIRLLNAAMVNGYSIVTYQRSLAATDRLDLPISITGAESVVWAIGPLNDYQEVSFHTFYNKHLHQIEFGRQPKWNCPLPEGARGNSNSSEQEDSAPAAQSSTGGAGYPPAGRPNVEPDEEFYENRAEALHRQPPQRRQETAIITQRRPVPTPKPVNSNGAWDIPAIQCHEPEDGVFYAQMGPTGGKHGYPAITGHVGWGISWYINGLLIPEIHVVRGKTYTFVVEGGNNPDIPAKYHPFYISDDPVGGYEHKREEEKKAVRIYAGVHRSRSGQVTPTGVGRLCNWTPDVEGPPADDYQSFGAYQRTLTLKCDAGEPGVITWKPDRNTPDTVYYHCFTHRYLGWKIHVHDSCDSEAGGLKGAASERHEIRLPAKATVAEPAPVHEDYAGEASVRHETKVSANDNFLLKHQTDLIKNHNMNGTPPKLSFEITKSSEITKLISDGIRAAEALEESLLRNPNLNPNHPNQNPIPNPHQKPNVTPTEISSRPEILLGETHAHTLNASPSASAYPSPSATLPSANLKLPILAAGPHLIHHPPHLHRLHHQPQHAPHPHVHLHHHNLTANLPALAQKTIGLSEFLRPPQNAPLFHPVKLPGRRPFPAPIKKVPASRPILPQQHPHLHPHPQQHPVLLQQQPSLIVSHYRKPIPGLLKPFVKEKPFPLQPLAASVLLLGQPTELGGLNNKGERLKIKGKPKIPVPYVDLEPQGSLQNTAIFNQPGGKGKGDQKPKASSVSISTTPIPLVKRPTVKEPSQEEIASMRPAVNQGFKPDTVIVESGFKPIVRTDGTGVQLPKEIIDQVAHRREDPGTEIDEVMETDTLFLAAQQGGSETQSFEPMFIPSPLDSTNATKVLRVNVKEVSPTASALRLPSAALEHALPSASELIKPTLDELFAEDLNEEELEMEPMPVADDVESLEETTKKDAVTTTINIPRNTTKKPDPDLLEDLFGPDEEELYADELELDMDDRVAAAAERIDTYYLPPDNRKIPDTRVPSGALYTFDGKSVVDSSLVLPPKLDAPDNANVHQRHAQYGLTPLEQLVRTTPQFGVYRGELPQEFRGTEPQPVSEYSHPAPFSRTTPVFSSSSGSTIYPYSSSTGASTSTVSSSASSPLSSSSLRPISTKLQLLKPEGRRA
Protein: Actin depolymerizing factor (Q4JHK7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MANAASGMAVHDDCKLKFLELKAKRTYRFIVFKIEEKQKQVVVEKVGEPTDSYEAFTASLPADECRYAVYDFDFVTDENCQKSRIFFIAWSPDTSKVRSKMIYASSKDRFKRELDGIQVELQATDPSEMDLDVIRSRAN
Protein: Protein lin-28 homolog B (Lin-28B) (Q6ZN17)
Organism: Homo sapiens (Human)
Function: Suppressor of microRNA (miRNA) biogenesis, including that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7 transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and sequester them in the nucleolus, away from the microprocessor complex, hence preventing their processing into mature miRNA. Does not act on pri-miR21. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state of embryonic stem cells by preventing let-7-mediated differentiation. When overexpressed, recruits ZCCHC11/TUT4 uridylyltransferase to pre-let-7 transcripts, leading to their terminal uridylation and degradation. This activity might not be relevant in vivo, as LIN28B-mediated inhibition of let-7 miRNA maturation appears to be ZCCHC11-independent. Interaction with target pre-miRNAs occurs via an 5'-GGAG-3' motif in the pre-miRNA terminal loop. Mediates MYC-induced let-7 repression (By similarity). When overexpressed, isoform 1 stimulates growth of the breast adenocarcinoma cell line MCF-7. Isoform 2 has no effect on cell growth.
Subcellular location: Nucleus. Nucleus, nucleolus {ECO:0000269|PubMed:22118463}. Cytoplasm {ECO:0000269|PubMed:16971064}. Note=Predominantly nucleolar (PubMed:22118463). In Huh7 cells, predominantly cytoplasmic, with only a subset of cells exhibiting strong nuclear staining; however, the specificity of the polyclonal antibody used in these experiments has not been not documented (PubMed:16971064). {ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:22118463}.
Interaction partners:
- Terminal uridylyltransferase 4
- High mobility group AT-hook 2
- Insulin-like growth factor 2 mRNA-binding protein 1
- Ribonuclease 3
- Endoribonuclease Dicer
- E3 ubiquitin-protein ligase TRIM71
- Developmental pluripotency-associated protein 3
- Myc proto-oncogene protein
- Transcription factor SOX-2
- Speckle targeted PIP5K1A-regulated poly
Sequence:
MAEGGASKGGGEEPGKLPEPAEEESQVLRGTGHCKWFNVRMGFGFISMINREGSPLDIPVDVFVHQSKLFMEGFRSLKEGEPVEFTFKKSSKGLESIRVTGPGGSPCLGSERRPKGKTLQKRKPKGDRCYNCGGLDHHAKECSLPPQPKKCHYCQSIMHMVANCPHKNVAQPPASSQGRQEAESQPCTSTLPREVGGGHGCTSPPFPQEARAEISERSGRSPQEASSTKSSIAPEEQSKKGPSVQKRKKT
Protein: chitin synthase (EC 2.4.1.16) (Q9GTZ7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
HELDPDYYEFETHIFFDDAFEISDHSDDDIQCNRFVKLLIATMDEAASEIHQTTIRLRPPKKYPTPYGGRLVWTLPGKTKFITHLKDKDRIRHRKRWSQVMYMYYLLGHRLMELPISVDRKDAIAENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKALMDDNVMKKYTTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFRIDNWTSFHYNIVPILAFMFICFTCKSNIQLFVAQVLSTAYALIMMAVIVGTALQLGEDGIGSPSAIFLISMVGSFFIAACLHPQEFWCITCGLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVAKKTKKELEAEKKAAEEAKKRVKQKSMLSFLQSGIGDNGDEEGSVEFSLAGLFRCIFCTHGKTSDEKQQLTSIAESLDTIKHRMDTIESAVDPHGHHASRHGRRRTTSSGSKDHHLLTSVAEKSGDESDESDSDTSAEPKQERDFLTNPYWIEDPDVRKGEVDFLSSTEIQFWKDLIDQYLYPIDNDPVEQARIAKDLKELRDSSVFAFFMINALFVLIVFLLQLNKDNIHVKWPFGVRTNITYDESTQEVHISKEYLQLEPIGLVFVFFFALILIIQFTAMLFHRFGTISHILASTELNFCKKKSEDLTQDQLIDKHAVEIVKNLQRLQGIDGDYDNDSGSGPDRIARRKTIQNLEKARQPRRQIGTLDVAFKKRFLKLTADAENNPATPILTRRLTMRAETIRALEVRKNSVMAERRKSAMQTLGAKNEYGITTGAPINNNGALPNQRSGRVSNAGISIKDVFNVNGGGAEQIYGSNGGGTINQGYEHVIDEDGDGNSLRLTTRNPHPHPHHQVSWGQNTNGGGGNGTGRL