wanglab/gogpt-training-data huggingface dataset:
Protein: Protein KASH5 (Coiled-coil domain-containing protein 155) (KASH domain-containing protein 5) (Q8N6L0)
Organism: Homo sapiens (Human)
Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homolog pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation.
Subcellular location: Nucleus outer membrane {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q80VJ8}. Nucleus envelope {ECO:0000269|PubMed:35587281}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q80VJ8}.
Interaction partners:
- SUN domain-containing protein 1
- SUN domain-containing protein 2
- Nesprin-4
- Dickkopf-like protein 1
- Telomere repeats-binding bouquet formation protein 1
- Membrane anchored junction protein
- Nesprin-3
- Inositol 1,4,5-triphosphate receptor associated 2
- Nesprin-1
- Telomere repeats-binding bouquet formation protein 2
Sequence:
MDLPEGPVGGPTAEMYLRERPEEARLGMPVSLEEQILNSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPKATVDLDTFLVVMRDWIAACQLHGGLELEEETAFQGALTSRQLPSGCPEAEEPANLESFGGEDPRPELQATADLLSSLEDLELSNRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSNPLCGVWQWEEVIHETSEETEFPSEAPAGGQRNFQGEPAHPEEGRKEPSMWLTRREEEEDAESQVTADLPVPLGAPRPGDIPENPPERPARRELQQALVPVMKKLVPVRRRAWGQLCLPPQRLRVTRHPLIPAPVLGLLLLLLLSVLLLGPSPPPTWPHLQLCYLQPPPV
Protein: Ribosomal RNA large subunit methyltransferase M (EC 2.1.1.186) (23S rRNA (cytidine2498-2'-O)-methyltransferase) (23S rRNA 2'-O-ribose methyltransferase RlmM) (P0ADR6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. Modifies C2498 in naked 23S rRNA, but not in assembled 50S subunits or ribosomes.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UPF0382 inner membrane protein YgdD
- Glycine cleavage system transcriptional activator
- Sulfur acceptor protein CsdE
- Ribosomal RNA large subunit methyltransferase K/L
- Ribosomal RNA large subunit methyltransferase E
- 23S rRNA
- Dual-specificity RNA methyltransferase RlmN
- tRNA1
Sequence:
MNKVVLLCRPGFEKECAAEITDKAGQREIFGFARVKENAGYVIYECYQPDDGDKLIRELPFSSLIFARQWFVVGELLQHLPPEDRITPIVGMLQGVVEKGGELRVEVADTNESKELLKFCRKFTVPLRAALRDAGVLANYETPKRPVVHVFFIAPGCCYTGYSYSNNNSPFYMGIPRLKFPADAPSRSTLKLEEAFHVFIPADEWDERLANGMWAVDLGACPGGWTYQLVKRNMWVYSVDNGPMAQSLMDTGQVTWLREDGFKFRPTRSNISWMVCDMVEKPAKVAALMAQWLVNGWCRETIFNLKLPMKKRYEEVSHNLAYIQAQLDEHGINAQIQARQLYHDREEVTVHVRRIWAAVGGRRDER
Protein: HTH-type transcriptional regulator SinR (P06533)
Organism: Bacillus subtilis (strain 168)
Function: Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.
Interaction partners:
- Protein SinI
- Signal peptidase I W
- Stage 0 sporulation protein A
- TasA anchoring/assembly protein
- Uncharacterized protein YveK
- Transition state regulatory protein AbrB
- Transcriptional regulator SlrA
- Biofilm-surface layer protein A
- Uncharacterized protein YmcA
- Putative glycosyltransferase EpsE
Sequence:
MIGQRIKQYRKEKGYSLSELAEKAGVAKSYLSSIERNLQTNPSIQFLEKVSAVLDVSVHTLLDEKHETEYDGQLDSEWEKLVRDAMTSGVSKKQFREFLDYQKWRKSQKEE
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (Neoplasm-related protein C140) (P21533)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02878}. Cytoplasm {ECO:0000250|UniProtKB:Q02878}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q02878, ECO:0000250|UniProtKB:Q2YGT9}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL19
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL29
Sequence:
MAGEKAEKPDKKEQKPAAKKAGGDATAPRALPAGAVKKSSSKAKKLRKSKPHCSRNPVLVRGIGRYSRSAMYSRKALYKRKYSAAKTKVEKKKKKEKVLATVTKTVGGDKNGGTRVVKLRKMPRYYPTEDVPRKLLSHGKKPFSQHVRRLRSSITPGTVLIILTGRHRGKRVVFLKQLGSGLLLVTGPLALNRVPLRRTHQKFVIATSTKVDISKVKIPKHLTDAYFKKKPLRKPRHQEGEIFDTEKEKYEITEQRKADQKAVDSQILPKIKAVPQLQGYLRSQFSLTNGMYPHKLVF
Protein: Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH) (O08795)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Neutral alpha-glucosidase AB
- Translocation protein SEC63 homolog
- Polycystin-2
- Galectin-3
Sequence:
MLLLLLLLLPLCWAVEVKRPRGVSLSNHHFYEESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEETEPKEEKPPVLPPTEEEEEEEEEPEEEEEEEEEEEEAPPPLQPPQPPSPTEDEKMPPYDEETQAIIDAAQEARSKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEAPSDGDHDEL
Protein: Thyrotropin-releasing hormone receptor (TRH-R) (Thyroliberin receptor) (P34981)
Organism: Homo sapiens (Human)
Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26735259}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-thyrotropin-releasing hormone
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Thyrotropin subunit beta
- Beta-arrestin-2
- Beta-arrestin-1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Thyrotropin receptor
- Appetite-regulating hormone
Sequence:
MENETVSELNQTQLQPRAVVALEYQVVTILLVLIICGLGIVGNIMVVLVVMRTKHMRTPTNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSLYCMLWFFLLDLNISTYKDAIVISCGYKISRNYYSPIYLMDFGVFYVVPMILATVLYGFIARILFLNPIPSDPKENSKTWKNDSTHQNTNLNVNTSNRCFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIYNLMSQKFRAAFRKLCNCKQKPTEKPANYSVALNYSVIKESDHFSTELDDITVTDTYLSATKVSFDDTCLASEVSFSQS
Protein: Beta-hexosaminidase (EC 3.2.1.52) (Beta-N-acetylglucosaminidase) (N-acetyl-beta-D-glucosaminidase NagA) (Q9HGI3)
Organism: Emericella nidulans (Aspergillus nidulans)
Function: Part of the binary chitinolytic system. Involved in hydrolyzation of chitobiose and higher chito-oligomers (produced from cell wall chitin by endochitinases), thus contributing to the formation of germ tubes, fruit-bodies and septa during hyphenation (Probable). Hydrolyzes synthetic substrates p-nitrophenyl-beta-N-acetyl-glucosamine (pNP-beta-GlcNAc), p-nitrophenyl-beta-N-acetyl-galactosamine (pNP-beta-GalNAc) and 5-bromo-4-chloro-3-indoyl-beta-D-N-glucosaminide (X-GlcNAc).
Subcellular location: Secreted {ECO:0000269|PubMed:12450128}.
Interaction partners:
Sequence:
MAYFRLYAVLLAVASSVAAVKVNPLPAPRHISWGHSGPKPLSDVSLRTERDTDDSILTNAWNRAWETIVSLEWVPAGIEAPIPEFDEFPTSTPSASAAATRSKRANVPIQFVDVDVEDWDADLQHGVDESYTLDAKAGSDAIDITAKTVWGALHAFTTLQQLVISDGNGGLILEQPVHIKDAPLYPYRGLMVDTGRNFISVRKLHEQLDGMALSKLNVLHWHLDDTQSWPVHIDAYPEMTKDAYSARETYSHDDLRNVVAYARARGIRVIPEIDMPAHSASGWQQVDPDIVACANSWWSNDNWPLHTAVQPNPGQLDIINPKTYEVVQDVYEELSSIFTDDWFHVGGDEIQPNCYNFSTYVTEWFQEDPSRTYNDLMQHWVDKAVPIFRSVSDSRRLVMWEDVVLNTEHADDVPTDIVMQSWNNGLENINKLTERGYDVIVSSADFMYLDCGRGGYVTNDDRYNEQTNPDPDTPSFNYGGIGGSWCGPYKTWQRIYNYDFTLNLTNAQAKHVIGATAPLWSEQVDDVNISNLFWPRAAALAELVWSGNRDAKGNKRTTLFTQRILNFREYLLANGVMAATVVPKYCLQHPHACDLNYDQTVLH
Protein: Ethylene-responsive transcription factor SHINE 3 (Q3E958)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes cuticle formation by inducing the expression of enzymes involved in wax biosynthesis. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At5g15190
- Homeobox-leucine zipper protein HDG1
- RING-type E3 ubiquitin transferase
- Exosome complex component RRP45B
- GDSL esterase/lipase At1g58430
- Probable lysophospholipase BODYGUARD 1
- Very-long-chain aldehyde decarbonylase CER1
- Protein ECERIFERUM 2
- Alkane hydroxylase MAH1
- 3-ketoacyl-CoA synthase 6
Sequence:
MVHSKKFRGVRQRQWGSWVSEIRHPLLKRRVWLGTFDTAETAARAYDQAAVLMNGQSAKTNFPVIKSNGSNSLEINSALRSPKSLSELLNAKLRKNCKDQTPYLTCLRLDNDSSHIGVWQKRAGSKTSPNWVKLVELGDKVNARPGGDIETNKMKVRNEDVQEDDQMAMQMIEELLNWTCPGSGSIAQV
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Bypass of SEC30 protein 1) (P43571)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. Required for the transport of misfolded protein to the Golgi, although dipensable for the transport of many normal proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- GPI-anchor transamidase
- GPI transamidase component GPI16
- GPI transamidase component GAA1
- GPI transamidase component GPI17
- GPI transamidase component GAB1
- Calnexin homolog
- Protein transport protein SEC13
Sequence:
MGIRRLVSVITRPIINKVNSSGQYSRVLATREDQDKASPKYMNNDKIAKKPYTYRLFSILGILSICSLLLISLLKPFNGADAPQCESIYMFPSYARIDGFDERYTPLAHKYHLYLYREQSVDREPLNGDELQLDGIPVLFIPGNAGSFRQCRSIASACSNIYFDSNTRATLRNENVRNLDFFTADFNEDFTAFHGETMLDQAEYLNDAIKYILSLYERTPDYPHPKPQSVIIVGHSMGGIVSRVMLTLKNHVPGSISTILTLSSPHAASPVTFDGDILKLYKNTNEYWRKQLSQNDSFFSKNISLVSITGGILDTTLPADYASVEDLVSLENGFTSFTTTIPDVWTPIDHLAIVWCKQLREVLARLLLESIDASKPEKVKPLNQRLQIARKLLLSGFEDYSWMNSKLNYPQENLQEFSDNFFSDYATLEMNDVLDFEMFNLEKWHNNYTKINIPSNISSTEHLHFTLLTSLDMPMIYFCTESRVNLSCITAVDSILTVPRSSKDTQFAADSSFGEAKNPFKAVSVGKNILQKYDYLMISKPTYGEFSEQEGMEDNQGFLLALLRNVSNVQIVNTTPSQILLFGEQLHLDGKDIEQVISFSNLWDSLLSYKLETKIEASNEGIASEETLFQPFIRQWVYEPFESKWHLNIINKSLDINMHNVAPFIPLNESEPRSLQLSFFIPPGMSLEAKMTINWSLTLKMLFIRYRLALASFPVAFIALVLSYQFYWYNKTSEFPSFDSTLGYILRKHGILMFFTLFLASPVVNNKLVQRILYLLDPVGLNYPFLLSERNMHANFYYLGIRDWFMSTIGILFGVMTVGLLALVSKIFGSLEILVIFLQRKLSKKNTEDKEAFDTIEHKAYGKGRLMASVLLLLLVFFHIPYQMAFVISLVIQIATCIRVALLKLSNNEQKLNLLNYNMTLLLLLLFVSAINIPIIIVFLHNVAIKWETSFRSHHNILAVAPIIFLVGNNSIFKMPNSVPLDTWDGKVTIILFVYLTVFSFIYGIRNLYWIHHLVNIICAWLLFFETIH
Protein: U2 small nuclear ribonucleoprotein auxiliary factor-like protein (F4KC77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASFEKFEPIFGEVVPERSDPGSGLLRRCLFHVYASDSYNLTVHVTDFISGVWTTILSVSQLDDMRDTVGIGGSWSEFVDYTVASLKSDNVKLLLGETSVSNGVKTARLVSQKAKGMPRINVPLTKMVESSASEAMANLSLELFRAFKSKQHLQGEVSFSAAATDEKDKRDATYNQLERYSRKLDVMAPSTNNRQDSPANQSAREANTKNPVKRVPAHRRTRKRGALLQDSEEEDG
Protein: GCN5-related N-acetyltransferase 2, chloroplastic (EC 2.3.1.255) (Acetyltransferase NSI) (AtNSI) (EC 2.3.1.48) (Nuclear shuttle protein-interacting protein) (Serotonin N-acetyl transferase 1) (AtSNAT) (AtSNAT1) (EC 2.3.1.87) (Q7X9V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acetyltransferase that acetylates in vitro histones H2A and H3. Does not act as a transcriptional activator but might be involved in the sink-source transition. In case of begomoviruses infection, acetylates the capsid protein (CP), but not the nuclear shuttle protein (NSP). Required for begomovirus infection and systemic spread.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25250906, ECO:0000269|PubMed:29967049, ECO:0000269|PubMed:32354877, ECO:0000269|PubMed:32633465}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit B2
- Phenylacetaldehyde synthase
- V-type proton ATPase catalytic subunit A
Sequence:
MLLIPISSSSSSSISPPPNSYPSNHHSLFFSNLTFPIQHGSRKLKTLRLRANFWESIRSGFVKNNNSTQLVEPPSIVNDEEEETEPLLPVEFTLVERNLEDGLVEEIIFSSGGEIDVYDLQGLCDKVGWPRRPLVKLAAALKNSYMVATLHSVMKSSSDSDSSEGGDGEKQQEKKLIGMARATSDHAFNATIWDVLVDPEYQGQGLGKALVEKLVRALLQRDIGNISLFADSQVVDFYQNLGFEADPEGIKGMFWYPK
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (Q5EBY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEADRSFGLAWVLLLLLGITAATGREVCLGTDMKLALPSSLENHYEMLRLLYTGCQVVHGNLEITHLQGNPDLSFLQEIVEVQGYVLIAHVSVRSLPLDNLRIIRGSQLYKSNYALAVHNNSNSSQAGLGLRELRLRSLTEILLGGVYIWGNPQLCFPRNINWEDTVSKVQNKPLHLQDIPKNCPRCSSACKSGGCWGEKDQDCQTLTSVNCSSGCSRCKGPKPSDCCHVQCAAGCTGPKDSDCLACRHFNDSGTCKDSCPPPTIYDPITFQSKPNKDKKFSFGATCVKQCPHNYLAMEVACTMVCPKANKEVISVEPDGQETQKCEKCEGECPKVCYGLGMGNLQGVSVVNSTNIGMFTGCEKIYGSLAFLSDSFKGNADTNSSGLQPSDLEKLKTIEEITGYLYIDAWSENLLDLSVFENLKVIRGQMLYKGVFSLGVQSLQIESLGLRSLRSVSGGLVLIHNNSRLCYTSSLPWTSLLHPTQGPNLISNNNKDQQTCVSEGKICDPLCGDSGCWGPGPSQCVSCLNYKRGTECVELCNVLHGSVREFEDGFNCVPCHPECRPINGTASCTGPGPDQCTDCMHFQDGDVCVERCPSGVKEEQHTVWKYSNATGHCLPCETNCTVSCPLDDRGCPIQQKTGPGTTVAITVGGVLLFIILLALLVFYLRRQKHQKKKETIRRRLQEHELVEPLTPSGAMPNQAQMRILKETELKKLRVLGSGAFGTVFKGIWAPDGENVRIPVAIKVLRENTSPKANKEILDEAYVMAGVASPYVCRLLGICLTSTVQLVTQLMPYGCLLDYVRENKDRIGSQYLLSWCVQIAKGMSYLEEVRLVHRDLAARNVLVKNPNHVKITDFGLARLLDIDEKEYHADGGKVPIKWMALESILHRKFTHQSDVWSYGVTVWELMTFGMKPYESFQARDIPELLEAGERLSQPCNCTKEVYMIMVKCWQIDPDNRPRFKDLVDEFTTMARDPSRYVVIQNEDQMSLSSPVDSEFFRILMAEEGGNVKEFLDAEEYLVPQPGSIFNTHGEMRANGPSRHHSHRSTDQMVEVDGLPNGRELYSSVSMIEQSQYPTLPVGATANGMWPGTQYPPLARSISHRSAGGQSDSVFLDGYVEDSCPPSSPCRYSKDPTMPNGIDGDLETDGNMVFLSHTLPRGTHTQPEYVNQDMASERPSTLPRKASERRFILNGLSTGNSVENPEYLVPIGSITPTSPAFDNPYYHDIAAKAQAVARVAINGGTNHRQPNGFMTPTAENPEYLGLADTWSGHKEYT
Protein: Allatostatin C receptor 2, isoform F (A0A0S0WMT8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Allatostatin C, isoform A
- Muscarinic acetylcholine Receptor, B-type, isoform A
Sequence:
MEGGWWRGGGGGGRLGGKAIMEGHSTPNGAAASHRNNSTRTNIATNGCAHSGILLFVLTAMTLTSLITPTEQLAVAPNGTTLHQLESVESESYPSINGTQNETMVTSVRPHLDHRNRPTQQNGSHYLEYDDDGPDCSYSYNFILKLITMILYALVCIIGLFGNTLVIYVVMRFSKMQTVTNIYILNLAIADECFLIGIPFLLYTMQVGNWPFGNYMCKAYMVSTSITSFTSSIFLLIMSADRYIAVCHPISSPRYRTPFVSKLVSAFAWMTSVLLMLPVILFASTVQSSNGNVSCNIEWPDTQNSHTDSTFILYSLVLGFATPLTFILVFYCLVIRKLHTVGPKHKSKEKKRSHRKVTKLVLTVISAYIFCWLPHWISQVALISSAPQRCASRLELAVFLACGCLSYSNSAMNPILYAFLSDNFKKSFMKACTCAARKDVNAQLQLENSFFPKFGKGRQSERLLGGNGKGGAQRGALTKKKCLATRNNNAPMATTTTTTTTTTGTDAVTCLQPPVHQVPAEIQVGNPATVLVVNAETNNCKPPVLHTDLXDRAPSMPLETVVFIARRXDHQVELDLDTAIDCQAIARQPECLL
Protein: N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.60) (Acylsphingosine deacylase NAAA) (EC 3.5.1.23) (N-acylsphingosine amidohydrolase-like) (ASAH-like protein) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta] (Q9D7V9)
Organism: Mus musculus (Mouse)
Function: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Monoglyceride lipase
- G-protein coupled receptor 55
- 
Sequence:
MGTLATRAACHGAHLALALLLLLSLSGPWLSAVVPGTPPLFNVSLDAAPEQRWLPMLRHYDPDFLRTAVAQVIGDRVPQWVLGMVGEIVSKVESFLPQPFTDEIRSICDSLNLSLADGILVNLAYEASAFCTSIVAQDSQGHIYHGRNLDYPFGKILRKLTANVQFIKNGQIAFTGTTFVGYVGLWTGQSPHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLSESESFEAAVYTLAKTPLIADVYYIVGGTSPKEGVVITRDRGGPADIWPLDPLNGEWFRVETNYDHWKPAPKVDDRRTPAIKALNATGQAHLNLETLFQVLSLFPVYNNYTIYTTVMSAAEPDKYLTMIRNPS
Protein: Origin recognition complex subunit 2 (Origin recognition complex 71 kDa subunit) (P32833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
Subcellular location: Nucleus.
Interaction partners:
- DNA replication licensing factor MCM2
- Nucleolar complex-associated protein 3
- Origin recognition complex subunit 6
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM3
- Minichromosome maintenance protein 5
- Origin recognition complex subunit 1
- Origin recognition complex subunit 5
- Cell division cycle protein CDT1
- Pre-rRNA-processing protein IPI3
Sequence:
MLNGEDFVEHNDILSSPAKSRNVTPKRVDPHGERQLRRIHSSKKNLLERISLVGNERKNTSPDPALKPKTPSKAPRKRGRPRKIQEELTDRIKKDEKDTISSKKKRKLDKDTSGNVNEESKTSNNKQVMEKTGIKEKREREKIQVATTTYEDNVTPQTDDNFVSNSPEPPEPATPSKKSLTTNHDFTSPLKQIIMNNLKEYKDSTSPGKLTLSRNFTPTPVPKNKKLYQTSETKSASSFLDTFEGYFDQRKIVRTNAKSRHTMSMAPDVTREEFSLVSNFFNENFQKRPRQKLFEIQKKMFPQYWFELTQGFSLLFYGVGSKRNFLEEFAIDYLSPKIAYSQLAYENELQQNKPVNSIPCLILNGYNPSCNYRDVFKEITDLLVPAELTRSETKYWGNHVILQIQKMIDFYKNQPLDIKLILVVHNLDGPSIRKNTFQTMLSFLSVIRQIAIVASTDHIYAPLLWDNMKAQNYNFVFHDISNFEPSTVESTFQDVMKMGKSDTSSGAEGAKYVLQSLTVNSKKMYKLLIETQMQNMGNLSANTGPKRGTQRTGVELKLFNHLCAADFIASNEIALRSMLREFIEHKMANITKNNSGMEIIWVPYTYAELEKLLKTVLNTL
Protein: Collagen alpha-1(XIV) chain (Undulin) (Q05707)
Organism: Homo sapiens (Human)
Function: Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P32018}.
Interaction partners:
- Decorin
- Collagen alpha-1
- Matrix metalloproteinase-9
- Collagenase 3
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Mimecan
Sequence:
MKIFQRKMRYWLLPPFLAIVYFCTIVQGQVAPPTRLRYNVISHDSIQISWKAPRGKFGGYKLLVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKESKPAQGQFRIKDLEKRKDPKPRVKVVDRGNGSRPSSPEEVKFVCQTPAIADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTLTGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYNVAEFDLMHTVVESLTRTLCSRVEEQDREIKASAHAITGPPTELITSEVTARSFMVNWTHAPGNVEKYRVVYYPTRGGKPDEVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHTASEGLRGTETTLALPMASDLLLYDVTENSMRVKWDAVPGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYAMFGEEASDPVTGQETTLALSPPRNLRISNVGSNSARLTWDPTSRQINGYRIVYNNADGTEINEVEVDPITTFPLKGLTPLTEYTIAIFSIYDEGQSEPLTGVFTTEEVPAQQYLEIDEVTTDSFRVTWHPLSADEGLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLDDGSESEVVTAVGTTLDSFWTEPATTIVPTTSVTSVFQTGIRNLVVGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPEEEVIGTVMVPGSQNNLLLKPLLPDTEYKVTVTPIYTDGEGVSVSAPGKTLPSSGPQNLRVSEEWYNRLRITWDPPSSPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFASQASGFSDALTGMVKTLFLGVTNLQAKHVEMTSLCAHWQVHRHATAYRVVIESLQDRQKQESTVGGGTTRHCFYGLQPDSEYKISVYTKLQEIEGPSVSIMEKTQSLPTRPPTFPPTIPPAKEVCKAAKADLVFMVDGSWSIGDENFNKIISFLYSTVGALNKIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTKTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVFFVDDFDAFKKIEDELITFVCETASATCPVVHKDGIDLAGFKMMEMFGLVEKDFSSVEGVSMEPGTFNVFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRILPDTPQEPFALWEILNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGPEIRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASANITSDGVEVLGKMVRSRGPGGNSAPFQLQMFDIVCSTSWANTDKCCELPGLRDDESCPDLPHSCSCSETNEVALGPAGPPGGPGLRGPKGQQGEPGPKGPDGPRGEIGLPGPQGPPGPQGPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGKDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERGDLQSQAMVRSVARQVCEQLIQSHMARYTAILNQIPSHSSSIRTVQGPPGEPGRPGSPGAPGEQGPPGTPGFPGNAGVPGTPGERGLTGIKGEKGNPGVGTQGPRGPPGPAGPSGESRPGSPGPPGSPGPRGPPGHLGVPGPQGPSGQPGYCDPSSCSAYGVRAPHPDQPEFTPVQDELEAMELWGPGV