wanglab/gogpt-training-data huggingface dataset:
Protein: Ribonucleoside-diphosphate reductase subunit alpha (EC 1.17.4.1) (Ribonucleotide reductase R1 subunit) (P9WH75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. When coexpressed in E.coli with nrdF2 the 2 proteins complement a temperature-sensitive E.coli mutant, however coexpression with nrdF1 does not complement.
Interaction partners:
- Ribonucleoside-diphosphate reductase subunit beta nrdF2
- Protein NrdI
- Glutaredoxin-like protein NrdH
- Ribonucleoside-diphosphate reductase subunit beta nrdF1
- R2-like ligand binding oxidase
- UPF0301 protein Rv0038
- Thymidylate kinase
- Cytidylate kinase
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Adenylate kinase
Sequence:
MPPTVIAEPVASGAHASYSGGPGETDYHALNAMLNLYDADGKIQFDKDREAAHQYFLQHVNQNTVFFHNQDEKLDYLIRENYYEREVLDQYSRNFVKTLLDRAYAKKFRFPTFLGAFKYYTSYTLKTFDGKRYLERFEDRVVMVALTLAAGDTALAELLVDEIIDGRFQPATPTFLNSGKKQRGEPVSCFLLRVEDNMESIGRSINSALQLSKRGGGVALLLTNIREHGAPIKNIENQSSGVIPIMKLLEDAFSYANQLGARQGAGAVYLHAHHPDIYRFLDTKRENADEKIRIKTLSLGVVIPDITFELAKRNDDMYLFSPYDVERVYGVPFADISVTEKYYEMVDDARIRKTKIKAREFFQTLAELQFESGYPYIMFEDTVNRANPIDGKITHSNLCSEILQVSTPSLFNEDLSYAKVGKDISCNLGSLNIAKTMDSPDFAQTIEVAIRALTAVSDQTHIKSVPSIEQGNNDSHAIGLGQMNLHGYLARERIFYGSDEGIDFTNIYFYTVLYHALRASNRIAIERGTHFKGFERSKYASGEFFDKYTDQIWEPKTQKVRQLFADAGIRIPTQDDWRRLKESVQAHGIYNQNLQAVPPTGSISYINHSTSSIHPIVSKVEIRKEGKIGRVYYPAPYMTNDNLEYYEDAYEIGYEKIIDTYAAATQHVDQGLSLTLFFKDTATTRDVNKAQIYAWRKGIKTLYYIRLRQMALEGTEVEGCVSCML
Protein: Kappa-type opioid receptor (K-OR-1) (KOR-1) (P41145)
Organism: Homo sapiens (Human)
Function: G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:22437504, ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}; Multi-pass membrane protein {ECO:0000269|PubMed:12004055, ECO:0000269|PubMed:22437504, ECO:0000269|PubMed:7624359, ECO:0000269|PubMed:8060324}.
Interaction partners:
Sequence:
MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPV
Protein: Polyamine-modulated factor 1 (PMF-1) (Q9CPV5)
Organism: Mus musculus (Mouse)
Function: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis (By similarity). May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Associated with the kinetochore. {ECO:0000250}.
Interaction partners:
- Kinetochore-associated protein DSN1 homolog
- Kinetochore-associated protein NSL1 homolog
- Protein MIS12 homolog
- Kinetochore protein Spc24
- Kinetochore protein Nuf2
- Outer kinetochore KNL1 complex subunit ZWINT
- Kinetochore protein NDC80 homolog
- Centromere protein T
- Kinetochore protein Spc25
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Sequence:
MAEVSRDSEAAERGPEGSSPEAVPGDATIPRVKLLDAIVDTFLQKLVADRSYERFTTCYKHFHQLNPEVTQRIYDKFVAQLQTSIREEISEIKEEGNLEAVLNSLDKIIEEGRERGEPAWRPSGIPEKDLCSVMAPYFLKQQDTLCHQVRKQEAKNQELADAVLAGRRQVEELQQQVRALQQTWQALHREQRELLSVLRAPE
Protein: Protein-lysine N-trimethyltransferase SMYD5 (EC 2.1.1.-) (Protein NN8-4AG) (Retinoic acid-induced protein 15) (SET and MYND domain-containing protein 5) ([histone H3]-lysine20 N-trimethyltransferase SMYD5) (EC 2.1.1.372) ([histone H4]-lysine36 N-trimethyltransferase SMYD5) (EC 2.1.1.359) (Q6GMV2)
Organism: Homo sapiens (Human)
Function: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression (By similarity). In association with the NCoR corepressor complex, is involved in the repression of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages by catalyzing the formation of H4K20me3 at the gene promoters (By similarity). Plays an important role in embryonic stem (ES) cell self-renewal and differentiation (By similarity). Promotes ES cell maintenance by silencing differentiation genes through deposition of H4K20me3 marks (By similarity). Maintains genome stability of ES cells during differentiation through regulation of heterochromatin formation and repression of endogenous repetitive DNA elements by depositing H4K20me3 marks.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:39048817, ECO:0000269|PubMed:39103523}.
Interaction partners:
- Protein-lysine N-methyltransferase SMYD4
- Histone-lysine N-methyltransferase SMYD1
Sequence:
MAASMCDVFSFCVGVAGRARVSVEVRFVSSAKGKGLFATQLIRKGETIFVERPLVAAQFLWNALYRYRACDHCLRALEKAEENAQRLTGKPGQVLPHPELCTVRKDLHQNCPHCQVMYCSAECRLAATEQYHQVLCPGPSQDDPLHPLNKLQEAWRSIHYPPETASIMLMARMVATVKQAKDKDRWIRLFSQFCNKTANEEEEIVHKLLGDKFKGQLELLRRLFTEALYEEAVSQWFTPDGFRSLFALVGTNGQGIGTSSLSQWVHACDTLELKPQDREQLDAFIDQLYKDIEAATGEFLNCEGSGLFVLQSCCNHSCVPNAETSFPENNFLLHVTALEDIKPGEEICISYLDCCQRERSRHSRHKILRENYLFVCSCPKCLAEADEPNVTSEEEEEEEEEEEGEPEDAELGDEMTDV
Protein: Inactive 2'-5'-oligoadenylate synthase 1D (Q8VI95)
Organism: Mus musculus (Mouse)
Function: Does not have 2'-5'-olygoadenylate synthetase activity, but can bind double-stranded RNA. May play a role in the control of female fertility, possibly by binding to and inhibiting OAS1A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15899864}.
Interaction partners:
Sequence:
MARELFRTPIWRLDKFIEDQLLPDTTFLTELRADIDSISAFLMERCFQGAAHPVRVSRVVMGGCYNEYTVLKGRSEANMVVFLINLTSFEDQFNGQVVFIEEIWRHLLQLQQEKLCKLKFEVQSPKEPNSRFLSFKLSCPERQHELEFDVQPAYDALYEVRHFKPFDSSNYNKVYAQLTHECTTLEKEGEFSICFTDLHQSFLRYRAPKLWNLIRLVKHWYQLCKEKLRGPLPPQYALELLTVYVWEYGIHENPGLHTAQCFRTVLELVTKYKRLRIYWTWCYDFQHEISDYLQGQIKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQIWIDSTFFTNHDMSIVEAWEVMPERQECVFL
Protein: Tripartite terminase subunit 3 (EC 3.1.-.-) (Terminase large subunit) (P04295)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM2 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM3 carries an RNase H-like nuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013, ECO:0000269|PubMed:16920825, ECO:0000269|PubMed:17392365}. Note=Responsible for the nuclear localization of the two others subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013, ECO:0000269|PubMed:17392365}.
Interaction partners:
Sequence:
MFGQQLASDVQQYLERLEKQRQLKVGADEASAGLTMGGDALRVPFLDFATATPKRHQTVVPGVGTLHDCCEHSPLFSAVARRLLFNSLVPAQLKGRDFGGDHTAKLEFLAPELVRAVARLRFKECAPADVVPQRNAYYSVLNTFQALHRSEAFRQLVHFVRDFAQLLKTSFRASSLTETTGPPKKRAKVDVATHGRTYGTLELFQKMILMHATYFLAAVLLGDHAEQVNTFLRLVFEIPLFSDAAVRHFRQRATVFLVPRRHGKTWFLVPLIALSLASFRGIKIGYTAHIRKATEPVFEEIDACLRGWFGSARVDHVKGETISFSFPDGSRSTIVFASSHNTNGIRGQDFNLLFVDEANFIRPDAVQTIMGFLNQANCKIIFVSSTNTGKASTSFLYNLRGAADELLNVVTYICDDHMPRVVTHTNATACSCYILNKPVFITMDGAVRRTADLFLADSFMQEIIGGQARETGDDRPVLTKSAGERFLLYRPSTTTNSGLMAPDLYVYVDPAFTANTRASGTGVAVVGRYRDDYIIFALEHFFLRALTGSAPADIARCVVHSLTQVLALHPGAFRGVRVAVEGNSSQDSAVAIATHVHTEMHRLLASEGADAGSGPELLFYHCEPPGSAVLYPFFLLNKQKTPAFEHFIKKFNSGGVMASQEIVSATVRLQTDPVEYLLEQLNNLTETVSPNTDVRTYSGKRNGASDDLMVAVIMAIYLAAQAGPPHTFAPITRVS
Protein: Glutathione peroxidase 1 (GPx-1) (GSHPx-1) (EC 1.11.1.9) (Cellular glutathione peroxidase) (Phospholipid-hydroperoxide glutathione peroxidase GPX1) (EC 1.11.1.12) (P07203)
Organism: Homo sapiens (Human)
Function: Protects the hemoglobin in erythrocytes from oxidative breakdown. In platelets, plays a crucial role of glutathione peroxidase in the arachidonic acid metabolism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}.
Interaction partners:
Sequence:
MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA
Protein: Preprofallaxidin-4 [Cleaved into: Fallaxidin-4.2] (B5LUQ5)
Organism: Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax)
Subcellular location: Secreted {ECO:0000250|UniProtKB:B5LUQ4}.
Interaction partners:
Sequence:
MASLKKFLFLVLFLGMVSLSICDKEKREGENEEEEEEHEEESEEKRGLFSFLPKVIGVIGPLIHPPS
Protein: Uncharacterized kinase C1B1.02c (EC 2.7.1.-) (O13863)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MEPGSKLSEDETFSQTFNEEEQEDSRNKDILAFDPSVDNEPLLTKKLSSLSIYSEPSPDEASNLQELKFVSSPPSVRVPRSRRNRRNSRVDSEARKRQFDRVKHSVSNSCKLHLSLQGQEAAQLRSDSLYLEASDKRDLTSLVTRVKELARKLSAARLAFRFRKVLLICNDNKESIERSVELAQWLLDTFSFTPSSSHNNMASSNTQSNTQLSEMESEEKSFNKDVYPNDEYTPFTPKNQFVIYLEDTLASLDVVESLSPKKNVRFWTSELCTQCPNLFDCVITVGDDSAALRASWLFQDVVPPVLSFSTAKAGFLSILPIAEYTKTLDLIFHRGFTVNLRMRFQCSIMRYVGEHSTHICEGQYSVLNELLIDRGPNPFMISLDLYVENEYITTLQSDGVCVSTPTGSTAYSVAAGGSLCHPGIPAILISAICPHSLSFRPIILPDSMTLRIVVPLDARSNAWCAFDGHHRIELGLGDYISISASSFPFPSVIRSKYSKDWFDILRQTLNWNDRKGRQRSSRYKSHVHKTNTSEEQN
Protein: Jasmonate-induced oxygenase 1 (EC 1.14.11.-) (2-oxoglutarate-dependent dioxygenase JOX1) (Jasmonic acid oxidase 1) (Q9SRM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 2-oxoglutarate-dependent dioxygenase involved in the oxidation of jasmonate (JA), a stress-induced phytohormone synthesized in response to attack by pathogens and herbivores, which triggers the activation of defense responses via the JA-mediated signaling pathway. Converts JA to 12-hydroxyjasmonate (12OH-JA), an inactive form of JA. Prevents over-accumulation of JA and indirectly its bioactive form JA-Ile under stress response. Acts as negative regulator of JA-mediated defense signaling, by contributing to 12OH-JA accumulation, which represses JA defense responses upon infection by the fungal pathogen Botrytis cinerea and the herbivorous caterpillar Mamestra brassicae.
Interaction partners:
- Protein STRICTOSIDINE SYNTHASE-LIKE 5
- 2-oxoglutarate-dependent dioxygenase-like protein
- NAC domain-containing protein 79
Sequence:
MNNLDEIKIESKTCLNDQEQEVKIDNMHMSDQDKNKIEIKNKSGLGEKWPEPIVRVQSLAESNLTSLPDRYIKPPSQRPQTTIIDHQPEVADINIPIIDLDSLFSGNEDDKKRISEACREWGFFQVINHGVKPELMDAARETWKSFFNLPVEAKEVYSNSPRTYEGYGSRLGVEKGAILDWNDYYYLHFLPLALKDFNKWPSLPSNIREMNDEYGKELVKLGGRLMTILSSNLGLRAEQLQEAFGGEDVGACLRVNYYPKCPQPELALGLSPHSDPGGMTILLPDDQVVGLQVRHGDTWITVNPLRHAFIVNIGDQIQILSNSKYKSVEHRVIVNSEKERVSLAFFYNPKSDIPIQPMQQLVTSTMPPLYPPMTFDQYRLFIRTQGPRGKSHVESHISPR
Protein: Transmembrane protein (O69657)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MHKRYAPQRPKPDTETYIEKCTDRRQDGGHDERRQLLRPVSMLPPGYPVEPPPVAPGYAPAGYPPYPATPPGYGPPGYGAPPSYGPPPGYGPPLGYPAAPPGCGPPPGYGPPLGYGPPVAPGAVKPGIIPLRPLTLSDIFNGAVGYIRANPKATLGLTAMVVVTLQIISLVALFGPMTAFGDIVTGEPDELTGAVVGGWSASFGASLLVSWLAGVLLSGMLTVIVGRAVFGSPITVGEAWAKVRGRLLALFGLALLEAAGVVAVLGLAVVILSGVAAAANEAAAALLGFPLLLVVGVSLAYLYVVLLFAPVLIVLERLPIVEAITRSFALVRHGFWRVLGIRLLTVLVVGVVGNAIAAPFMIVGEIVTAVTASDGSVTMRLVGATLSAIGVTIGQIVTAPFSAGVVVLLYTDRRIRAEAFDLVLQTGLEAGPAGGPAPVESTDNLWLTRPF
Protein: Protein shisa-5 (Scotin) (Q9D7I0)
Organism: Mus musculus (Mouse)
Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein {ECO:0000269|PubMed:12135983}. Nucleus membrane {ECO:0000269|PubMed:12135983}.
Interaction partners:
Sequence:
MAAPAPSLWTLLLLLLLLPPPPGAHGELCRPFGEDNSIPVFCPDFCCGSCSNQYCCSDVLRKIQWNEEMCPEPESRFSTPAEETPEHLGSALKFRSSFDSDPMSGFGATVAIGVTIFVVFIATIIICFTCSCCCLYKMCCPQRPVVTNTTTTTVVHAPYPQPQPQPVAPSYPGPTYQGYHPMPPQPGMPAAPYPTQYPPPYLAQPTGPPPYHESLAGASQPPYNPTYMDSLKTIP
Protein: Actin-related protein 10 (Actr10 protein) (Q7ZVU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPLFEGLGSGGEKTAVVIDLGAAYTKCGFAGETGPRFIIPSEIKHPGSQEVVAVVQFNINTEELYTILKEFIHLLYFRHLLVNPRDRRVVVIESILCPSHYRDTLSRVLFRHFEVPSVLFAPSHLMSIMTLGLQSALVMDCGYTETLVLPIYEGIPILSAWEALPMGGKAIHKELQSLLSEQCTVDTDSSTGLQLPSVISHIPEDVVEDIKVRTCFVSDLQRGLKIQEAKFNTDAERPAPPPDVDYPLDGQKILHVKGFIRDSVAEMLFEQDNEEKSIATLLLDTLVKCPIDTRKVLSENLLIIGGTAMLPGFLHRLLAEIRSLVEKPKYRDALATKSFRIHSPPAKPNCTAWLGGAIFGALQDILGSRSVSRDYYNHTGRIPDWCCLSSPPPDSIYEAGKTPPPLMKRAFSTEK
Protein: Down syndrome cell adhesion molecule 1, isoform AS (Q0E9L3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQFYITEAENEYVIKGNAAVVKCKIPSFVADFVQVEAWVDEEGMELWRNNATDAYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPISSAVPKVVSLAKFDMKTYSGSSTMALLCPAQGYPVPVFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFDFGDAPTNVEDSVSVMCLISNGDLPIDIEWFFNDYGISSYSGINVVKGGKRNSMLSIDSVQARHAGKYSCRAKNHAAAVNYTTELIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Aladin (Adracalin) (Q9NRG9)
Organism: Homo sapiens (Human)
Function: Plays a role in the normal development of the peripheral and central nervous system. Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19782045}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26246606}. Nucleus envelope {ECO:0000269|PubMed:27754849}. Note=In metaphase cells localizes within the spindle with some accumulation around spindle poles, with the highest concentration between the centrosome and metaphase plate (PubMed:26246606). The localization to the spindle is microtubule-mediated (PubMed:26246606). {ECO:0000269|PubMed:26246606}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup88
- Nucleoporin NDC1
- Nucleoporin SEH1
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup155
- Nucleoporin NUP35
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein Nup93
Sequence:
MCSLGLFPPPPPRGQVTLYEHNNELVTGSSYESPPPDFRGQWINLPVLQLTKDPLKTPGRLDHGTRTAFIHHREQVWKRCINIWRDVGLFGVLNEIANSEEEVFEWVKTASGWALALCRWASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVASLAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWTCERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGKPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIAHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL
Protein: Mitochondrial carrier protein, putative (Q387U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSAAEKKHAPLVDVVAGGLGSAAAKSLLAPFQRIVILQQLGEHRNLNTFQLVSHIKRNEGWRGFWRGNLTSMIIRVPYSGMQFVTYSRLKFLFQDLSERYVRPPKGDDGDIRNASRHVETAELFLMKCGAGGISATIAGVAVYPGEVVRLRLMSGEKQFKSIMGTIRIIHAETNSMKNFYRGLGASLLQRVPDILINFATYETIKYKLMEKDFLKDHPSYKNAISTTIGGATAAVASIAVCFPLDVAKRRIGMSGQGKSGIVHRGVRECLWHVYRYEGIRGLYGGASVEIMRCVPQVVLMWFFIEATQKFLTNYGFGSDAQP
Protein: Cation channel sperm-associated auxiliary subunit zeta (CatSper-zeta) (CatSperzeta) (Protein expressed in male leptotene and zygotene spermatocytes 622) (MLZ-622) (Testis-expressed protein 40) (Q9CQP8)
Organism: Mus musculus (Mouse)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for a distribution of the CatSper complex in linear quadrilateral nanodomains along the flagellum, maximizing fertilization inside the mammalian female reproductive tract. Together with EFCAB9, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:28226241}; Peripheral membrane protein {ECO:0000305}. Note=Specifically located in the principal piece of sperm tail (PubMed:28226241). Although it does not contain a transmembrane domain, localizes with the CatSper complex at the flagellum membrane (PubMed:28226241). {ECO:0000269|PubMed:28226241}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit gamma 2
- Solute carrier organic anion transporter family member 6C1
Sequence:
MEESVKPVPKHANHRRSSVRSSLYGDVRDLWSTATMSTANVSVSDVCEDFDEEGKSVRNRIRKYSQTISIRDSLNLEPEEIQQQARRELELCHGRSLEHGEDHEESETSLASSTSESLIFSLWKPHRTYWTEQQNRLPLPLMELMETEVLDILKKALITYRSTIGRNHFMTKELQGYIEGIRKRRNKRLYFLDQ
Protein: Lymphocyte antigen 75 (Ly-75) (C-type lectin domain family 13 member B) (DEC-205) (gp200-MR6) (CD antigen CD205) (O60449)
Organism: Homo sapiens (Human)
Function: Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment (By similarity). Causes reduced proliferation of B-lymphocytes.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- C-type lectin domain family 4 member A
- CD209 antigen
- Cancer/testis antigen 1
- Integrin alpha-X
- C-type lectin domain family 9 member A
- C-type lectin domain family 4 member K
- T-lymphocyte activation antigen CD86
- T-cell surface glycoprotein CD4
- Tumor necrosis factor receptor superfamily member 5
- C-type lectin domain family 7 member A
Sequence:
MRTGWATPRRPAGLLMLLFWFFDLAEPSGRAANDPFTIVHGNTGKCIKPVYGWIVADDCDETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSSAMLWWKCEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGSEESLCDQPYHEIYTRDGNSYGRPCEFPFLIDGTWHHDCILDEDHSGPWCATTLNYEYDRKWGICLKPENGCEDNWEKNEQFGSCYQFNTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTIGGSSCARMDAESGLWQSFSCEAQLPYVCRKPLNNTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVCKRKGEKLNDASSDKMCPPDEGWKRHGETCYKIYEDEVPFGTNCNLTITSRFEQEYLNDLMKKYDKSLRKYFWTGLRDVDSCGEYNWATVGGRRRAVTFSNWNFLEPASPGGCVAMSTGKSVGKWEVKDCRSFKALSICKKMSGPLGPEEASPKPDDPCPEGWQSFPASLSCYKVFHAERIVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKRSPDLQGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFHRPWRRGWHFYDDREFIYLRPFACDTKLEWVCQIPKGRTPKTPDWYNPDRAGIHGPPLIIEGSEYWFVADLHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQKWWIRISEWPIDDHFTYSRYPWHRFPVTFGEECLYMSAKTWLIDLGKPTDCSTKLPFICEKYNVSSLEKYSPDSAAKVQCSEQWIPFQNKCFLKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRLRIPENFFEEESRYHCALILNLQKSPFTGTWNFTSCSERHFVSLCQKYSEVKSRQTLQNASETVKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAETNGQLEDCVVLDTDGFWKTVDCNDNQPGAICYYSGNETEKEVKPVDSVKCPSPVLNTPWIPFQNCCYNFIITKNRHMATTQDEVHTKCQKLNPKSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTPLSYTHWRAGRPTIKNEKFLAGLSTDGFWDIQTFKVIEEAVYFHQHSILACKIEMVDYKEEYNTTLPQFMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDGSESSFEWSDGSTFDYIPWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKPTKSKKLSRLTYSSRCPAAKENGSRWIQYKGHCYKSDQALHSFSEAKKLCSKHDHSATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKVECEHGFGRVVCKVPLGPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEIMLPSFHD
Protein: Small ribosomal subunit protein uS3 (EC 4.2.99.18) (40S ribosomal protein S3) (E9PL09)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
Interaction partners:
Sequence:
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
Protein: Narrow, isoform B (A0A0B4JCT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKIVLFCLLSLLACAAGQRITTIHLDGVQYFISRMNPYSPELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNAGYGNYDFWTSGNRLGTGMFLWMSTGLPFNATFDFFENSADAIQAGLLDPVDHNSNTSPQRTARDSSGAEKGCVILKQPTLKWMPEDCSAVKDFICEQTRCYYYNYGSIPVSSAQG
Protein: T-cell surface glycoprotein CD3 epsilon chain (A0A8I6AAG4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
PHLCLKQKTNGKIELSGQQRQNEKNPNTCTHQGLVFRLKSESSFQNGGAAAELHCFLELPGKEPQLSKLLCVKCCAFTFNAGCFLVQLPPELAGSLCLIPCSKCPSPWHRKYCYVTVGGKDLRCQFWSDRSTTLLVWNFRHSQHLLTHVSPACFPVGTCQEDIEDTVTDDGAQKQYEVSISGTSVELTCPLENEDNLKWEKNDKVLPDKNEKHLVLEDFSEVKDSGYYVCYTESSRKNTYLYLKARVCENCMEVDLTAVSIIIIVDICITLGLLMVVYYWSKKRKAKAKPVTRGTGTGGRPRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRAV