wanglab/gogpt-training-data huggingface dataset:
Protein: E1B protein, small T-antigen (E1B 19 kDa protein) (E1B-19K) (E1B-175R) (P03247)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity).
Subcellular location: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
Interaction partners:
Sequence:
MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQEEARRRRRQEQSPWNPRAGLDPRE
Protein: Probable leucine-rich repeat receptor-like protein kinase At5g05160 (EC 2.7.11.-) (Q9FHK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable leucine-rich repeat receptor-like protein kinase.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- WUSCHEL-related homeobox 4
- CLAVATA3/ESR
- CLAVATA3/ESR
- Dof zinc finger protein DOF5.6
- WUSCHEL-related homeobox 14
- Ribonuclease 3-like protein 3
Sequence:
MNSSHTAFVAASFFFLLLAATAVLVSADLASDEQALLNFAASVPHPPKLNWNKNLSLCSSWIGITCDESNPTSRVVAVRLPGVGLYGSIPPATLGKLDALKVLSLRSNSLFGTLPSDILSLPSLEYLYLQHNNFSGELTTNSLPSISKQLVVLDLSYNSLSGNIPSGLRNLSQITVLYLQNNSFDGPIDSLDLPSVKVVNLSYNNLSGPIPEHLKKSPEYSFIGNSLLCGPPLNACSGGAISPSSNLPRPLTENLHPVRRRQSKAYIIAIVVGCSVAVLFLGIVFLVCLVKKTKKEEGGGEGVRTQMGGVNSKKPQDFGSGVQDPEKNKLFFFERCNHNFDLEDLLKASAEVLGKGSFGTAYKAVLEDTTAVVVKRLREVVASKKEFEQQMEIVGKINQHSNFVPLLAYYYSKDEKLLVYKYMTKGSLFGIMHGNRGDRGVDWETRMKIATGTSKAISYLHSLKFVHGDIKSSNILLTEDLEPCLSDTSLVTLFNLPTHTPRTIGYNAPEVIETRRVSQRSDVYSFGVVILEMLTGKTPLTQPGLEDERVVIDLPRWVRSVVREEWTAEVFDVELLKFQNIEEEMVQMLQLALACVARNPESRPKMEEVARMIEDVRRLDQSQQLQQNRTSSEATSNVSE
Protein: Oxaloacetate tautomerase FAHD1, mitochondrial (EC 5.3.2.2) (Fumarylacetoacetate hydrolase domain-containing protein 1) (FAH domain-containing protein 1) (Q93ZE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable acylpyruvase. Binds copper in vitro.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20018591}.
Interaction partners:
- Fumarylacetoacetase
- Oxaloacetate tautomerase FAHD2, mitochondrial
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Homogentisate 1,2-dioxygenase
- Fumarate hydratase 1, mitochondrial
- Fumarate hydratase 2
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
Sequence:
MATSMIQRMFKQGTKIVCVGRNYAAHAKELGNAVPKEPVIFLKPTSSYLENGGTIEIPHPLDSLHHEVELALVIGQKARDVPESIAMDYIGGYAVALDMTARELQASAKASGLPWTVAKGQDTFTPISSVLPKAMVRDPDNLELWLKVDGETRQKGLTKDMIFKVPYLISYISSIMTLYEGDVILTGTPEGVGPVKIGQKITAGITGLSEVQFDVERRVKPLS
Protein: Adenosine transporter 2, putative (Q586M5)
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:
MAMLGFESTAEFFVYLTFIFFGMSVMNVTNAIYSNYNFFSEYYKFVKKQEKAEPENESFWKHMFTYYNVVVFTMQVVLEAFMLTPLGRRIPISWRLIFGLTIPMVEIIVILVIPAVGGSENGAIATMMMVAFVGGISKTLCDSSNAALAGPFPTKFYGAIVWGLAISGLMTSFLAIVIQASMDSSFTSKNTQSQIYFGLVMLLQVVACVLLVLLRKNPYAIKYAAEFRYAARKDGVTGDRADGEFDAKGTGPADENRYPDEKENKNVLNADIDPDDMRDTDQVEGTTNAQQMLDASVMVVVKRIWPMLVACFFVFFATLLVFPGVFIAAKTGDTSGWYFTVVVAMFNLGDFLSRLVLQFKQLHVSPRMVMIGSFARALLIIPLSLCAAGTVTGVWLPYIVSLLWGLTNGYFGGLSMIYGPRTGSLTTAGQRSLAAICINVALLMGLFVGAMFALAVKEGLPK
Protein: T-complex protein 11-like protein 2 (Q8N4U5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A7Z033}. Note=Accumulates around the actin complex before the formation of microfilament bundles and microtubule extension. {ECO:0000250|UniProtKB:A7Z033}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-1C chain
Sequence:
MPFNGEKQCVGEDQPSDSDSSRFSESMASLSDYECSRQSFASDSSSKSSSPASTSPPRVVTFDEVMATARNLSNLTLAHEIAVNENFQLKQEALPEKSLAGRVKHIVHQAFWDVLDSELNADPPEFEHAIKLFEEIREILLSFLTPGGNRLRNQICEVLDTDLIRQQAEHSAVDIQGLANYVISTMGKLCAPVRDNDIRELKATGNIVEVLRQIFHVLDLMQMDMANFTIMSLRPHLQRQLVEYERTKFQEILEETPSALDQTTEWIKESVNEELFSLSESALTPGAENTSKPSLSPTLVLNNSYLKLLQWDYQKKELPETLMTDGARLQELTEKLNQLKIIACLSLITNNMVGAITGGLPELASRLTRISAVLLEGMNKETFNLKEVLNSIGIQTCVEVNKTLMERGLPTLNAEIQANLIGQFSSIEEEDNPIWSLIDKRIKLYMRRLLCLPSPQKCMPPMPGGLAVIQQELEALGSQYANIVNLNKQVYGPFYANILRKLLFNEEAMGKVDASPPTN
Protein: Lysine-specific demethylase 6A (EC 1.14.11.68) (Histone demethylase UTX) (Ubiquitously-transcribed TPR protein on the X chromosome) (Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein) ([histone H3]-trimethyl-L-lysine(27) demethylase 6A) (O15550)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A. Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Retinoblastoma-binding protein 5
- Histone-lysine N-methyltransferase 2C
- WD repeat-containing protein 5
- PAX-interacting protein 1
- Nuclear receptor coactivator 6
- Histone-lysine N-methyltransferase 2D
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- PAXIP1-associated glutamate-rich protein 1
- Protein dpy-30 homolog
- Histone-lysine N-methyltransferase EZH2
Sequence:
MKSCGVSLATAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARTKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKSCSNTSALAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGHAVSHPPVQQQAHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRPTGVAQVRSTGIPNGPTADSSLPTNSVSGQQPQLALTRVPSVSQPGVRPACPGQPLANGPFSAGHVPCSTSRTLGSTDTILIGNNHITGSGSNGNVPYLQRNALTLPHNRTNLTSSAEEPWKNQLSNSTQGLHKGQSSHSAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNILTVPETSRHTGETPNSTASVEGLPNHVHQMTADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGTGTCDKVNNIHPAVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPMKTDLLLVNHKPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGRRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Down syndrome cell adhesion molecule 1, isoform BZ (A0A0B4K7T4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQHYEEDIHKAFVIRGNSAILKCDIPSFVADFVNVISWHSDEKENFYPGTEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGFKAPSFPSVASTFTIQSPKKSELALTCEAQSYPVPIFKWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPQIVPFAYEDLINMGDSIDLFCQIQKGDRPIKVHWSFERSAGDYGFDQVQPQMRTNRISEKTSMISIPSASPAHTGRDTCIASNKAGTTTYSVDLTVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) (Q9Y262)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MSYPADDYESEAAYDPYAYPSDYDMHTGDPKQDLAYERQYEQQTYQVIPEVIKNFIQYFHKTVSDLIDQKVYELQASRVSSDVIDQKVYEIQDIYENSWTKLTERFFKNTPWPEAEAIAPQVGNDAVFLILYKELYYRHIYAKVSGGPSLEQRFESYYNYCNLFNYILNADGPAPLELPNQWLWDIIDEFIYQFQSFSQYRCKTAKKSEEEIDFLRSNPKIWNVHSVLNVLHSLVDKSNINRQLEVYTSGGDPESVAGEYGRHSLYKMLGYFSLVGLLRLHSLLGDYYQAIKVLENIELNKKSMYSRVPECQVTTYYYVGFAYLMMRRYQDAIRVFANILLYIQRTKSMFQRTTYKYEMINKQNEQMHALLAIALTMYPMRIDESIHLQLREKYGDKMLRMQKGDPQVYEELFSYSCPKFLSPVVPNYDNVHPNYHKEPFLQQLKVFSDEVQQQAQLSTIRSFLKLYTTMPVAKLAGFLDLTEQEFRIQLLVFKHKMKNLVWTSGISALDGEFQSASEVDFYIDKDMIHIADTKVARRYGDFFIRQIHKFEELNRTLKKMGQRP
Protein: NAD-dependent histone deacetylase SIR2 (EC 2.3.1.286) (Regulatory protein SIR2) (Silent information regulator 2) (P06700)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:9214640}. Note=Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1.
Interaction partners:
- Nucleolar protein NET1
- Regulatory protein SIR1
- Tyrosine-protein phosphatase CDC14
- Regulatory protein SIR4
- Regulatory protein SIR3
- DNA replication fork-blocking protein FOB1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Histone H3
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Histone H4
Sequence:
MTIPHMKYAVSKTSENKVSNTVSPTQDKDAIRKQPDDIINNDEPSHKKIKVAQPDSLRETNTTDPLGHTKAALGEVASMELKPTNDMDPLAVSAASVVSMSNDVLKPETPKGPIIISKNPSNGIFYGPSFTKRESLNARMFLKYYGAHKFLDTYLPEDLNSLYIYYLIKLLGFEVKDQALIGTINSIVHINSQERVQDLGSAISVTNVEDPLAKKQTVRLIKDLQRAINKVLCTRLRLSNFFTIDHFIQKLHTARKILVLTGAGVSTSLGIPDFRSSEGFYSKIKHLGLDDPQDVFNYNIFMHDPSVFYNIANMVLPPEKIYSPLHSFIKMLQMKGKLLRNYTQNIDNLESYAGISTDKLVQCHGSFATATCVTCHWNLPGERIFNKIRNLELPLCPYCYKKRREYFPEGYNNKVGVAASQGSMSERPPYILNSYGVLKPDITFFGEALPNKFHKSIREDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQVLINRDPVKHAEFDLSLLGYCDDIAAMVAQKCGWTIPHKKWNDLKNKNFKCQEKDKGVYVVTSDEHPKTL
Protein: Fibrillarin, putative (Q388C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar RNA binding protein, putative
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit 2
- Uncharacterized protein
- Nrap protein domain-containing protein
- HEAT repeat-containing protein 1
- Centromere/microtubule binding protein cbf5, putative
- 50S ribosomal protein L7Ae, putative
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- Periodic tryptophan protein 2, putative
Sequence:
MRGGRGGGRGAGGGGFGRGGRGRGAFGGGGGGGRGGGRGSGRGGRGGGRGGGRGGGRGGGKAGGGMKGNIFQPHARMRGCYLLAGKDTLATKSLVPGVSIYGEKRVSGTIAGETESCEFRVWNPYRSKLAAAIYAGVAQIYMEPGSTVLYLGAASGTTVSHVSDLVGPEGVVYAVEFSHRSGRDLEEMSKRRSNIVPILEDARYPQKYRMLIPRLVDCIFMDVAQPDQARILALNAQHFLKQNGGFVISIKANCIDSTADSATVFASEVQKLKDSGLRPKEQASLEPFERDHAVVTGYYKSPPQ
Protein: Membrane associated guanylate kinase, WW and PDZ domain containing 1 (A0A8I3NPD4)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MASGGIPTHSSPAAQSLRSPNVDVFFLFYILLTGGKLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALQSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGDQEEHTLQEAALPPVNSSIVAAPITDASQKFPQYLPLCAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQPQQQQQQQQQQQQPPEEWTEDHSSLVPPVIPNHPPSNPEPAREAPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNGSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLIECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEYPPAEAPAPDQTDSSGQKKPDPFKIWAQSRSMYENRLPDCQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAAPKAENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSAAVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKPESQFEFKAPQAAQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYDPSSDRHGPAAAAGPQGVPEVRAAPPDRRPHPSLESSYPPDLHQSSQHGEKRAHGRDPKGSSRESSRQPNEHHTWNGTSRRPDGGACRPKDRAPEGRREAPPERLVPNGPKRRSPEKQRREGTRSADTTLERREKPERRRERSPGRRRDGSPGPRRRSLERLLEQTRPAERRRGMGSSPERRAKSTERRRARSPERRRERSLEKRDRDRDRDRDRDRDREELQRGGARGRAEPGPKPAPAAAPEPRRRPYKECSTDLSI
Protein: Large neutral amino acids transporter small subunit 2 (4F2-LC5) (L-type amino acid transporter 2) (Solute carrier family 7 member 8) (Q9N1Q4)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UHI5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UHI5}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9UHI5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UHI5}. Note=Localized to the cytoplasm when expressed alone. When coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi. {ECO:0000250|UniProtKB:Q9UHI5}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter heavy chain SLC3A1
- Solute carrier family 43 member 1
Sequence:
MEKGARHRHNTDKNHAGGSESEDFPEASSGGGGVALKKEIGLVSACGIIVGNIIGSGIFVSPKGVLENAGSVGLAVIVWIVTGLITAVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGFLRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPDSGLRLLAAICLLLLTWVNCSSVRWATRVQDIFTAGKLLALALIIIMGVVQICKGEYFWLEPKNAFDNFQEPDIGLIALAFLQGSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYITAMSPQELLASNAVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVKRCTPIPALLFTCLSTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPIKINLLFPIIYLLFWAFLLIFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFNDFIELLTLVSQKMCVVVYPEVDGGSGTEGTREDMEEQQQPICQPSPGKDKDSLEQSQP
Protein: Pumillio RNA binding protein, putative (Q38CK7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCSSSQGSLSLFLFVLFALKVSFWVYRMWTVQEDEYKNTELSFSGLELSPLSGTEDAAFKPIGVYTKSSQVFVNASTTPLTGTPPNDRCPTATLLPPQRTPGSPAAAGRFFPRSQAANVSVMRVDAPPFEPSSNNLAAAITFVETPTGGKRGGLPFTGPSERRSPHLMMPIDDTPGRDKDRTTSQYVEWSGHHVNSYHSHNAMRPFTTGGSGNSTVSVENLRGNVYELAKDQHGCRFLQRLLCDPEADCEIPRTIMSEIVPHVAELMTDQYANFLVQKLFDIMPKDVRYSVACVAAPKIAAIALTPHGTFSVQKMIETISSREELVIIREALSKDVVRLVKDANGNHAIQKVLQLFEPDDKEFVYAAVAVDCITIAKNKQGCCVLQRCLEYASPAQRSTLVRHILECCLQIAEDPYGNYVLQYVISAGDSKTIDTIAIAFLPHLVQLCMNKFSSNVMEKVLCRVSPLVQEMYVDTMCTPEVAARLIQDDFGNYVLQTALTICTAGQAEALVSVIRPLMPSIRNTPYAKKLEGKIESAMLKNANGHVPAVGVEMGRLLEMQEAGSEHSPSCHSSDIRAPQNQPLSG
Protein: SCF E3 ubiquitin ligase complex F-box protein grrA (F-box and leucine-rich repeat protein grrA) (F-box/LRR-repeat protein grrA) (SCF substrate adapter protein grrA) (C8V4D4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in meiosis and required for ascospore formation. Involved in substrate recognition in ubiquitin-dependent degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16824096}. Note=In the cytoplasm of ascogenous cells. Within these cells, defined areas that resembled immature ascospores were excluded from the staining.
Interaction partners:
- E3 ubiquitin ligase complex SCF subunit sconC
- Protein phosphatase PP2A regulatory subunit B
- Cullin-1
- Uncharacterized protein
- RING-box protein 1
- SCF ubiquitin ligase subunit CulC, putative
- Serine/threonine-protein phosphatase PP2A catalytic subunit
- Ubiquitin-like domain-containing protein
- Protein phosphotase 2a 65kd regulatory sububit
- Cullin-associated NEDD8-dissociated protein 1, C-terminal part
Sequence:
MARSRQPTRFSSEAPSESSSSTSPERAADDDTDFFTLQANDSQSSIGAGNPRDSHIQNDPETVLPPIAYLPPEILISIFSKLSSPRDLLSCLLVCRIWALNCVGLLWHRPSCNNWDNLKKIAAAVGEEDSFFLYSSLIKRLNLSALTEDVSDGTVVPFSQCNRIERLTLTNCRKLTDIGVSDLVVGSRHLQALDVSELRSLTDHTLFKVAENCNRLQGLNITGCVKVTDDSLIAVSQNCRLLKRLKLNGVSQVTDKAILSFAQNCPSILEIDLQECKLVTNQSVTALMTTLQNLRELRLAHCTEIDDSAFLDLPRHIQMTSLRILDLTACENIRDEAVERIVSSAPRLRNLVLAKCKFITDRAVWAICKLGKNLHYVHLGHCSNINDSAVIQLVKSCNRIRYIDLACCSRLTDRSVQQLATLPKLRRIGLVKCQLITDASILALARPAQDHSVPCSSLERVHLSYCVNLTMVGIHALLNSCPRLTHLSLTGVAAFLREELTVFCREAPPEFTRQQREVFCVFSGEGVNRLRNHLNREAAPQRDANEATMYDDEEELDEDEGQVTGLMHAAAINDDDYINITPPHA
Protein: Secretogranin-2b (Secretogranin II b) [Cleaved into: Secretoneurin-b (SNb)] (A0JMK6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules (By similarity). Required for neurovascular modeling of the hindbrain. Acts in a non-cell autonomous manner and is required for migration and proliferation of central artery endothelial cells. Required for normal courting behavior and spawning.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Chromogranin B
- Neuromedin U
Sequence:
MMLSLPKLSAGGVVVLLATLLHTLTVQGASVRHHRLRGGDQGGFLAPSSDMIKALEYIESLKQRADGPESPTGDYDEVDKFRFLVQLASLQDENTPTHEDATRWPDNKVPQWVRSLLRVLDQAGESPESQAAGNERRLHKTRRPVADGESPAGDYAGFVKPHKKYPLMFEDEENGRDNKRATEDLDEQYTPQSLANMRSIFEELGKLSAAQKRDDEEDGEDDDDLYRVRNAAYEDVTGGEEWVPLEEQLETEELVKGSHEEYKRALGDISEQGMENMERRGEEEDENPDDDTKLVDYYLLKVLEMTDQAQKRDLMEGRRRLLSRPSLIDPRAIKQLLSAISMKLQVPPEDLVGMLFMEETRKQQQRLPEPQLARNPSQPRYKSRVIKYYNGRQPEVTVSDIPHDVKTEDILKVLGLGNLANKNAKFSLLKQRPYKTAMTNYFNPNGRRGSLFLSELNKAPSKRKDDYDDDDAVDEDEESTFLAAKLLTEYPDTSSSNRKRAIDSAANGQLPYELYEEAMKDFFDQVDNGKSALAKRDTQGKEEPEGPQKPPAQDPAQETVDQTPPESGTEDGKEYHGKIVAGM
Protein: Small ribosomal subunit protein mS29 (28S ribosomal protein S29, mitochondrial) (MRP-S29) (S29mt) (Death-associated protein 3) (DAP-3) (Q9ER88)
Organism: Mus musculus (Mouse)
Function: Involved in mediating interferon-gamma-induced cell death.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P51398}.
Interaction partners:
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS14m
Sequence:
MLTGITRLFSRVQKLDPRCFLHMSVQATQNSQVPAERPRTVSRTSDSDPAKHGEQHEGQHYSIPLQDLKTVFPHGLPPRYMMQVKTFGEACLMVRKPALELLGYLKNTNFAHPAVRYLLYGEKGTGKTLSLCHAVHFCARHDWLILHIPDAHLWVKNCRELLQSTHNKQRFDQPLEASTWLKNFKTTNERFLSQIKVQEKYVWNKRESTEKGSPLGEVVEQGLTRVRNATDAVGVVLKELKAQSALGLFHLLVAVDGVNALWGRTTLKKEDRTLIAPEELSLVHNLRKMVKNDWHGGAIVLSLSQTGSLFKSRTAYLPHELLGKEGFNALEPFLPILIPNYNPKEFESSFQYYLENNWLQHEKASTEEGRKELRFLSNCNPEQLERLCASL