wanglab/gogpt-training-data huggingface dataset:
Protein: Patched domain-containing protein 1 (Q96NR3)
Organism: Homo sapiens (Human)
Function: Required for the development and function of the thalamic reticular nucleus (TRN), a part of the thalamus that is critical for thalamocortical transmission, generation of sleep rhythms, sensorimotor processing and attention.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20844286, ECO:0000269|PubMed:33856728}; Multi-pass membrane protein {ECO:0000269|PubMed:20844286}. Cell projection, dendritic spine {ECO:0000269|PubMed:33856728}.
Interaction partners:
- Disks large-associated protein 2
- SH3 and multiple ankyrin repeat domains protein 2
- Neuroligin-4, X-linked
- Neuroligin-3
- Contactin-associated protein-like 2
- Sonic hedgehog protein
- Ras/Rap GTPase-activating protein SynGAP
- Probable ATP-dependent RNA helicase DDX53
- SH3 and multiple ankyrin repeat domains protein 3
Sequence:
MLRQVLHRGLRTCFSRLGHFIASHPVFFASAPVLISILLGASFSRYQVEESVEHLLAPQHSLAKIERNLVNSLFPVNRSKHRLYSDLQTPGRYGRVIVTSFQKANMLDQHHTDLILKLHAAVTKIQVPRPGFNYTFAHICILNNDKTCIVDDIVHVLEELKNARATNRTNFAITYPITHLKDGRAVYNGHQLGGVTVHSKDRVKSAEAIQLTYYLQSINSLNDMVAERWESSFCDTVRLFQKSNSKVKMYPYTSSSLREDFQKTSRVSERYLVTSLILVVTMAILCCSMQDCVRSKPWLGLLGLVTISLATLTAAGIINLTGGKYNSTFLGVPFVMLGHGLYGTFEMLSSWRKTREDQHVKERTAAVYADSMLSFSLTTAMYLVTFGIGASPFTNIEAARIFCCNSCIAIFFNYLYVLSFYGSSLVFTGYIENNYQHSIFCRKVPKPEALQEKPAWYRFLLTARFSEDTAEGEEANTYESHLLVCFLKRYYCDWITNTYVKPFVVLFYLIYISFALMGYLQVSEGSDLSNIVATATQTIEYTTAQQKYFSNYSPVIGFYIYESIEYWNTSVQEDVLEYTKGFVRISWFESYLNYLRKLNVSTGLPKKNFTDMLRNSFLKAPQFSHFQEDIIFSKKYNDEVDVVASRMFLVAKTMETNREELYDLLETLRRLSVTSKVKFIVFNPSFVYMDRYASSLGAPLHNSCISALFLLFFSAFLVADSLINVWITLTVVSVEFGVIGFMTLWKVELDCISVLCLIYGINYTIDNCAPMLSTFVLGKDFTRTKWVKNALEVHGVAILQSYLCYIVGLIPLAAVPSNLTCTLFRCLFLIAFVTFFHCFAILPVILTFLPPSKKKRKEKKNPENREEIECVEMVDIDSTRVVDQITTV
Protein: coproporphyrinogen oxidase (EC 1.3.3.3) (Q6FM03)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Porphobilinogen deaminase
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MTAPQDPKHLPIRQQMEALIRRKQKEITEGLESIDTVKFTADTWERGNDGGGGTSMVIQNGSTFEKGGVNVSVVYGELTPGAVLAMKQEHKDLKLPESANGLPNSEGVKFFACGLSMVIHPVNPLAPTTHLNYRYFETWNPDGTPQTWWFGGGADLTPFYLFEEDAEHFHKLHKAALDKHDTALYPRFKKWCDEYFYIAHRGETRGIGGIFFDDYNEKDPQEILKICEDCFDAFLPSYLTIMKRRKDLPYNEKQKNWQLIRRGRYAEFNLIYDRGTQFGLRTPGSRVESILMSLPLHASWVYNHHPEPGSEEAKLLEVTTKPREWVN
Protein: Insulator binding factor 2 (RE22911p) (Q9VHG6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Insulator binding factor 1, isoform A
- Centrosome-associated zinc finger protein Cp190
- Zinc finger protein ZIPIC
- Boundary element associated factor
- Modifier of mdg4
- Zinc finger protein su
- LD05287p
- FI23914p1
Sequence:
MSQAKKAKRPSGLSKDETWKKLGFLPAFKGGKDGEPKKYRALCTHCRKCQSNTSIDRLIIHRKSCLKFREDLTAEFGIKVEATDAAPAEQSSSGSTIDFTSNILLDKLIDEDDSSARNQESNLVSYLTDLDQLVIPSSDANRLQKDLIKAETEYLVVKSEYFTKMNEISELKRTVTLLEAKKTQLEIAKLRAECE
Protein: Protein CHROMATIN REMODELING 19 (AtCHR19) (EC 3.6.4.-) (AtRAD54-like protein) (Q9ZUL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs (By similarity). Probable chromatin remodeling factor. Probable helicase-like transcription factor involved in transcriptional gene silencing. Associates with SUVR2 and contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. May be involved in nucleosome positioning to form ordered nucleosome arrays on chromatin.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:25420628}.
Interaction partners:
- Probable inactive histone-lysine N-methyltransferase SUVR2
- Telomerase reverse transcriptase
- DNA mismatch repair protein MSH5
- DNA-directed primase/polymerase protein
Sequence:
MKRDFDEISEEEWSQHSFNASRVLKRPRTPKKTRAATNPTPSIESFAFRRPSTAMTIESNSSDGDCVEIEDLGDSDSDVKIVNGEDLLLEDEEEVEETKVVMRAARVGRRFVIEDEEASDDDDDEAESSASEDEFGGGGGGSGGRRGEDEDVVGKALQKCAKISADLRKELYGTSSGVTDRYSEVETSTVRIVTQNDIDDACKAEDSDFQPILKPYQLVGVNFLLLLYKKGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVLQYHGAARAAYSRELNSLSKAGKPPPFNVLLVCYSLFERHSEQQKDDRKVLKRWRWSCVLMDEAHALKDKNSYRWKNLMSVARNANQRLMLTGTPLQNDLHELWSLLEFMLPDIFTTENVDLKKLLNAEDTELITRMKSILGPFILRRLKSDVMQQLVPKIQRVEYVLMERKQEDAYKEAIEEYRAASQARLVKLSSKSLNSLAKALPKRQISNYFTQFRKIANHPLLIRRIYSDEDVIRIARKLHPIGAFGFECSLDRVIEEVKGFNDFRIHQLLFQYGVNDTKGTLSDKHVMLSAKCRTLAELLPSMKKSGHRVLIFSQWTSMLDILEWTLDVIGVTYRRLDGSTQVTDRQTIVDTFNNDKSIFACLLSTRAGGQGLNLTGADTVIIHDMDFNPQIDRQAEDRCHRIGQTKPVTIFRLVTKSTVDENIYEIAKRKLVLDAAVLESGVHVDDNGDTPEKTMGEILASLLMG
Protein: Large ribosomal subunit protein bL35m (39S ribosomal protein L35, mitochondrial) (L35mt) (MRP-L35) (Q9CQL6)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL15m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein mL45
- Large ribosomal subunit protein uL30m
- Acyl carrier protein, mitochondrial
- Large ribosomal subunit protein bL32m
Sequence:
MAASIFTGAVRAASGIFRPLNVLASSTYRNCARNACLNSSLCTIHFRHIQTSVVSSAPRLVTSVGHLAYGHTTTVLNRVATLVPSVLKPPVRALTYCSTRKGKRKTVKSVVHRFLRLHSGLWLRRKAGYKKKLWKKSTARKKRLREFVFCSKTQSKLLDKMTTSFWKRRNWYAGDPYQMYHDRTNLRV
Protein: Maf1 regulator (Q57YV3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MEFVPLESFEFLNSLLQGVEAQGCLMTVRLEAFTCRCTRKKKLLAASIAEYANKTTPPLRPLCSANAPVPPLLNLSDDSVHVVPTEPVEPSDIDDRLVFLVAALNSIYGEDGYDFSVLTEEDFVPCDEAHVRAEVNNTLRSFPSSCGPAVGQFWVRVTEHASDASQGCEYFRFASPSCDPMASRALFSQHYFLYNKRTRLLVSLLIFAEGNLYRGDDGTMIENSLYYETDDNSNHQRPWLSSPDGASEDDEQVLVGKNVHYYYRP
Protein: Proteolipid protein 2 (Differentiation-dependent protein A4) (Intestinal membrane A4 protein) (Q04941)
Organism: Homo sapiens (Human)
Function: May play a role in cell differentiation in the intestinal epithelium.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Myelin proteolipid protein
- Phosducin-like protein 2
- Phosducin-like protein 3
- Beclin-1
- Interferon regulatory factor 3
Sequence:
MADSERLSAPGCWAACTNFSRTRKGILLFAEIILCLVILICFSASTPGYSSLSVIEMILAAIFFVVYMCDLHTKIPFINWPWSDFFRTLIAAILYLITSIVVLVERGNHSKIVAGVLGLIATCLFGYDAYVTFPVRQPRHTAAPTDPADGPV
Protein: Divergent paired-related homeobox (A6NFQ7)
Organism: Homo sapiens (Human)
Function: Transcription factor that acts as repressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Paired-like homeodomain transcription factor LEUTX
- Tetra-peptide repeat homeobox protein 1
- Double homeobox protein B
- NANOG neighbor homeobox
Sequence:
MPGSEDLRKGKDQMHSHRKRTMFTKKQLEDLNILFNENPYPNPSLQKEMASKIDIHPTVLQVWFKNHRAKLKKAKCKHIHQKQETPQPPIPEGGVSTSVGLRNADTLPRLPNAAHPIGLVYTGHRVPSFQLILYPNLKVPANDFIGHRIVHFGCCRDPNIYCLYPILESQVCAPSFHSGSPACSSNQSRER
Protein: PX domain-containing protein (D9PTP5)
Organism: Caenorhabditis elegans
Interaction partners:
- PX domain-containing protein
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26
- Sorting nexin-3
- Sorting nexin-27
- Sorting nexin lst-4
- Sorting nexin-17 homolog
- Amphiphysin
- Sorting nexin-13
Sequence:
MLGDGEEVFANPLQEASSDDVTSPPAAAADVEVSLNDDDDVTTTTTNDDTFRTARSTLNDSQNTTVVQEEKKKAEKEESYSSLADNRNHRTEEINIDMNSDEAICVDISDALSEREKVKYTVHTRTRLQEMKPETAVVREHEEFLWLHGTLEDNENYAGFIIPPAPPKPNFDSSREKLQKLGEGEATMTKEEFLKMKHDLEQDYLAQFKKTVAMHEVFLQRIAAHPVFKNDQNFRIFLQYENELSVRGKNKKEQVESFWKRFTQSADEVLLSGQKDVDEFFEKEKNYMVEYNIHIKEAAAKSEKLIAARKNVVASFSKIGDSFERIARGEPNKSLARTFAQGADAMFKLKKVESRSSNDEELKLGDTLHYFARDTQAAKDLLYRRMRCLANYEAANKNLERARAKNREIPKAEAEQSEACKKFEEITGLSKNELKELKTRRVQAFKKNLTDLAELEIKHSKAEISLLRDVVERLKSSQ
Protein: N-alpha-acetyltransferase 15, NatA auxiliary subunit a (F1QE25)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- N-alpha-acetyltransferase 50
- N-terminal amino-acid N
- Huntingtin-interacting protein K
- Small integral membrane protein 13
- N
- N-alpha-acetyltransferase 60
- Cysteine-rich protein 2-binding protein
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
Sequence:
MPSITLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNSKFAEHGETLAMKGLTLNCLGRKEEAYDLVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKIVEEFRKTQQTSPDKVDYEYSELLLYQNQLLREAELFKEALDHLTSYEKQICDKLAVEETRGELLLKLDRAGEATEVYHRLLERNPENWSYYQGLEKALKPKSAEDKQKIYEDAWVKYPKGLVPRRLPLSFLTGEKFRECLDRYLRMNFSKGCPPVFTTLKSLYHHKDKVAIIEELVVGYDKSLKTCKMFNQNDDGKIEPPTTLLWVQYFLAQHFNHIGKHTVALEYINTAIESTPTLIELFLIKAKIYKHAGNIREAARWMDEAQALDTADRFINSKCAKYLLKAGLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECALAYKSLNKYGEALKKCHEIERHFVEITDDQFDFHTYCMRKMTLRSYVDLLNLEDVLRMHPFYFKAARTAIEIYLSLHDNPLSDDNKESQADNANLTDKELKKLRNKQRRAQKKAQLEEEKKNAEKEKQLKNQKKKKEEDEEEIGGPKEELIPEKLAKIENPLEEAVKFLTPLKNLVKNKIETHLLAFEIYLRKEKYLLMLQSVKRAYSLDPDHPWLHQCLVRFFKGVSDSKDMPEAVQTVLKQEITKLFGESDPKTFNKNFLSKHANSIPHRVAAAKMMVFLDSSSEGKAAELATSLNESLTDRSLQTCAEVLQALRDGSLGSQQEKFTESYRVSCHGLYPYAVAFMPPGYQDNTAVTTNGDLSPCDHEDLPNEM
Protein: Uncharacterized protein Rv2597 (P9WL73)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv2598
- UPF0719 transmembrane protein Rv2600
- Polyamine aminopropyltransferase
- Uncharacterized protein Rv2599
- Secreted protein
Sequence:
MGNLLVVIAVALFIAAIVVLVVAIRRPKTPATPGGRRDPLAFDAMPQFGPRQLGPGAIVSHGGIDYVVRGSVTFREGPFVWWEHLLEGGDTPTWLSVQEDDGRLELAMWVKRTDLGLQPGGQHVIDGVTFQETERGHAGYTTEGTTGLPAGGEMDYVDCASAGQGADESMLLSFERWAPDMGWEIATGKSVLAGELTVYPAPPVSA
Protein: Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Q63621)
Organism: Rattus norvegicus (Rat)
Function: Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity). Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33 signaling system (By similarity). Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD (By similarity). May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-33
- Interleukin-1 receptor-like 1
- Receptor-type tyrosine-protein phosphatase delta
- Interleukin-1 receptor type 1
- Interleukin-1 beta
- Interleukin-1 receptor type 2
- Interleukin-1 alpha
- Interleukin-1 receptor-like 2
- Interleukin-1 receptor-associated kinase 4
- TNF receptor-associated factor 6
Sequence:
MGLPWCLMSLFFCGILQSHASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMRLPVHRLYIEQGIHNITCPNVDGYFPSSVKPSVTWYKGCTEIVNFHNVQPKGMNLSFFIPLVSNNGNYTCVVTYLENGRLFHLTRTMTVKVVGSPKDAVPPHIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEIWWTIDGKKPDDVPVDITIIESVSYSSTEDETRTQILSIKKVTPEDLKRNYVCHARNAEGEAEQAAKVKQKVIPPRYTVELACGFGATVFLVVVLIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLTLRGVLENEFGYKLCIFDRDSFPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKDLKVKELKRAKSVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSSDKQGLSYSSLKNV
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (Q9VXY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha
- Dihydrolipoyl dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Probable 2-oxoadipate dehydrogenase complex component E1 homolog
- Acetyl-coenzyme A synthetase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Acyl-CoA synthetase short-chain family member 3, mitochondrial
Sequence:
MATHLLRNGATCWLLRNCISQRAALRRCLHVTSSLDKTVSFNLSDIGEGIREVTVKEWFVKEGDTVEQFDNLCEVQSDKASVTITSRYDGKITKIHHKIDEIALVGKPLLDFDVVNEDEDEPEDSSSSSSSTSSDSSASENEEKQSAEASATPTEGRVIIPATPSVRRLAKEHQLDLAKVPATGKNGRVLKGDILEFLGQVPPGTNVPHPTLLAKTPSAAPSGAASVSVPADRVEVLKGVRKAMLKSMTESLKIPHFAYSDEIDMTQLMQFRNQLQLVAKENGVPKLTFMPFCIKAASIALSKYPIVNSSLDLASESLVFKGAHNISVAIDTPQGLVVPNIKNCQTKTIIEIAKDLNALVERGRTGSLSPADFADGTFSLSNIGVIGGTYTHPCIMAPQVAIGAMGRTKAVPRFNDKDEVVKAYVMSVSWSADHRVIDGVTMASFSNVWKQYLENPALFLLH
Protein: Elongator complex protein 4 (hELP4) (PAX6 neighbor gene protein) (Q96EB1)
Organism: Homo sapiens (Human)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:11889558, ECO:0000269|PubMed:22854966}. Nucleus {ECO:0000269|PubMed:11889558}.
Interaction partners:
- Elongator complex protein 5
- Elongator complex protein 1
- Elongator complex protein 3
- Elongator complex protein 6
- Elongator complex protein 2
- DnaJ homolog subfamily C member 24
- Mitochondrial inner membrane protease subunit 1
- Peroxisome biogenesis factor 2
- Doublecortin domain-containing protein 1
- Superkiller complex protein 8
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIERLHLPPDLSDTVSRSSKMDLAESAKRLGPGCGMMAGGKKHLDF
Protein: Kinase (EC 2.7.-.-) (B2RCP4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPAFRAMDVEPRAKGVLLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRKFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGIVDIVDNSDCEPKSKLLRWTTNKKHHVLETEKTPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYTVEKKGNISSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTSRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGSGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLERQESYRFYSSSLLVIYDGKERPEVVLDSDAEDLEDLSEESADESAGAYAYKPIGASSVDVRMIDFAHTTCRLYGEDTVVHEGQDAGYIFGLQSLIDIVTEISEESGE
Protein: Aquaporin-2 (AQP-2) (ADH water channel) (Aquaporin-CD) (AQP-CD) (Collecting duct water channel protein) (WCH-CD) (Water channel protein for renal collecting duct) (P41181)
Organism: Homo sapiens (Human)
Function: Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Plays an essential role in renal water homeostasis.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12194985, ECO:0000269|PubMed:15509592, ECO:0000269|PubMed:7510718}; Multi-pass membrane protein {ECO:0000269|PubMed:24733887}. Basolateral cell membrane {ECO:0000250|UniProtKB:P34080}; Multi-pass membrane protein {ECO:0000269|PubMed:24733887}. Cell membrane {ECO:0000269|PubMed:15509592, ECO:0000269|PubMed:24733887, ECO:0000269|PubMed:7524315, ECO:0000269|PubMed:8140421}; Multi-pass membrane protein {ECO:0000269|PubMed:24733887}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12194985, ECO:0000269|PubMed:15509592}; Multi-pass membrane protein {ECO:0000269|PubMed:24733887}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12194985}; Multi-pass membrane protein {ECO:0000269|PubMed:12194985, ECO:0000269|PubMed:24733887}. Note=Shuttles from vesicles to the apical membrane (PubMed:15509592). Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane (PubMed:15509592). PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated (By similarity). {ECO:0000250|UniProtKB:P34080, ECO:0000269|PubMed:15509592}.
Interaction partners:
- Vasopressin V2 receptor
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Uromodulin
- Vasopressin-neurophysin 2-copeptin
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Putative aquaporin-12A
- Aquaporin-11
- Chloride channel protein ClC-Ka
Sequence:
MWELRSIAFSRAVFAEFLATLLFVFFGLGSALNWPQALPSVLQIAMAFGLGIGTLVQALGHISGAHINPAVTVACLVGCHVSVLRAAFYVAAQLLGAVAGAALLHEITPADIRGDLAVNALSNSTTAGQAVTVELFLTLQLVLCIFASTDERRGENPGTPALSIGFSVALGHLLGIHYTGCSMNPARSLAPAVVTGKFDDHWVFWIGPLVGAILGSLLYNYVLFPPAKSLSERLAVLKGLEPDTDWEEREVRRRQSVELHSPQSLPRGTKA
Protein: Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39) (P54205)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:11859847, ECO:0000269|PubMed:17993516}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:17993516). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000269|PubMed:17993516}.
Interaction partners:
- Ribulose bisphosphate carboxylase small subunit
- Carboxysome assembly protein CcmM
- RuBisCO chaperone RbcX
- Phosphoribulokinase
- Phosphoglycerate kinase
- Slr0458 protein
- Phosphoglycolate phosphatase
- RuBisCO accumulation factor 1
- Slr1762 protein
- Carboxysome assembly protein CcmN
Sequence:
MVQAKAGFKAGVQDYRLTYYTPDYTPKDTDLLACFRMTPQPGVPAEEAAAAVAAESSTGTWTTVWTDNLTDLDRYKGRCYDLEAVPNEDNQYFAFIAYPLDLFEEGSVTNVLTSLVGNVFGFKALRALRLEDIRFPVALIKTFQGPPHGITVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQEAIEKAQAETNEMKGHYLNVTAGTCEEMMKRAEFAKEIGTPIIMHDFFTGGFTANTTLARWCRDNGILLHIHRAMHAVVDRQKNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGERGITMGFVDLMREDYVEEDRSRGIFFTQDYASMPGTMPVASGGIHVWHMPALVEIFGDDSCLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREACRWSPELAAACELWKEIKFEFEAMDTL
Protein: Hemolysin (Q9I710)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- UPF0312 protein PA0423
- DUF5862 domain-containing protein
Sequence:
MAYAEWIAVKVVVSKSIGTVGIRNATLQWGKFYRYTNKDDEISTEEVSSMNVQAGSPQWIASCGRENASSGTQGSFDCYDGNTKMGTFSWDDPWKSGATNTWSFTPASADYAGITSGGNATGTDIGEVTLTLGRFS
Protein: Protein DETOXIFICATION 30 (AtDTX30) (Multidrug and toxic compound extrusion protein 30) (MATE protein 30) (Q9LS19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 42
- Major facilitator superfamily protein
- Major facilitator superfamily protein
- At2g34355
- Sugar transporter ERD6-like 2
Sequence:
MEEDKILTETLLSAAEEPPALPFSSVEDIPPITTVGGFVKEFNVEVKKLWYLAGPAIFMSITQYSLGAATQVFAGHISTIALAAVSVENSVIAGFSFGVMLGMGSALETLCGQAFGAGKLSMLGVYLQRSWVILNVTAVILSLLYIFAAPILAFIGQTPAISSATGIFSIYMIPQIFAYAVNYPTAKFLQSQSKIMVMAAISAVALVLHVLLTWFVIEGLQWGTAGLAVVLNASWWFIVVAQLVYIFSGTCGEAWSGFSWEAFHNLWSFVRLSLASAVMLCLEVWYLMAVILFAGYLKNAEISVAALSICMNILGWTAMIAIGMNAAVSVRVSNELGAKHPRTAKFSLLVAVITSTVIGLAISIALLIFRDKYPSLFVGDEEVIIVVKDLTPILAVSIVINNVQPVLSGVAVGAGWQAVVAYVNIVCYYVFGIPFGLLLGYKLNFGVMGIWCGMLTGTVVQTIVLTWMICRTNWDTEAAMAEGRIREWGGEVSDQLLN
Protein: Protein ViaA (VWA domain protein interacting with AAA ATPase) (P0ADN0)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Regulatory ATPase RavA
- Inducible lysine decarboxylase
- Cell division protein ZapC
- UPF0227 protein YcfP
Sequence:
MLTLDTLNVMLAVSEEGLIEEMIIALLASPQLAVFFEKFPRLKAAITDDVPRWREALRSRLKDARVPPELTEEVMCYQQSQLLSTPQFIVQLPQILDLLHRLNSPWAEQARQLVDANSTITSALHTLFLQRWRLSLIVQATTLNQQLLEEEREQLLSEVQERMTLSGQLEPILADNNTAAGRLWDMSAGQLKRGDYQLIVKYGEFLNEQPELKRLAEQLGRSREAKSIPRNDAQMETFRTMVREPATVPEQVDGLQQSDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGESWREKVIERPVVHKDYDEQPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRIALAENRRCYIMLFSTEIVRYELSGPQGIEQAIRFLSQQFRGGTDLASCFRAIMERLQSREWFDADAVVISDFIAQRLPDDVTSKVKELQRVHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGMRSRLLRRWRR
Protein: Guanine nucleotide-binding protein G(o) subunit alpha (P53359)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear.
Interaction partners:
Sequence:
MGCASSAEERAAPSAQQADREKLKEDGIQAAKDIKLLLLGAGESGKSTIVKQMKIIHESGFTNEDFKQYRPVVYSNTIQSLVAILRAMPTLGITYANKDRESDGKMVFDVIQRMEDTEPFSEELLAAMKRLWADAGVQECFGRSNEYQLNDSAKYFLDDLDRLGARDYQPTEEDILRTRVKTTGIVEVHFSFKNLNFKLFDVGRGQRSERKKWIHCFEDVTAIIFCVAMSEYDQVLHEDETTNRMQESLKLFDSICNNKWFTDTSIILFLNKKDLFEEKIRKSPLTICFPEYTRAYQEYGEAAAYIRSQFEAKNNSTTKEIYCHMTATDTNNNQFVFDAVTDVIIANNLRGCGLY
Protein: Homocysteine S-methyltransferase (EC 2.1.1.10) (S-methylmethionine:homocysteine methyltransferase) (Q47690)
Organism: Escherichia coli (strain K12)
Function: Catalyzes methyl transfer from S-methylmethionine or S-adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine.
Interaction partners:
- Probable S-methylmethionine permease
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine synthase
- Cystathionine gamma-synthase
- Cystathionine beta-lyase MetC
- Methionine synthase
- S-ribosylhomocysteine lyase
- Free methionine-R-sulfoxide reductase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Aromatic-amino-acid aminotransferase
Sequence:
MSQNNPLRALLDKQDILLLDGAMATELEARGCNLADSLWSAKVLVENPELIREVHLDYYRAGAQCAITASYQATPAGFAARGLDEAQSKALIGKSVELARKAREAYLAENPQAGTLLVAGSVGPYGAYLADGSEYRGDYHCSVEAFQAFHRPRVEALLDAGADLLACETLPNFSEIEALAELLTAYPRARAWFSFTLRDSEHLSDGTPLRDVVALLAGYPQVVALGINCIALENTTAALQHLHGLTVLPLVVYPNSGEHYDAVSKTWHHHGEHCAQLADYLPQWQAAGARLIGGCCRTTPADIAALKARS