wanglab/gogpt-training-data huggingface dataset:
Protein: ER membrane protein complex subunit 2 (Tetratricopeptide repeat protein 35) (TPR repeat protein 35) (Q15006)
Organism: Homo sapiens (Human)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22119785}; Peripheral membrane protein {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}; Cytoplasmic side {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:32439656}. Note=May also localize to the nuclear envelope. {ECO:0000250|UniProtKB:Q9CRD2}.
Interaction partners:
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 9
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 8
- ER membrane protein complex subunit 5
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 3
- Derlin-2
Sequence:
MAKVSELYDVTWEEMRDKMRKWREENSRNSEQIVEVGEELINEYASKLGDDIWIIYEQVMIAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTNTAARKRKIAIRKAQGKNVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEELMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIASNPKASAKTKKDNMKYASWAASQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS
Protein: Transcriptional adapter ADA2 (Q75LL6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). The exact mechanism of action is not yet known (By similarity). ADA2 and GCN5 function to acetylate nucleosomes, opening up the promoter region. The ADA2-GCN5 histone acetyltransferase (HAT) module is recruited by WOX11 to regulate crown root cell proliferation and stem cell maintenance of root meristem. The ADA2-GCN5 HAT module together with WOX11 targets and regulates a set of root-specific genes involved in carbon metabolism, cell wall biosynthesis, and auxin transport and response.
Subcellular location: Nucleus {ECO:0000269|PubMed:28487409}.
Interaction partners:
- Histone acetyltransferase GCN5
- Os09g0431500 protein
- ubiquitinyl hydrolase 1
- Transcription and mRNA export factor ENY2
- Os01g0510800 protein
- Expressed protein
- Transcription initiation factor TFIID subunit 9
- Os07g0612500 protein.
- Os07g0645100 protein
- Os07g0645200 protein
Sequence:
MGRSRGVPNSGDDETNHRSKRRRVASSGDAPDSLSAACGGAGEGGGKKALYHCNYCNKDISGKIRIKCSKCPDFDLCVECFSVGAEVTPHRSNHPYRVMDNLSFPLICPDWNADEEILLLEGIEMYGLGNWAEVAEHVGTKTKAQCIDHYTTAYMNSPCYPLPDMSHVNGKNRKELLAMAKVQGESKKVLPGDLTPKDESPFSPPRVKVEDALGEGLAGRSPSHIAGGANKKASNVGQFKDGANVAKVEDGHVDRSIGVKKPRYSADEGPSLTELSGYNSKRHEFDPEYDNDAEQALAEMEFKETDSETDRELKLRVLRIYLSRLDERKRRKEFILERNLLFPNPLEKDLTNEDKEVYHRYKVFMRFLSKEEHEALVRSVLEERKIRRRIQELQECRSAGCRTLAEAKIHIEQKRKKEHEVNAQKAKESGQLLSNTKVVHKTNRPMKIESDGNLDQKKGGASLDSTGRDSPKTTGHAGTKHWDDWDIVGFPGAELLSTSEKNLCCQNRLLPNHYLKMQEVLMQEIFKGSVAKKEDAHVLFKVDPAKVDNVYDMVTKKLGTNEEAPTV
Protein: DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.38) (APOBEC-related cytidine deaminase) (APOBEC-related protein) (ARCD) (APOBEC-related protein 9) (ARP-9) (CEM-15) (CEM15) (Deoxycytidine deaminase) (A3G) (Q9HC16)
Organism: Homo sapiens (Human)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against Vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12808466, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21659520, ECO:0000269|PubMed:21835787}. Nucleus {ECO:0000269|PubMed:18667511}. Cytoplasm, P-body {ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:22915799}. Note=Mainly cytoplasmic (PubMed:16527742, PubMed:16699599, PubMed:21835787). Small amount are found in the nucleus (PubMed:18667511). During HIV-1 infection, virion-encapsidated in absence of HIV-1 Vif (PubMed:12859895). {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21835787}.
Interaction partners:
- Cullin-5
- Core-binding factor subunit beta
- Cytidine deaminase
- Bone marrow stromal antigen 2
- Elongin-B
- DNA dC->dU-editing enzyme APOBEC-3F
- Tripartite motif-containing protein 5
- Protein deacetylase HDAC6
- Elongin-C
- RING-box protein 2
Sequence:
MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN
Protein: Zgc:55492 (Q7ZVY8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGKDYYSVLGIQKGASDDEIKKAYRKQALKYHPDKNKSAGAEEKFKEIAEAYDVLSDPKKKDIYDRFGEEGLKGGAPGGGGGGGNYTYTFQGDPHAMFSEFFGGRNPFEHIFGHNGGMDENMETDDLFASFGMGGIGGFPRSFTTHSHGGRMERKQDPAVIHDLRVSLDEVFTGCTKKMKISRKRLNPDGRTTRSEDKILTVEVKKGWKEGTKITFPREGDETPSNIPADVVFVLKDKPHPVYKRDGSDIIYPAKITLKEALCGCVINVPTLDGRTVKVTSQDIVRPGMKRRLTGEGLPLPKSPDRRGDLVVEYEVRFPEKLSQNAKDTIANVLPAS
Protein: T-cell leukemia homeobox protein 1 (Homeobox protein Hox-11) (Proto-oncogene TCL-3) (T-cell leukemia/lymphoma protein 3) (P31314)
Organism: Homo sapiens (Human)
Function: Controls the genesis of the spleen. Binds to the DNA sequence 5'-GGCGGTAAGTGG-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Paired box protein Pax-2
- Protein phosphatase EYA1
- T-cell acute lymphocytic leukemia protein 1
- Nuclear pore complex protein Nup214
- PHD finger protein 6
- Rhombotin-1
- Protein lyl-1
- Rhombotin-2
- Tyrosine-protein kinase ABL1
- Transcription factor 21
Sequence:
MEHLGPHHLHPGHAEPISFGIDQILNSPDQGGCMGPASRLQDGEYGLGCLVGGAYTYGGGGSAAATGAGGAGAYGTGGPGGPGGPAGGGGACSMGPLTGSYNVNMALAGGPGPGGGGGSSGGAGALSAAGVIRVPAHRPLAGAVAHPQPLATGLPTVPSVPAMPGVNNLTGLTFPWMESNRRYTKDRFTGHPYQNRTPPKKKKPRTSFTRLQICELEKRFHRQKYLASAERAALAKALKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQANRILLQLQQEAFQKSLAQPLPADPLCVHNSSLFALQNLQPWSDDSTKITSVTSVASACE
Protein: Protein SMY2 (Suppressor of MYO2-66 protein) (P32909)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Suppressor of the MYO2 gene.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATP-dependent RNA helicase DHH1
- Protein EAP1
- Protein SCP160
- Branchpoint-bridging protein
- Splicing factor MUD2
- E3 ubiquitin-protein ligase HEL2
Sequence:
MIAPDSQRLFGSFDEQFKDLKLDSVDTENNNTHGVSTILDSSPASVNNNTNGAVAASVNTVPGSTFRSNTPLLGGRHPLSRTSSLIDSIGIQRAASPFSSMKEPFIPQSSGVMSSSFWHGDHPESRVSTPVQQHPLLQRNESSSSFSYAANLGVNLSTHSLAVDITPLSTPTAAQSHVNLFPSSDIPPNMSMNGMSQLPAPVSVESSWRYIDTQGQIHGPFTTQMMSQWYIGGYFASTLQISRLGSTPETLGINDIFITLGELMTKLEKYDTDPFTTFDKLHVQTTSSDSINLNLAPYASGVAATGTIKATENDIFKPLTHDNIWDMDGGTTSKGVDIKLASATTISQTDESHKQEYKSTTMLEKGKKEKSESVAKALLDEQEKRNRELKRKEEARLSKKQKQKEDDLLKKQKEQKEQKEKEALEAEKQKKSEKTKKDTQTQTEGFKTSKDLPSLNSSSANPAPWASKVKVNNAIETSIKNGVSSTGKKKGEPLGLQQRNSKEEKQKEELKSVLNWANKSSLPSNQTIDIKSQFQKSPKGMKESSPLKELEDPNFIEEQKKLWEKVQSSSKQVKSTSSASTTTSSWTTVTSKGKAPIGTVVSPYSKTNTSLNSSLTAKTSTTSTTTTFASMNNVSPRQEFIKWCKSQMKLNSGITNNNVLELLLSLPTGPESKELIQETIYANSDVMDGRRFATEFIKRRVACEKQGDDPLSWNEALALSGNDDDGWEFQVVSKKKGRKH
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase 25 kDa subunit) (SPase 25 kDa subunit) (Q9VYY2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q28250}.
Interaction partners:
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit SEC11
- Uncharacterized protein
- Translocon-associated protein subunit gamma
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- RE14391p
- Endoplasmic reticulum chaperone BiP
- DSec61alpha
Sequence:
MGKKDEKSQQGEELVKVNKWDGSAVKHALDDAVKTCLLGDRPQLKEQFGLVNTRLALCALAVSVAIMAHAWDFTHPFPESRPVLLFSVLAYFALLGILTLHSSFREKGTFAVALQKDKERERLWEASSDMRKYDDKYLLTLSVRDTKNGKRREQSSNKSCAAFIDQNGIVLDNLVANEVNRLFNALAADKKNASSLSSN
Protein: NADP-dependent 3-hydroxy acid dehydrogenase YdfG (L-allo-threonine dehydrogenase) (EC 1.1.1.381) (Malonic semialdehyde reductase) (EC 1.1.1.298) (P39831)
Organism: Escherichia coli (strain K12)
Function: NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
Interaction partners:
- Probable malonic semialdehyde reductase RutE
- Putative carbamate hydrolase RutD
- Enterobactin synthase component F
- Low specificity L-threonine aldolase
- 2-amino-3-ketobutyrate coenzyme A ligase
- L-threonine 3-dehydrogenase
- UPF0381 protein YfcZ
- Ureidoacrylate amidohydrolase RutB
- 3-aminoacrylate deaminase RutC
- Thiol peroxidase
Sequence:
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWCNIDILVNNAGLALGMEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ
Protein: Ribosome biogenesis protein RLP24 (Ribosomal protein L24-like) (Q07915)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of NOG1 to pre-60S ribosomal particles. Activates and recruits ATPase AFG2 to cytoplasmic pre-60S ribosomal particles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12808088}. Nucleus {ECO:0000269|PubMed:12808088}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:12808088}.
Interaction partners:
- Ribosome assembly factor MRT4
- Large ribosomal subunit protein uL29A
- Ribosome biogenesis protein ERB1
- Probable metalloprotease ARX1
- Ribosome biogenesis protein NSA2
- Ribosome biogenesis protein NSA1
- Ribosome biogenesis protein YTM1
- Nucleolar GTP-binding protein 1
- 27S pre-rRNA
- 60S ribosome subunit biogenesis protein NIP7
Sequence:
MRIYQCHFCSSPCYPGHGIMFVRNDAKEFRFCRSKCHKAFKQRRNPRKLKWTKAFRKAAGKELAVDSTLTFAQRRNVPVRYNRELVATTLKAMARIEEIRQKRERAFYKNRMRGNKEKDFLRDKKLVESNPELLRIREVEIARKLAKEQERAESVSEQEESEEEEEDMEIDSDEEEEEQLEKQKILLKNRRRNTKKIAF
Protein: methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (Q385A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 3-methylcrotonyl-CoA carboxylase, putative
- Biotin--acetyl-CoA-carboxylase ligase, putative
- Isovaleryl-coA dehydrogenase, putative
- Probable enoyl-CoA hydratase, mitochondrial
- Methylglutaconyl-CoA hydratase, mitochondrial, putative
- hydroxymethylglutaryl-CoA lyase
- Citrate synthase
Sequence:
MKSFCRLGKVCGCSVSVVFSHRVFALGPRRDYSTSEVPLGSSQVPKGDPRKEQKGGNMSEVYLFHPAQYESAPATTRPNVLHYPAESTNPEFKANTERMKALTAELRRRVQVIVDGDSEADKRARDRHISRGKLLVHQRIEKLVDPMSPFLELSQLAGGDLYPGEACHRGGILTGIGVVHGMRVMIVANDATVKGGTYYPITVKKHLRAQRIAEENRLPCIYLVDSGGANLGMQGDVFPDEQHFGRIFFNQANMSAKGIAQIATVMGSCTAGGAYVPAMSDESIIVKGNGTIFLGGPPLVFAATGEEVTPEELGGADVHCRASGVTDYFATDDLHALYLTRRIVANLNRNDCERPCRGREFTPPLYDPSEIGGFIPDMGADVVKGFDVRAVIARLVDGSEFDEFKKLYGDTLVCGFARFEGMLVGIVANNGILYSESALKGAHFVELCSHRNIPLLFLQNITGFMVGKTYEEGGIAKNGAKLVTAVSTTHVPKITIIIGGSYGAGNYGMCGRAFGPRFLFMWPNARISVMGGNQAATVLALTNSKLRENEVQDFKAKVRSKYEYEGSCYYSTARLWDDGVIAPEDTRAVVVQALLSTLSAPCGETKFGVFRM
Protein: Elongation factor G, mitochondrial (EF-Gmt) (EC 3.6.5.-) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (Q8K0D5)
Organism: Mus musculus (Mouse)
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis.
Subcellular location: Mitochondrion.
Interaction partners:
- Ubiquitin-like protein FUBI
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS7m
- Ribosome-recycling factor, mitochondrial
- Small ribosomal subunit protein bS16m
- Elongation factor Tu, mitochondrial
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS17
Sequence:
MRLLRVAAALGRGPFPRVPAVLGWQGKQADWKTRRWCSSGPVPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIATMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWKDININIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVSRQMKRYNVPFLTFINKLDRMGSNPSRALQQMRSKLNHNAAFVQIPIGLEGDFKGIIDLIEERAIYFDGDFGQIVRYDEIPAGLRAAAADHRQELIECVANSDEQLGELFLEEKIPSVSDLKRAIRRATLSRSFTPVFLGSALKNKGVQPLLDAVLEYLPNPSEVQNYAILNQNDSKEKTKILMNPQRDDSHPFVGLAFKLEAGRFGQLTYVRNYQGELKKGSTIYNTRTGKKVRVQRLVRMHADMMEDVEEVYAGDICALFGIDCASGDTFTNKDNSDLSMESIHVPEPVISIAMRPSNKNDLEKFSKGIGRFTREDPTFKVHFDPESKETIVSGMGELHLEIYAQRMEREYGCPCITGKPKVAFRETIVAPVPFDFTHKKQSGGAGQFGKVIGVLEPLPPEDYTKLEFSDETFGSNVPKQFVPAVEKGFLDACEKGPLSGHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALANGTLCIIEPIMSVEVIAPNEFQGTVFAGINRRHGVITGQDGIEDYFTLYADVPLNNMFGYSTELRSCTEGKGEYTMEYCRYQPCSPSTQEELINKYLEATGQLPVKKGKAKN
Protein: L-arabinokinase (AtISA1) (EC 2.7.1.46) (O23461)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Arabinose kinase. Involved in the salvage pathway which converts free L-arabinose to UDP-L-arabinose. May play a role in arabinose transport.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-sugar pyrophosphorylase
- Glucuronokinase 1
- Alpha-L-arabinofuranosidase 1
- Probable glucuronokinase 2
- ADP-glucose phosphorylase
- Thylakoid lumenal P17.1 protein
- Alpha-L-arabinofuranosidase 2
- Mevalonate/galactokinase family protein
- UDP-arabinose 4-epimerase 1
- Aldo-keto reductase family 4 member C10
Sequence:
MSERAKLQKKKKVTEDLLDSLLLLPPWRNFAISQSHQSIIESSSQRLPEKMRIDENEGVSASSKHLVFAYYVTGHGFGHATRVVEVVRHLIAAGHDVHVVTGAPDFVFTSEIQSPRLKIRKVLLDCGAVQADALTVDRLASLEKYVETAVVPRAEILETEVEWLHSIKADFVVSDVVPVACRAAADAGIRSVCVTNFSWDFIYAEYVMAAGYHHRSIVWQIAEDYSHCEFLIRLPGYCPMPAFRDVIDVPLVVRRLHKSRKEVRKELGIAEDVNVVILNFGGQPSGWNLKETSLPTGWLCLVCGASETLELPPNFIKLAKDAYTPDIIAASDCMLGKIGYGTVSEALSYKVPFVFVRRDYFNEEPFLRNMLEFYQCGVEMIRRDLLMGQWTPYLERAVSLKPCYEGGINGGEIAAHILQETAIGRHCASDKLSGARRLRDAIILGYQLQRVPGRDIAIPEWYSRAENELGQSAGSSPTVQANENNSLVESCIDDFDILQGDVQGLSDTCTFLKSLAMLDAIHDSEKSTEKKTVRERKAAGGLFNWEEEIFVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAVQRNLPGKHRLWKHAQARQQAKGQVPTPVLQIVSYGSEISNRAPTFDMDLSDFMDGDEPISYEKARKFFAQDPAQKWAAYVAGTILVLMIELGVRFEDSISLLVSSAVPEGKGVSSSAAVEVASMSAIAAAHGLSIDPRDLAILCQKVENHIVGAPCGVMDQMTSSCGEANKLLAMICQPAEVVGLVEIPNHVRFWGIDSGIRHSVGGADYRSVRVGAYMGRKMIKSMASSILSPSASSANGGNPEELEDEGIDLLEAEASLDYLCNLSPHRYEARYADKLPDIMLGQTFIEEYADHDDPVTVIDQKRSYSVKAPARHPIYENFRVKTFKALLTSATSDEQLTALGGLLYQCHYSYSACGLGSDGTNRLVQLVQGMQHNKSNSEDGTLYGAKITGGGSGGTVCVVGRNSLRSSQQILEIQQRYKAATGYLPLIFEGSSPGAGKFGYLRIRRRISL
Protein: Mitochondrial import inner membrane translocase subunit Tim21 (TIM21-like protein, mitochondrial) (Q9BVV7)
Organism: Homo sapiens (Human)
Function: Participates in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Also required for assembly of mitochondrial respiratory chain complex I and complex IV as component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex. Probably shuttles between the presequence translocase and respiratory-chain assembly intermediates in a process that promotes incorporation of early nuclear-encoded subunits into these complexes.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit Tim17-A
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit Tim17-B
- Mitochondrial import inner membrane translocase subunit TIM16
- Reactive oxygen species modulator 1
Sequence:
MICTFLRAVQYTEKLHRSSAKRLLLPYIVLNKACLKTEPSLRCGLQYQKKTLRPRCILGVTQKTIWTQGPSPRKAKEDGSKQVSVHRSQRGGTAVPTSQKVKEAGRDFTYLIVVLFGISITGGLFYTIFKELFSSSSPSKIYGRALEKCRSHPEVIGVFGESVKGYGEVTRRGRRQHVRFTEYVKDGLKHTCVKFYIEGSEPGKQGTVYAQVKENPGSGEYDFRYIFVEIESYPRRTIIIEDNRSQDD
Protein: Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52) (Q9H6E5)
Organism: Homo sapiens (Human)
Function: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16790842}. Nucleus speckle {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:18305108}.
Interaction partners:
- Poly
- Poly
- Poly
- Spliceosome associated factor 3, U4/U6 recycling protein
- Protein lin-28 homolog A
- U4/U6 small nuclear ribonucleoprotein Prp4
- U4/U6 small nuclear ribonucleoprotein Prp31
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- DIS3-like exonuclease 2
- Centrosomal AT-AC splicing factor
Sequence:
MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDLGKASELAETPKEEKAEGAAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASRLEPSINVEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGGLPSNLWEGLRLGPLNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPLAPFTQLTAALVQVFREALGCHIEQATKRTRSEGGGTGESSQGGTSKRLKVDGQKNCCEEGKEEQQGCAGDGGEDRVEEMVIEVGEMVQDWAMQSPGQPGDLPLTTGKHGAPGEEGQPSHAALAERGPKGHEAAQEWSQGEAGKGASLPSSASWRCALWHRVWQGRRRARRRLQQQTKEGAGGGAGTRAGWLATEAQVTQELKGLSGGEERPETEPLLSFVASVSPADRMLTVTPLQDPQGLFPDLHHFLQVFLPQAIRHLK
Protein: Ras/Rap GTPase-activating protein SynGAP (Q3TPW3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELSPSSGGAAEALSWPEMFTGLESDSPLPPEDLDAVVPVSGAVAGGMLDRILLESVCQQQSWVRVFDVKGPPTHRLSCGQSPYTETTSWERKYCILTDSQLVLLNKEKEMPVEGQDQQTDSTKGRCLRRTVSVPSEGQFPEYPQEGTTKLGKPKKGKTSLRFIG
Protein: Thrombopoietin (C-mpl ligand) (ML) (Megakaryocyte colony-stimulating factor) (Megakaryocyte growth and development factor) (MGDF) (Myeloproliferative leukemia virus oncogene ligand) (P40225)
Organism: Homo sapiens (Human)
Function: Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.
Subcellular location: Secreted {ECO:0000269|PubMed:32150607, ECO:0000269|PubMed:7822271}.
Interaction partners:
- Thrombopoietin receptor
- Erythropoietin
- Granulocyte colony-stimulating factor
- Kit ligand
- Interleukin-3
- Erythropoietin receptor
- Fms-related tyrosine kinase 3 ligand
- Leptin
- Prolactin
- Tyrosine-protein kinase JAK2
Sequence:
MELTELLLVVMLLLTARLTLSSPAPPACDLRVLSKLLRDSHVLHSRLSQCPEVHPLPTPVLLPAVDFSLGEWKTQMEETKAQDILGAVTLLLEGVMAARGQLGPTCLSSLLGQLSGQVRLLLGALQSLLGTQLPPQGRTTAHKDPNAIFLSFQHLLRGKVRFLMLVGGSTLCVRRAPPTTAVPSRTSLVLTLNELPNRTSGLLETNFTASARTTGSGLLKWQQGFRAKIPGLLNQTSRSLDQIPGYLNRIHELLNGTRGLFPGPSRRTLGAPDISSGTSDTGSLPPNLQPGYSPSPTHPPTGQYTLFPLPPTLPTPVVQLHPLLPDPSAPTPTPTSPLLNTSYTHSQNLSQEG