wanglab/gogpt-training-data huggingface dataset:
Protein: Serine hydroxymethyltransferase, mitochondrial (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Serine methylase) (P34897)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis. Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism: thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA. Also required for mitochondrial translation by producing 5,10-methylenetetrahydrofolate; 5,10-methylenetetrahydrofolate providing methyl donors to produce the taurinomethyluridine base at the wobble position of some mitochondrial tRNAs. Associates with mitochondrial DNA. In addition to its role in mitochondria, also plays a role in the deubiquitination of target proteins as component of the BRISC complex: required for IFNAR1 deubiquitination by the BRISC complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21876188, ECO:0000269|PubMed:24075985}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18063578}. Mitochondrion inner membrane {ECO:0000269|PubMed:21876188}. Cytoplasm {ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:24075985}. Note=Mainly localizes in the mitochondrion. Also found in the cytoplasm and nucleus as part of the BRISC complex (PubMed:24075985). {ECO:0000269|PubMed:24075985}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- BRISC complex subunit Abraxas 2
- Lys-63-specific deubiquitinase BRCC36
- BRISC and BRCA1-A complex member 2
- Glycine dehydrogenase
- Thymidylate synthase
- BRISC and BRCA1-A complex member 1
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Phosphoserine phosphatase
Sequence:
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
Protein: Homeobox protein MOX-1 (Mesenchyme homeobox 1) (P50221)
Organism: Homo sapiens (Human)
Function: Mesodermal transcription factor that plays a key role in somitogenesis and is specifically required for sclerotome development. Required for maintenance of the sclerotome polarity and formation of the cranio-cervical joints. Binds specifically to the promoter of target genes and regulates their expression. Activates expression of NKX3-2 in the sclerotome. Activates expression of CDKN1A and CDKN2A in endothelial cells, acting as a regulator of vascular cell proliferation. While it activates CDKN1A in a DNA-dependent manner, it activates CDKN2A in a DNA-independent manner. Required for hematopoietic stem cell (HSCs) induction via its role in somitogenesis: specification of HSCs occurs via the deployment of a specific endothelial precursor population, which arises within a sub-compartment of the somite named endotome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P32442}. Cytoplasm {ECO:0000250|UniProtKB:P32442}. Note=Localizes predominantly in the nucleus. {ECO:0000250|UniProtKB:P32442}.
Interaction partners:
- Paired box protein Pax-1
- Homeobox protein MOX-2
- Keratin, type I cytoskeletal 24
- Sclerostin
- T-box transcription factor TBX6
- Protein phosphatase EYA2
- Homeobox protein SIX1
Sequence:
MDPAASSCMRSLQPPAPVWGCLRNPHSEGNGASGLPHYPPTPFSFHQKPDFLATATAAYPDFSASCLAATPHSLPQEEHIFTEQHPAFPQSPNWHFPVSDARRRPNSGPAGGSKEMGTSSLGLVDTTGGPGDDYGVLGSTANETEKKSSRRRKESSDNQENRGKPEGSSKARKERTAFTKEQLRELEAEFAHHNYLTRLRRYEIAVNLDLSERQVKVWFQNRRMKWKRVKGGQPISPNGQDPEDGDSTASPSSE
Protein: Apoptosis inducing factor mitochondria associated 3 (C9K029)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGCFSKPKPVELKIEVVLPEKERGKEELSASGKGSPRAYQGNGTARHFHTEERLSTPHPYPSPQDCVEAAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSLHKFQVKIEKEKVYVRASKQALQLQRRTKVMAKCISPSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRADVCVVGIVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREVETGDMSWLTGKGS
Protein: Succinate-CoA ligase ADP-forming subunit beta (A0A2R8Y5P6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQ
Protein: Purine-rich element-binding protein gamma (Q8R4E6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MERARRRGGGGSGGGRGRGGKNVGGPGLSKSRLYPQAQHSHYPHYSASATPNQSGGTSEIQELASKRVDIQKKRFYLDVKQSSRGRFLKIAEVWIGRGRQDNIRKSKLTLSLSVAAELKDCLGDFIEHYAHLGLKGHRQEHGQSKEQVSRRRQKHSAPSPPVSVGSEEHPHSVLKTDYIERDNRKYYLDLKENQRGRFLRIRQTMMRGTGMIGYFGHSLGQDQTIVLPAQGMIEFRDALVQLIEDYGEGDIEERRCGDDDPLELPEGTSFRVDNKRFYFDVGSNKYGIFLKVSEVRPPYRNTITVPFKAWTRFGENFIKYEEEMRKICNSHKEKRMDGRRASGEEQECLD
Protein: Mitotic check point protein BUB2 (Cell cycle arrest protein BUB2) (P26448)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the GTP-binding protein TEM1 by the BFA1/BUB2 complex.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole.
Interaction partners:
- Cell division control protein 15
- Protein TEM1
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Tyrosine-protein phosphatase CDC14
- Mitotic check point protein BFA1
- Protein phosphatase PP2A regulatory subunit B
- Mitotic spindle checkpoint component MAD2
- DNA damage-inducible protein 1
- Antagonist of mitotic exit network protein 1
- Guanine nucleotide exchange factor LTE1
Sequence:
MTSIEDLISNPPLLLHSSLSQLRYLILSEGLPISEDKQQQRTRCYVWTVLSQTSMEASTQRYLALLKLGPPSTTIYQKIKNDTSRTFQTDPNFRNRVSEDALIRCLSCFAWQTQQRRQKTRFGRIPVSTYVQGMNVLLAPLLYSCPSEPMAYQLFTKLCYEMIPTYLTKNLNGAQNGAKLLDISLRIIDPKLSKFLSDNLLTAEIYGMPSILTLSSCNKPLDQVIKLWDFMFAYGFHMNILFVVAFLVKMRSKVFKSDSPVNLLRQFPDFDADEIIRLGVGFIAKIPAQIYDLLVDHLTDPDIYIP
Protein: CASP-like protein 1B1 (AtCASPL1B1) (Q9FI10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAVSKLTLAATSGKSCKILLGLRLLAFSATLSAAIVMGLNKETKTFIVGKVGNTPIQATFTAKFDHTPAFVFFVVANAMVSFHNLLMIALQIFGGKMEFTGFRLLSVAILDMLNVTLISAAANAAAFMAEVGKNGNKHARWDKICDRFATYCDHGAGALIAAFAGVILMLIISAASISRLVQPNKCCSTTASPSVVP
Protein: At1g11480/T23J18_15 (Eukaryotic translation initiation factor-like protein) (Q94C21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKKKSAAMTLKDFHGGSIPSDLPLPSAPGVTPKVIPDRPVFDRAPWGNSIGRPDQRARPSSSHAIRNLDDKSLFLPHNVNIGRNFSEDERKPLDGHSAPRRVVSDDVFRFANNRLEMKADSVLAGRHSGWAAGPLTHSGTGNIENSVSGNHSNIWNGRKEVSVANNEPGQSPWTKQPAVSNLVHTSALDQVSSGGWQSKLLVPSQMGFDVVKHSEIDTRVYKTNSPVISQGVEPHGTHVERALIAEDGIQRGKKLSREYEKIPGPTYVDAKEAKIVANTNDKPHPKYSDVKPAGHLVQPTAPSEVVERPKLNLLPRTKPLESVEKPVNDEKLENSASVLIQRENATQKSFNNSKSGLSTDEIPNQPAERPKLNLKPVAQLLEQPEVKTEKDRSAVFGGARPRELVLKERGIDEPEHHKLDQPTDRMVLKPIERVPEHASQRPVSSPRDMRTRKFDQKDGRNVSDIARSETQRRNWRENENKSARQQQQTQEKTRHPSPETWRKPVPQKLDSPNGTGIRHGKAASALELAQAYSPFSDPKSGIGSSNSFNKSRNNQTQQQPFSRLVGSTTTGRQINGY
Protein: IP12864p (Spermitin, isoform C) (Q4V4X9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLHCQVEGAKAEQRECPVMHSENSAETFSSEESQASDCNQPLDVQSPKLTTNIEESFKVDCKLSLNTLLSPINITDPLLMCSISEFNKEEQTMEPYFIQELDMACAGQEVEQVAEENVFETGPQLKLPENQPINDSITTETNETKLPSTEALNVLNLAEFSEPVMEKSNISIEEVNLTGAEEINEPISDEPNSQLVESAAKLQPKSLGIQIPPLQIEDLISPLVEQPKIATKLGVISFLTGNKLALTPSVRLSFGDRVTTRTNKKSKEIVQQQASKALKALISVFTMQRRLEASQCDNSNNSRSKRFEQLKSSLTFSRVFRQNIFQPTSKIESRQQNTDANSLESGEPNFKSTSAYKEPLPIPYRQDAGEGLTCNGLNVSKDSVFSEVSESDVSETHNKLFAMKKTQEGLSSTRSIGELSNILNNGRVLFSQPVRLFCFNKLKEWKRQGEGQIEVIEHHGSYYIVLHDKVSGELIIHMRVDEKWRIDYMTKSSYSCRWTNINYANCRDGTLERIACSFREPSHAAEFVARIRNSALQSRLECSS
Protein: Desiccation-related protein PCC13-62 (P22242)
Organism: Craterostigma plantagineum (Blue gem) (Torenia plantagineum)
Interaction partners:
Sequence:
MAQQPTFASAALVSFFLALICSCSYAAWHHEKDDIPKSDVSLLEFPLNLELLEAEFFAWAAFGKGIDELEPELAKGGPSPIGVQKANLSPFIRDIIAQFAYQEFGHVRAIQSSVEGFPRPLLDLSAKSFATVMDSAFGKTLKPPFDPYANDINYLLACYVVPYVGLTGYVGANPKLESPVSRKLVAGLLAVEAGQDAIIRALLYERATDKVEPYGITVAEFTNKISELRNKLGDKGVKDLGLIVEPELGAEGKISGNVLAGDKNSLAFPRTPERCLGSCTAAAMRPSPAAFIPKAPTGKSPSLIWRIRAFSIV
Protein: Chloride channel 2 isoform 3 (A0A0S2Z364)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAAWFPDGIHTDSSTYRIVPGGYAVVAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQERRATQTSPLSDQEGPPTPEASVCFQVNTEDSAFPAARGETHKPLKPALKRGPSVTRNLGESPTGSAESAGIALRSLFCGSPPPEAASEKLESCEKRKLKRVRISLASDADLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPHSRHGLPREGSPSDSDDKCQ
Protein: Probable conserved Mce associated membrane protein (O07419)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Probable conserved Mce associated membrane protein
- Probable conserved Mce associated transmembrane protein
- Mce-family protein Mce1F
- Conserved integral membrane protein YrbE1B
- Probable conserved Mce associated protein
- Secreted protein
- Mce-family protein Mce1B
- Mce-family protein Mce1C
- Mce-family protein Mce1A
- Conserved integral membrane protein YrbE1A
Sequence:
MKAADSAESDAGADQTGPQVKAADSAESDAGELGEDACPEQALVERRPSRLRRGWLVGIAATLLALAGGLGAAGYFALRSHQESQSIAREDLAAIEAAKDCVAATQAPDAGAMSASMQKIIECGTGDFGAQASLYTSMLVEAYQAASVHVQVTDMRAAVERNNNDGSVDVLVALRVKVSNTDSDAHEVGYRLRVRMALDEGRYKIAKLDQVTK
Protein: C-terminal-binding protein 2 (CtBP2) (P56546)
Organism: Mus musculus (Mouse)
Function: Corepressor targeting diverse transcription regulators. Isoform 2 probably acts as a scaffold for specialized synapses (By similarity). Functions in brown adipose tissue (BAT) differentiation.
Subcellular location: Nucleus {ECO:0000305}. Synapse {ECO:0000250}.
Interaction partners:
- C-terminal-binding protein 1
- Protein bassoon
- DNA endonuclease RBBP8
- Histone deacetylase 1
- Transcription factor 7
- Histone deacetylase 2
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1
- Krueppel-like factor 3
- Zinc finger protein 217
Sequence:
MALVDKHKVKRQRLDRICEGIRPQIMNGPLHPRPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKEFFVTSAPWSVIDQQAIHPELNGATYRYPPGIVGVAPGGLPPAMEGIIPGGIPVTHNLPTVAHPSQAPSPNQPTKHGDNREHPNEQ
Protein: Intercellular adhesion molecule 4 (ICAM-4) (Landsteiner-Wiener blood group glycoprotein) (LW blood group protein) (CD antigen CD242) (Q14773)
Organism: Homo sapiens (Human)
Function: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM4 is also a ligand for alpha-4/beta-1 and alpha-V integrins.
Subcellular location: [Isoform Long]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Short]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERM2}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Integrin beta-2
- Integrin alpha-L
- Intercellular adhesion molecule 1
- Glycophorin-B
- Intercellular adhesion molecule 2
- E3 ubiquitin-protein transferase MAEA
Sequence:
MGSLFPLSLLFFLAAAYPGVGSALGRRTKRAQSPKGSPLAPSGTSVPFWVRMSPEFVAVQPGKSVQLNCSNSCPQPQNSSLRTPLRQGKTLRGPGWVSYQLLDVRAWSSLAHCLVTCAGKTRWATSRITAYKPPHSVILEPPVLKGRKYTLRCHVTQVFPVGYLVVTLRHGSRVIYSESLERFTGLDLANVTLTYEFAAGPRDFWQPVICHARLNLDGLVVRNSSAPITLMLAWSPAPTALASGSIAALVGILLTVGAAYLCKCLAMKSQA
Protein: Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (P36010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12472466}. Mitochondrion intermembrane space {ECO:0000269|PubMed:12472466, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}. Note=Localizes predominantly to the cytoplasm. A small fraction is present in the mitochondrial intermembrane space.
Interaction partners:
- Thymidylate kinase
- Uridylate kinase
- Inosine triphosphate pyrophosphatase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- CTP synthase 2
- CTP synthase 1
- Mitochondrial import receptor subunit TOM40
- Small ribosomal subunit protein uS10m
- Guanylate kinase
- Small ribosomal subunit protein uS15m
Sequence:
MSSQTERTFIAVKPDGVQRGLVSQILSRFEKKGYKLVAIKLVKADDKLLEQHYAEHVGKPFFPKMVSFMKSGPILATVWEGKDVVRQGRTILGATNPLGSAPGTIRGDFGIDLGRNVCHGSDSVDSAEREINLWFKKEELVDWESNQAKWIYE
Protein: Inactive 2'-5' oligoadenylate synthetase 1C (2',5'-oligoadenylate synthetase-like 5) (Q924S2)
Organism: Mus musculus (Mouse)
Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA.
Interaction partners:
Sequence:
MENGLCSIQARELDEFICDYLFPDTTFLTELRADIDSISAFLKERCFQGAAHPVRVSRVVMGGSYDEHTALKGKSEAKMVLFFNNLTSFEEQLKRRGEFVEEIQKHLCQLQQEKPFKVKFEVQSSEEPNSRSLSFKLSSPELQQEVEFDVQPAYDVLYELRNNTYAEPQFYNKVYAQLIHECTTLEKEGDFSICFTDLHQNFMRYRAPKLWNLIRLVKHWYQLCKEKLREPLPPQYALELLTVYVWEHSNKNQEKVTTAKNFRTFLELVAYYKNLRIYWTWYYDFRHQEVCAYLCRQLKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQTWMQSSCFRNCDMSFVPTWDLSPERQECAFQ
Protein: Interferon regulatory factor 3 (IRF-3) (P70671)
Organism: Mus musculus (Mouse)
Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14653}. Nucleus {ECO:0000250|UniProtKB:Q14653}. Mitochondrion {ECO:0000250|UniProtKB:Q14653}. Note=Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm. Recruited to mitochondria via TOMM70:HSP90AA1 upon Sendai virus infection. {ECO:0000250|UniProtKB:Q14653}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Serine/threonine-protein kinase TBK1
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Interferon regulatory factor 7
- Transcription factor Jun
- Histone acetyltransferase p300
- Ubiquitin-like protein ISG15
- Mitochondrial antiviral-signaling protein
- TIR domain-containing adapter molecule 1
- Z-DNA-binding protein 1
Sequence:
METPKPRILPWLVSQLDLGQLEGVAWLDESRTRFRIPWKHGLRQDAQMADFGIFQAWAEASGAYTPGKDKPDVSTWKRNFRSALNRKEVLRLAADNSKDPYDPHKVYEFVTPGARDFVHLGASPDTNGKSSLPHSQENLPKLFDGLILGPLKDEGSSDLAIVSDPSQQLPSPNVNNFLNPAPQENPLKQLLAEEQWEFEVTAFYRGRQVFQQTLFCPGGLRLVGSTADMTLPWQPVTLPDPEGFLTDKLVKEYVGQVLKGLGNGLALWQAGQCLWAQRLGHSHAFWALGEELLPDSGRGPDGEVHKDKDGAVFDLRPFVADLIAFMEGSGHSPRYTLWFCMGEMWPQDQPWVKRLVMVKVVPTCLKELLEMAREGGASSLKTVDLHISNSQPISLTSDQYKAYLQDLVEDMDFQATGNI
Protein: Thioredoxin M4, chloroplastic (AtTrxm4) (Q9SEU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase involved in the redox regulation of enzyme of the oxidative pentose phosphate pathway. Under reducing conditions, inhibits the glucose-6-phosphate dehydrogenase.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
Interaction partners:
- Thioredoxin F1, chloroplastic
- Thioredoxin F2, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Peroxiredoxin Q, chloroplastic
- Thioredoxin-like protein CDSP32, chloroplastic
- Rhodanese-like domain-containing protein 14, chloroplastic
- Peroxiredoxin-2E, chloroplastic
- Malate dehydrogenase, chloroplastic
- Protein PROTON GRADIENT REGULATION 5
Sequence:
MASLLDSVTVTRVFSLPIAASVSSSSAAPSVSRRRISPARFLEFRGLKSSRSLVTQSASLGANRRTRIARGGRIACEAQDTTAAAVEVPNLSDSEWQTKVLESDVPVLVEFWAPWCGPCRMIHPIVDQLAKDFAGKFKFYKINTDESPNTANRYGIRSVPTVIIFKGGEKKDSIIGAVPRETLEKTIERFLVE
Protein: FERM domain-containing protein A (Q54EW0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Key regulator of adhesion dynamics, it acts as an anti-adhesive. Plays a critical role in the regulation of cell-cell adhesion, multi-cellular development and, in particular, the formation of the organising center known as the tip. Required for turnover of paxillin-adhesion sites during cell migration. Plays a major role in normal cell shape, cell-substrate adhesion and actin cytoskeleton organization.
Interaction partners:
- FERM domain-containing protein B
Sequence:
MAVLSLVELCFISIMERMEYNNQALQKIPPQLIERLINFMVYKLPPNHLSLQTISKPIRIKLVRQNRVITMRFSIYNTIDKIIHQIYERIINEEKMEQNEKQKNSSNNNLLSLLTLNNNNQNNNSSIITTTTTTTNNNNNSNCGSSSSSSSSKQILWGSIENYGLFQQSGSFRNARWLQLDKTLAYYEIDSNETLEFKTCKSVLKIRFFGPWERVVHPLHQSTMLDETIKTFVFDESKTVSEISMELAKKLQLKYPEELSLKVQCEEEDDGRGIWLSADLTLPEQGIDPLYTIFLLKRQFFFCKDIIIDFSMDAEMLHFVFCQCLDAIIDTSHPCSPTESILFAALQCQICFGDYVHGSKEIDQIRQRDFLPMEFINQKNILKEILIQYQRLIGMSEQKAKLNYIQLAKSLKTYGYTFFKVTNRQTSIVNNNLSSSGGSGNGSGSGNGSSSSSSNSSSGNNNNHNHHNHQQLFGISSEAVLTLDPMTNNTISLYSLSNIRKWHVLNNVFTIEYNDRKDTFISMEAEAISHVLSSYIHHNLRETPSIQKQWDQNYLSVSGRNSLTNGRKRLSTCSNCSSDSMEFDSSKSNTKDKDWKYQYGLVIKKCALYIEPKKLYINPLSTQITGSMVNKELNKDTKVTKVLKVLTDLSSKMILSFSKSSPAKEREIVVKFSDKKVKSFVVDEQKTVSEITQEIGLKLGIKNPEEFSLQLIVNNKNNNNNNNSNNSSTSSSSSSSVNNSGIFDGLNNSNVNNVFYNSYIVNSSISNNSNSNSNSNILNNSNDEQSTSTSTSSSLGGIWLKPYQPLSEQSISPDSKLLFKKKFYTSDIGAADDCNSDPVYFNLLFFQSKDAIISNTYTCSKEEAIQLAATLFQINFGDHNPNIHKPGFLKSQDLKFFLPPNSLELWGLSFQKIEKSIYKEHQNLRGIKEVYAKYRYVQLCRSLKTFGAIFFSVRQLLPNKTNGSSSSSSNNNGGNSNNGINGNGIITGGNGGSGGGGSGIGGNGSGINTGGNGFGGSQQIPINQPLVLGFSRKCILFMTAKTKKFLVEYPLTHLRRWAYHKDTQCLTLDFGDYEMGRIVLQTTESEEISSYLSDYIDYIQTKLVGSQSFSRSIFNSDNNSSSFFSNSFCNNTTTTTTTTTTTTTTTTTTTTNNV
Protein: Microtubule nucleation factor SSNA1 (Nuclear autoantigen of 14 kDa) (Sjoegren syndrome nuclear autoantigen 1) (O43805)
Organism: Homo sapiens (Human)
Function: Microtubule-binding protein which stabilizes dynamic microtubules by slowing growth and shrinkage at both plus and minus ends and serves as a sensor of microtubule damage, protecting microtubules from the microtubule-severing enzyme SPAST. Induces microtubule branching which is mediated by the formation of long SSNA1 fibrils which guide microtubule protofilaments to split apart from the mother microtubule and form daughter microtubules (By similarity). Plays a role in axon outgrowth and branching. Required for cell division.
Subcellular location: Nucleus {ECO:0000269|PubMed:9430706}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12640030, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25390646}. Midbody {ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:12640030}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12640030}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JJ94}. Note=In sperm, strongly expressed in the basal body region with weaker expression in the axoneme (PubMed:12640030). Localizes to axon branching points in neurons (By similarity). {ECO:0000250|UniProtKB:Q9JJ94, ECO:0000269|PubMed:12640030}.
Interaction partners:
- Spastin
- Atlastin-2
- Atlastin-3
- Serine/threonine-protein kinase PLK1
- Charged multivesicular body protein 1b
- Centlein
- 26S proteasome regulatory subunit 8
- Atlastin-1
- Tubulin gamma-1 chain
Sequence:
MTQQGAALQNYNNELVKCIEELCQKREELCRQIQEEEDEKQRLQNEVRQLTEKLARVNENLARKIASRNEFDRTIAETEAAYLKILESSQTLLSVLKREAGNLTKATAPDQKSSGGRDS
Protein: Immunoglobulin superfamily containing leucine-rich repeat protein (Q6GU68)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRALCLLCWAVLLNLVRACPEPCDCGEKYGFQIADCAYRDLEGVPPGFPANVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRSVAIGALAPLSHLKSLDLSHNLLSEFAWSDLHNLSALQLLKMDSNELAFIPRDAFSSLSALRSLQLNHNRLHALAEGTFAPLTALSHLQINDNPFDCTCGIVWFKTWALASAVSIPEQDNIACTTPHVLKGIPLGRLPPLPCSAPSVQLSYQPSQDGAELRPGFVLALHCDVDGQPVPQLHWHIHTPGGTVEIASPNVGTDGRALPGALATSGQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESSVNVALATPGEGGEDAVGHKFHGKAVEGKGCYTVDNEVQPSGPEDNVVIIYLSRAGPPEAAIAADGRPAQQFSGILLLGQSLLVLSFFYF
Protein: LPS-assembly lipoprotein LptE (Q83LX4)
Organism: Shigella flexneri
Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01186}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186}.
Interaction partners:
- LPS-assembly protein LptD
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system protein LptA
- Leucine--tRNA ligase
- Lipopolysaccharide export system ATP-binding protein LptB
- Outer membrane protein assembly factor BamC
- Putative permease, YjgP/YjgQ family
- Code: G
- Nicotinate-nucleotide adenylyltransferase
- Exopolysaccharide synthesis regulator.
Sequence:
MRYLATLLLSLAVLITAGCGWHLRDTTQVPSTMKVMILDSGDPNGPLSRAVRNQLRLNGVELLDKETTRKDVPSLRLGKVSIAKDTASVFRNGQTAEYQMIMTVNATVLIPGRDIYPISAKVFRSFFDNPQMALAKDNEQDMIVKEMYDRAAEQLIRKLPSIRAADIRSDEEQTSTTTDTPATPARVSTMLGN