wanglab/gogpt-training-data huggingface dataset:
Protein: Cofilin-1 (18 kDa phosphoprotein) (p18) (Cofilin, non-muscle isoform) (P23528)
Organism: Homo sapiens (Human)
Function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics. Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Required for neural tube morphogenesis and neural crest cell migration (By similarity).
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P18760}. Cell projection, growth cone {ECO:0000250|UniProtKB:P18760}. Cell projection, axon {ECO:0000250|UniProtKB:P18760}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.
Interaction partners:
- Actin, cytoplasmic 1
- LIM domain kinase 1
- Protein phosphatase Slingshot homolog 1
- Actin, cytoplasmic 2
- Actin nucleation-promoting factor WASL
- Src substrate cortactin
- LIM domain kinase 2
- Hematopoietic lineage cell-specific protein
- WD repeat-containing protein 1
- Profilin-1
Sequence:
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
Protein: DNA-directed RNA polymerase subunit beta (RNAP subunit beta) (EC 2.7.7.6) (RNA polymerase subunit beta) (Transcriptase subunit beta) (P0A8V2)
Organism: Escherichia coli (strain K12)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- Large ribosomal subunit protein uL6
- Transcription termination/antitermination protein NusG
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL10
- Transcription termination/antitermination protein NusA
- DNA-directed RNA polymerase subunit beta'
- Small ribosomal subunit protein uS10
Sequence:
MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVPVEYIAGKVVAKDYIDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETLRVDPTNDRLSALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLREEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLSAIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGVVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQILEAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDEEVMRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTSGQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLLKEIRSLGINIELEDE
Protein: T6J4.11 protein (Q9FX61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKKLLDITRTDSAEKKRVRDESFDEAVLDSPEVKRLRDDLFDVLDDSDPEPVSQDLDSVMKSFEDELSTVTTTTAQGSSTAGETQPDLGYLLEASDDELGLPPPPSISPVPVAKEEVTTETVTDLVRASSDSSGIDEIWGFEDHVSNYGGLDFGSGVGDGGDYVAVEGLFEFSDDCFDSGDLFSWRSESLPAE
Protein: Sodium-dependent nutrient amino acid transporter 1 (DmNAT1) (Q9W4C5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
Sequence:
MELKGVQPSNGSSNGSGNGATNAASTEKTDAEKPTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGWKYWKVALTTSVCGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWVYGLQNFCDDIEFMCNRRVSLYWRVCWSFFTPVMMIIIFIYSMVTIEPIKYSELYFPEAANIAGWLLFAIGAAQFPLWGLWYISRHPQGTYWKSLKASLKPSDRWGPANPEIRREWVIFKNQKAAQRATQKDTSKLGFFWRKVANFCGSNK
Protein: ETHYLENE INSENSITIVE 3-like 1 protein (Q9SLH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor acting as a positive regulator in the ethylene response pathway. Could bind the primary ethylene response element present in the ETHYLENE-RESPONSE-FACTOR1 promoter.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- EIN3-binding F-box protein 1
- EIN3-binding F-box protein 2
- Ethylene-insensitive protein 2
- Ethylene-responsive transcription factor 1B
- Ethylene-responsive transcription factor 2
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 6
- Transcription factor MYC2
- Serine/threonine-protein kinase CTR1
- Ethylene receptor 1
Sequence:
MMMFNEMGMYGNMDFFSSSTSLDVCPLPQAEQEPVVEDVDYTDDEMDVDELEKRMWRDKMRLKRLKEQQSKCKEGVDGSKQRQSQEQARRKKMSRAQDGILKYMLKMMEVCKAQGFVYGIIPEKGKPVTGASDNLREWWKDKVRFDRNGPAAIAKYQSENNISGGSNDCNSLVGPTPHTLQELQDTTLGSLLSALMQHCDPPQRRFPLEKGVSPPWWPNGNEEWWPQLGLPNEQGPPPYKKPHDLKKAWKVGVLTAVIKHMSPDIAKIRKLVRQSKCLQDKMTAKESATWLAIINQEEVVARELYPESCPPLSSSSSLGSGSLLINDCSEYDVEGFEKEQHGFDVEERKPEIVMMHPLASFGVAKMQHFPIKEEVATTVNLEFTRKRKQNNDMNVMVMDRSAGYTCENGQCPHSKMNLGFQDRSSRDNHQMVCPYRDNRLAYGASKFHMGGMKLVVPQQPVQPIDLSGVGVPENGQKMITELMAMYDRNVQSNQTPPTLMENQSMVIDAKAAQNQQLNFNSGNQMFMQQGTNNGVNNRFQMVFDSTPFDMAAFDYRDDWQTGAMEGMGKQQQQQQQQQDVSIWF
Protein: Olfactory receptor (Q8VGL1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Receptor-transporting protein 1
- Guanine nucleotide-binding protein G
Sequence:
MSNCSNNALVTEFILLGFPELCHLQGLLFGFFLIIYVVTVLENLVIVGTISASRQLHTPMYFFLANLSVLETLYTTVTVPKLLADLLAGAKTISFSGCLTQLFLFLSLGSSECFLLSTMACDRYLAICRPLHYPAIMDSKLCLHLALSAWLGGFLASFVSTALISRLRFCGPNALNHFFCDISPLLQLSCTDTTAIEMLDFVAALAVLATSLIVTSVSYVHIIATVLRIPGGAGRRKAFSTCASHLVVVLIFYTTTTFMYARPHAISSFDLNKLVSVIYSVVTPLLNPIIYCLRNRDIREAFTKFLQPLRFP
Protein: Hirudin variant-1 (Hirudin-1) (Hirudin-I) (Lepirudin) (P01050)
Organism: Hirudo medicinalis (Medicinal leech)
Function: Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen.
Subcellular location: Secreted.
Interaction partners:
Sequence:
VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ
Protein: Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.30) (EC 1.14.11.n4) (Hypoxia-inducible factor asparagine hydroxylase) (Q8BLR9)
Organism: Mus musculus (Mouse)
Function: Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Poly [ADP-ribose] polymerase tankyrase-2
- Neurogenic locus notch homolog protein 1
- Hypoxia-inducible factor 3-alpha
- Transient receptor potential cation channel subfamily V member 3
- RelA-associated inhibitor
- Apoptosis-stimulating of p53 protein 1
- Transient receptor potential cation channel subfamily A member 1
- Chromodomain Y-like protein
Sequence:
MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
Protein: SgraIR restriction enzyme (Q9F6L0)
Organism: Streptomyces griseus
Interaction partners:
Sequence:
MPFTYSIEATRNLATTERCIQDIRNAPVRNRSTQFQLAQQNMLAYTFGEVIPGFASAGINGMNYRDVIGRPVENAVTEGTHFFRDDFRVDSNAKAKVAGDIFEIVSSAVMWNCAARWNSLMVGEGWRSQPRYSRPTLSPSPRRQVAVLNLPRSFDWVSLLVPESQEVIEEFRAGLRKDGLGLPTSTPDLAVVVLPEEFQNDEMWREEIAGLTRPNQILLSGAYQRLQGRVQPGEISLAVAFKRSLRSDRLYQPLYEANVMQLLLEGKLGAPKVEFEVHTLAPEGTNAFVTYEAASLYGLAEGRSAVHRAIRELYVPPTAADLARRFFAFLNERMELVNG
Protein: DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (Rad51B) (RAD51-like protein 1) (O15315)
Organism: Homo sapiens (Human)
Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- HCG2039718, isoform CRA_g
- DNA repair protein RAD51 homolog 3
- DNA repair protein RAD51 homolog 4
- DNA repair protein XRCC2
- DNA repair protein XRCC3
- Cell cycle checkpoint protein RAD1
- Breast cancer type 2 susceptibility protein
- Fanconi anemia group M protein
- DNA repair protein SWI5 homolog
- Breast cancer type 1 susceptibility protein
Sequence:
MGSKKLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLVLQETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF
Protein: Meiosis-specific cyclin crs1 (Cyclin-like protein regulated via splicing 1) (Meiotically up-regulated gene 17 protein) (O43008)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiotic chromosome segregation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiosis-specific cyclin rem1
- RNA binding exosome specificity factor Mmi1
- Meiosis-specific transcription factor mei4
- Cyclin puc1
Sequence:
MLTSKHEFSLFLNTPAINSKSEKEVISEGPLTTSNEIDVTFSESFSSHLINLRRVPSVNSIIEQEKKGLTKISPSILNQNIAYKEKRQQLFSVLYEETVGYVSMDTLCIAISLLDRCFTVKPTIPTTSFKIYAIGCLFIAFKLTSDYSVAKKSFCENLAPSLSTKNLEKYEKIVLALLNFDIYVISLPSVESFLTPLIFQHVFFKSLPSESCDQMMVEWQYLLVEVMKDCQFIEYRPTEILCASFWVLLEIIWPSAFDFKPFQHLCSLPTNGSADETYIKHSNRFHDLIISIQRIADMLA
Protein: ATP-dependent helicase/deoxyribonuclease subunit B (At3g51610) (Q8L776)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein DEFECTIVE IN EXINE FORMATION 1
- Exonuclease V, chloroplastic
- Bidirectional sugar transporter SWEET8
- Cyclin-dependent kinase G1
- Callose synthase 5
- No exine formation 1
- Exonuclease V
- Cytochrome P450 703A2
- Transcription factor DYT1
Sequence:
MAGMAAVAGLRPWNAFIQALVLISLSFPFLSSAYRPGDIVRMSKMGQYHSSRTTWHDVIGKHCPIFAVNREVLIPIAKPIGYTGTDPYKIKFQVGSEKFLIHWLLVINRKSSEVPMIDVNLRYSGGDLLGVTAQVIDMPHSYLNTHPEIRKQFWDPQHWPKHVLVRYTWKEQSEIDVSSGFYVLFGSALTFSFVLSIYVLQSSREKLARFVRETVVESSSMNVGEFGKGD
Protein: DnaJ heat shock protein family (Hsp40) member C7 (K7EJL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDF
Protein: Xylanase inhibitor protein 1 (XIP-I) (Class III chitinase homolog a) (RIXI protein) (Q7GCM7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Fungal xylanase inhibitor. Possesses competitive inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 11 (GH11). May function in plant defense against secreted fungal pathogen xylanases. Is similar to class III chitinases, but does not exhibit chitinase activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MVALGRRSWLVPLAMVLAVSSCLAGPAMAAGKTGQMTVFWGRNKNEGTLKETCDTGLYTTVVISFYSVFGHGRYWGDLSGHDLRVIGADIKHCQSKNIFVFLSIGGAGKDYSLPTSKSAADVADNIWNAHMDGRRPGVFRPFGDAAVDGIDFFIDQGAPDHYDDLARNLYAYNKMYRARTPVRLTATVRCAFPDPRMKKALDTKLFERIHVRFYDDATCSYNHAGLAGVMAQWNKWTARYPGSHVYLGLAAANVPGKNDNVFIKQLYYDLLPNVQKAKNYGGIMLWDRFYDKQTGYGKTVKYWA
Protein: mRNA-decapping enzyme subunit 1 (Q12517)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:10761922, ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:14562095}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay.
Interaction partners:
- 5'-3' exoribonuclease 1
- ATP-dependent RNA helicase DHH1
- Enhancer of mRNA-decapping protein 3
- m7GpppN-mRNA hydrolase
- Protein SCD6
- Enhancer of mRNA-decapping protein 2
- LSM1-LSM7 complex subunit LSM1
- Enhancer of mRNA-decapping protein 1
- Probable tubulin--tyrosine ligase PBY1
- LSM complex subunit LSM4
Sequence:
MTGAATAAENSATQLEFYRKALNFNVIGRYDPKIKQLLFHTPHASLYKWDFKKDEWNKLEYQGVLAIYLRDVSQNTNLLPVSPQEVDIFDSQNGSNNIQVNNGSDNSNRNSSGNGNSYKSNDSLTYNCGKTLSGKDIYNYGLIILNRINPDNFSMGIVPNSVVNKRKVFNAEEDTLNPLECMGVEVKDELVIIKNLKHEVYGIWIHTVSDRQNIYELIKYLLENEPKDSFA
Protein: Hypermethylated in cancer 1 protein (Hic-1) (Q9R1Y5)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3' (By similarity). May act as a tumor suppressor. Involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1 (By similarity). In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells (By similarity). Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes (By similarity). Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex (By similarity). Probably represses transcription from ACKR3, FGFBP1 and EFNA1 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- NAD-dependent protein deacetylase sirtuin-1
Sequence:
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLTDSVEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGSGGGGYAPYGRPGRGLRAATPVIQACYSSPAGPPPPPAAEPPSGPDAAVNTHCAELYASGPGPAASLCAPERRCSPLCGLDLSKKSPPGSSVPERPLSERELPPRPDSPPGAGPAVYKEPSLALPPLPPLPFQKLEEAVPTPDPFRGSGGSPGPEPPGRPDGSSLLYRWMKHEPGLGSYGDELVRDRGSPGERLEERGGDPAASPGGPPLGLVPPPRYPGSLDGPGTGADGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVTGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDSRTIDRFSPT
Protein: Lysophospholipase D GDPD1 (EC 3.1.4.-) (Glycerophosphodiester phosphodiesterase 4) (Glycerophosphodiester phosphodiesterase domain-containing protein 1) (Q9CRY7)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-acyl-lysophosphatidylethanolamin (N-acyl-lysoPE). In addition, hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F7}. Membrane {ECO:0000269|PubMed:25596343}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25596343}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8N9F7}. Note=Concentrated at the perinuclear region and the cell periphery. {ECO:0000250|UniProtKB:Q8N9F7}.
Interaction partners:
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Autotaxin
- Lysophospholipase D GDPD3
- Lysophospholipid acyltransferase LPCAT4
- Lysoplasmalogenase TMEM86B
- Cytosolic phospholipase A2
- Lysophosphatidic acid receptor 1
- Cytosolic phospholipase A2 epsilon
- Phospholipase A2 group V
- Cytosolic phospholipase A2 zeta
Sequence:
MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPINIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKDFLNNFSA
Protein: Anthranilate--CoA ligase (EC 6.2.1.32) (Q9I4X3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the formation of anthraniloyl-CoA, which is the priming step for entry into the Pseudomonas quinolone signal (PQS) biosynthetic pathway. Also active on a variety of aromatic substrates, including benzoate and chloro and fluoro derivatives of anthranilate.
Interaction partners:
- Anthraniloyl-CoA anthraniloyltransferase
- Anthranilate synthase component 1, pyocyanine specific
- 2-heptyl-4
- 2-heptyl-4
- Anthranilate synthase component 2, pyocyanine specific
- 2-aminobenzoylacetyl-CoA thioesterase
- Multiple virulence factor regulator MvfR
- Anthranilate synthase component 1
- Anthranilate synthase component 2
- 2-heptyl-3-hydroxy-4
Sequence:
MSTLANLTEVLFRLDFDPDTAVYHYRGQTLSRLQCRTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSLSGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLADTLYHDNLPEERAC
Protein: CD209g antigen (D3Z5D4)
Organism: Mus musculus (Mouse)
Interaction partners:
- Lymphocyte-specific protein 1
- CD209f antigen
Sequence:
MLATLVQVSRIRAYSQGQTQDQQGSSSLDKVAVPREQTHSGLEQIQQIQQQLTQFNASLAGLCRPCPWDWELFQGSCYLFSRTLGSWETSASSCEDLGAHLVIVNSVSEQQFLKYWHIRKNQLTWIGLSDHRSEGSWQWVDDTPLKLSFWKEGEPNNEGDEDCVVMAEDKWNDSRCTANNFWVCEQPSAPCPGY
Protein: F-box/kelch-repeat protein At3g27150 (Q9LI89)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box/kelch-repeat protein At1g23390
- F-box protein PP2-A14
- Probable BOI-related E3 ubiquitin-protein ligase 2
Sequence:
MLTLGEDQIGRIGASSSWSRSKKLRVHRYEIPDLNVEPSLDWDGEETGEATKALSSTCLKPKDADYCLLNVPQLVYELEVEILARVPRFEYWKLKLLNKGFSRLLKSDEIFKVRRERGVVEPSVFMLSSGDTCWTMFDKGFGNCQKLPELPSDICFLHGDKESLCAGTHLIVTGKEEKSIALWRYELETSKWFKGPAMITPRILFASATCGTVVFVAGGLKIEGNGTMEVVDSVEKYDSKTKTWTLLRGMHKRRKFCSGCYLRGKFYVLGGRDENGQNLTCGESYDEKTNTWELIPDILKDMSFSSVQSPPLIAVVGDDLYSLETSANELRVYDANANSWKKLGDVPVRAKSNGGWGVAFKSLGDKLLVIGASAGPSRAETMSVYTSRPSANPANKLYWEESKRCCGVRFNHFILNCCVMIA
Protein: Valine--pyruvate aminotransferase (EC 2.6.1.66) (Alanine--valine transaminase) (P96847)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Acyl-CoA dehydrogenase IpdE2
- Probable acyl-CoA dehydrogenase FadE32
- 3-[
- Probable acyl-CoA dehydrogenase FadE31
- 
- L-asparaginase
- Glutamate decarboxylase
- Prephenate dehydratase
Sequence:
MTDRVALRAGVPPFYVMDVWLAAAERQRTHGDLVNLSAGQPSAGAPEPVRAAAAAALHLNQLGYSVALGIPELRDAIAADYQRRHGITVEPDAVVITTGSSGGFLLAFLACFDAGDRVAMASPGYPCYRNILSALGCEVVEIPCGPQTRFQPTAQMLAEIDPPLRGVVVASPANPTGTVIPPEELAAIASWCDASDVRLISDEVYHGLVYQGAPQTSCAWQTSRNAVVVNSFSKYYAMTGWRLGWLLVPTVLRRAVDCLTGNFTICPPVLSQIAAVSAFTPEATAEADGNLASYAINRSLLLDGLRRIGIDRLAPTDGAFYVYADVSDFTSDSLAFCSKLLADTGVAIAPGIDFDTARGGSFVRISFAGPSGDIEEALRRIGSWLPSQ