wanglab/gogpt-training-data huggingface dataset:
Protein: Pituitary-specific positive transcription factor 1 (PIT-1) (Growth hormone factor 1) (GHF-1) (P10037)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P28069}.
Interaction partners:
- Homeobox protein prophet of Pit-1
- Thyrotropin subunit beta
- Homeobox expressed in ES cells 1
- Growth hormone-releasing hormone receptor
- Prolactin
- Prolactin-6A1
- Pituitary homeobox 1
- LIM/homeobox protein Lhx3
- T-box transcription factor 19
- LIM homeobox 4
Sequence:
MSCQPFTSADTFIPLNSDASAALPLRMHHSAAEGLPASNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGTLTPCLYKFPDHTLSHGFPPLHQPLLAEDPTASEFKQELRRKSKLVEEPIDMDSPEIRELEQFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEHSKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR
Protein: MYB transcription factor-like protein (Myb domain protein 109) (Putative transcription factor MYB109) (Q9LDW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transmembrane protein
- Germin-like protein subfamily 2 member 2
- Probable cysteine protease RD19B
Sequence:
MEGETHQSEPLPLASGDSDEGISAAIEAELAELAAGDSSGGGGCGGGGGGIRSKVKGPWSTEEDAVLTKLVRKLGPRNWSLIARGIPGRSGKSCRLRWCNQLDPCLKRKPFSDEEDRMIISAHAVHGNKWAVIAKLLTGRTDNAIKNHWNSTLRRKYADLWNNGQWMANSVTTASVKNENVDETTNPPSSKQQLPQGDINSSPPKPPQVSDVVMEEAANEPQEPQEQQEQAPPVVSNVPTENNVFRPVARVGAFSIYNPTSQKNGYRDYNIVPCEGPLIQAAKPDSLAGKFLQSLCDEPQIPSKCGHGCSTLPAETKFSRNSVLGPEFVDYEEPSAVFNQELISIATDLNNIAWIKSGLDNAVVREAEQSLKMDNYNYNDPRIKFTGMMPRQDFFCARS
Protein: Parkin coregulated gene protein homolog (Hypertension-related protein 1-like protein) (PARK2 coregulated gene protein) (Q9DAK2)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A5PK71}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}.
Interaction partners:
- Meiosis-expressed gene 1 protein
- WD repeat-containing protein 90
- Enkurin
- EF-hand domain-containing protein 1
- EF-hand domain-containing family member C2
- Cilia- and flagella-associated protein 52
- EF-hand domain-containing family member B
- Tektin-2
- E3 ubiquitin-protein ligase parkin
- Meiosis-specific nuclear structural protein 1
Sequence:
MPKRTKLLPQQTFQVHQPRSLVSEGFTVKAMMKNSVVRGPPVAGAFKERPAKPTTFRKCYERGDFPIALEHDSKGNKIAWKVEIEKLDYHHYLPLFFDGLSEMTFPYEFFARRGIHDMLEHGGNKILPVIPQLIIPIKNALNLRNRQIICVTLKVLQHLVVSSEMVGEALLPYYRQILPILNIFKNMNVNSGDGIDYSQQKRENIGDLIQETLEAFERYGGEDAFINIKYMVPTYESCLLN
Protein: Glutathione peroxidase-like peroxiredoxin GPX3 (EC 1.11.1.24) (Glutathione peroxidase homolog 3) (GPx 3) (Q59WD3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator CAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging. The enzyme is not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, GPX3 is directly oxidized at Cys-43 to form a cysteine sulfenic acid (-SOH). Cys-43-SOH then forms either an intramolecular disulfide bond (Cys-43 with Cys-89) or a transient, intermolecular disulfide bond with 'Cys-446' of CAP1, which is further resolved into a CAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-43 in GPX3 (By similarity). Required for C.albicans-mediated macrophage killing.
Interaction partners:
- CAP1-binding-protein
- Thioredoxin
Sequence:
MGNELLSTARIYTFKIPDAYNNVIDFDQFKNKVILIVNVASLCGFTPQYKELQLLYEKYHERGLEILGFPCNQFGNQEPLQEEEIVESCRRNFGVSFPIMKKTKVNIDCDGHESELYKYLKSEKPGEVGFKGVRWNFEKFIVNRKGEVVARFNSLITPLQLEGFIEQLLSE
Protein: Enhancer of mRNA-decapping protein 4 (Protein VARICOSE) (Q9LTT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: As a component of the decapping complex, involved in the degradation of mRNAs. Essential for postembryonic development, especially during the formation of the shoot (SAM) and root apical meristems. Required for normal patterning of internal tissues of leaves.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:17158604, ECO:0000269|PubMed:17513503}.
Interaction partners:
- mRNA-decapping enzyme subunit 2
- mRNA-decapping enzyme-like protein
- Protein decapping 5
- 5'-3' exoribonuclease 4
- DEAD-box ATP-dependent RNA helicase 12
- Varicose-related protein
- Sm-like protein LSM4
- Sm-like protein LSM1A
- Sm-like protein LSM2
- Sm-like protein LSM5
Sequence:
MASSPGNTNPHNTPPFDLGILFKPSSNPYPPPAASYPPPTGPFLHNQYDQQHYAPPGISAQPSPVTQQQQDVSSSSAATNLHPQRTLSYPTPPLNLQSPRSNHNPGTHILALLNNTNNGAPVANQEPSHQLPVVNHNEIARSFPGGSGPIRVPSCKLPKGRRLIGEHAVYDVDVRLQGEIQPQLEVTPITKYGSDPQLVVGRQIAVNKVYICYGLKGGNIRVLNINTALRSLFRGHSQRVTDMAFFAEDVDMLASVSLDGKVFVWKISEGSEGEDQPQITGKIVLALQILGEEDTKHPRVCWHCHKQEILVVSIGKHVLRIDTTKVGRGEVFSAEAPLQCPLDKLIDGVQIVGKHDGEVTDLSMCQWMTTRLVSSSVDGTIKIWQDRKAQPLVVLRPHDGHPVSSATFVTSPERPDHIILITGGPLNREMKIWVSAGEEGWLLPADAESWRCTQTLDLKSSTEPRAEEAFFNQVIALSEAGLLLLANAKRNALYAVHLDYGSSPVGTRMDYLSEFTVTMPILSFIGTNDPPEEPIVKVYCVQTLAIQQYTLDLCLCLPPPIENMGLEKSDSSVSREANLVEGMSEPSGLKPTDLPSVDSVPKPSIIVNRSESANKLSFPSAEATSQAIVPPNGEPKTSGLPSQTSGAGSAYATLPQLPLSPRLSSKLSGYHTPVEAIEPVIPHHELGGKTPSADYSVDRQMDAVGERNLDVSSVEEISRSKDSNVTPDDDVSGMRSPSAFFKHPTHLVTPSEILMGVSSAEASITTEDRRDRDANIQDVNNDPRDTEVEVKEISEARSTQNGEINDHDETENCTSENREKVFCSQVSNLSTEMARDCYPSTEGTFIPGESKAYGQPIKAGDESGVDSRGGPAKLLKGKKQKAKNSQGPGLSSTSSNVANLADSFNEQSQSLSHPMTDLLPQLLAMQETMNQVMASQKEMQRQLSNAATGPIGKESKRLEVALGRMIEKSSKSNADALWARIQEETVKNEKALRDHAQQIVNATTNFMSKELNAMFEKTIKKELAAIGPALARSVVPVIEKTVSSAITESFQRGIGDKAVNQLDKSVNIKLEATVARQIQAQFQTSGKQALQEGLRSSVESSVIPSFEKACKAMFDQIDSAFQKGIAEHTNAAQQRFDSGHSQLAHTLKESITSASSVAQALSRELAETQRNLLALAAAGANSGGSNSLVTQLSGGPLGALLEKVEAPMDPTTELSRLISERKYEESFTSALQRSDVSIVSWLCSQVDLRGLLAMNPLPLSQGVLLSLLQQLACDISKDTSRKLAWMTDVVAAINPSDQMIAVHARPIFEQVYQILHHHRNAPGSDVSAIRLIMHVINSMLMGCK
Protein: UPF0126 inner membrane protein YadS (P0AFP0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Vitamin B12-binding protein
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Sequence:
MLVYWLDIVGTAVFAISGVLLAGKLRMDPFGVLVLGVVTAVGGGTIRDMALDHGPVFWVKDPTDLVVAMVTSMLTIVLVRQPRRLPKWMLPVLDAVGLAVFVGIGVNKAFNAEAGPLIAVCMGVITGVGGGIIRDVLAREIPMILRTEIYATACIIGGIVHATAYYTFSVPLETASMMGMVVTLLIRLAAIRWHLKLPTFALDENGR
Protein: Proteasome-associated ATPase (AAA ATPase forming ring-shaped complexes) (ARC) (Proteasomal ATPase) (O50202)
Organism: Rhodococcus erythropolis (Arthrobacter picolinophilus)
Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.
Interaction partners:
- Prokaryotic ubiquitin-like protein Pup 2
- Proteasome subunit alpha 2
- Proteasome subunit beta 2
- Glycerol kinase
- Glycerol kinase
- Pup--protein ligase 2
- Pup deamidase/depupylase
- Hypothetical protein
- Serine protease
- Serine protease
Sequence:
MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELLNKFVGETERHIRMIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVDGLPINADDLAEFGGDRTACLKAMIVRVVDRMYAESEENRFLEVTYANGDKEVLFFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL
Protein: Brevinin-2ISb (F1T154)
Organism: Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae)
Function: Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=12.5 ug), against Gram positive bacteria S.aureus ATCC 6538 (MIC=6.3 ug) and B.subtilis ATCC 6633 (MIC=25 ug). Has no activity against methicillin-resistant S.aureus ATCC 43300 (MIC= ug) and fungus C.albicans ATCC 90028.
Subcellular location: Secreted {ECO:0000305|PubMed:21193000}.
Interaction partners:
Sequence:
MFTMKKSLLVLFFLGTISLSLCQEERNADEEDGGEATEEEVKRSFLTTFKDLAIKAAKSAGQSVLSTLSCKLSNTC
Protein: DNA repair protein RAD51 homolog (Q95Q25)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364139}.
Interaction partners:
- DNA repair and recombination protein RAD54-like
- Exonuclease 1
- Crossover junction endonuclease MUS81
- RecQ-like DNA helicase blm-1
- Meiotic recombination protein spo-11
- Breast cancer type 1 susceptibility protein homolog
- Serine/threonine-protein kinase chk-1
- ATP-dependent helicase wrn-1
- DNA repair endonuclease XPF
- DNA repair and recombination protein RAD54-like
Sequence:
MGQSWGYEGIAKRSLCTHKWLYNLNLHSINLFLPIESKMSAQASRQKKSDQEQRAADQALLNAAIEDNAMEQDENFTVIDKLESSGISSGDISKLKEAGYYTYESLAFTTRRELRNVKGISDQKAEKIMKEAMKFVQMGFTTGAEVHVKRSQLVQIRTGSASLDRLLGGGIETGSITEVYGEYRTGKTQLCHSLAVLCQLPIDMGGGEGKCMYIDTNATFRPERIIAIAQRYNMDSAHVLENIAVARAYNSEHLMALIIRAGAMMSESRYAVVIVDCATAHFRNEYTGRGDLAERQMKLSAFLKCLAKLADEYGVAVIITNQVVAQVDGGASMFQADAKKPIGGHIIAHMSTTRLYLRKGKGENRVAKMVQSPNLPEAEATYSITNHGIEDARED
Protein: Inactive uridine phosphorylase B (SmUPb) (G4VGH9)
Organism: Schistosoma mansoni (Blood fluke)
Interaction partners:
Sequence:
MATVQPIVNSHLSELDEDVFHHFGFTTKSFDFKEKFGDVKFVCVCGSSGRIHNFAISMAKLAGLALPVENIAGSHARFVLYKVDHILFADHGIGIPSTLILMHEVTKLLYYAGCKDVLFIRLGTSDGLGVKPGTIVLSDRCVNTKLEPYNELCILGKPVRRQTKVDSNAVNELKKLSENLSLKCSVVVGGTITANDFYEELGRLNGSICTFSKEEKLAFLQSVYDHGIRNMEMEGAAITSHCNLTGHRAILVCVTVVNRLETDEVTTSTDEFKLFEQLPGQLVGEYLKRNNGIIVR
Protein: Bifunctional purine biosynthetic protein ADE1 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GAR synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIR synthetase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase)] (P20772)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ade10
- Uncharacterized protein C8E4.05c
- Uncharacterized urease accessory protein ureD-like
- Methylenetetrahydrofolate dehydrogenase [NAD
Sequence:
MEPIIALLIGNGGREHTIAWKLCESPLISKVYVAPGNGGTASNGAESKMENVNIGVCDFEQLVKFALDKDVNLVIPGPELPLVEGIEGHFRRVGIPCFGPSALAARMEGSKVFSKDFMHRNNIPTAVYKSFSNYDHAKSFLDTCTFDVVIKADGLAAGKGVIIPKTKKEAFEALESIMLNEEFGSAGKNVVIEELLEGEELSILTFSDGYTCRSLPPAQDHKRAFDGDKGPNTGGMGCYAPTPVASPKLLETVQSTIIQPTIDGMRHEGYPLVGILFTGLMLTPSGPRVLEYNVRFGDPETQAVLPLLESDLAEIILACVNHRLDAIDIVISRKFSCAVVCVAGGYPGPYNKGDIITFDALKDKNTRIFHAGTSIRDGNVVTNGGRVLAVEATGDSVEAAVRLAYEGVKTVHFDKMFYRKDIAHHALNPKRKTREILTYENSGVSVDNGNEFVQRIKDLVKSTRRPGADADIGGFGGIFDLKQAGWNDPLLVSATDGVGSKLLIALSLNKHDTVGIDLVAMNVNDLVVQGAEPLIFLDYFATGSLDLKVSTSFVEGVVKGCKQAGCALVGGETSEMPGLYHDGHYDANGTSVGAVSRDDILPKPESFSKGDILLGLASDGVHSNGYSLVRKIVEYSDLEYTSVCPWDKNVRLGDSLLIPTRIYVKPLLHVIRKNIVKGMAHITGGGLVENVPRMLPSHLNAIIDVDTWEVPEVFKWLKDAGNVPISDMARTFNMGIGMVVAVASEDAEETMKELTSVGETVYRIGQLVDKESSSERCHLVNLNKWETF
Protein: Canoe, isoform F (A0A0B4KFK9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDWGIRRSIMFHVRRRPADSQPRRRKKKPLGAANGANHISGDREGPVLVEVTHSGDGGRRIKLGSDPVEVGSANTNCLQLFGPSIQPRHCLISLLEGVCTVTPLHTDALTFVNGHHISQPTILHNGSVVMFGRVASYRFLDSPTDGRYNLALSQSQLDSACLYESRSPTSPGSWNDEDGALSSTHKSDYDHHQQANHSSAYHNNNNNSSDHPLSSTLRDVVDSKAGQDQGANSGNYDGQSLEGNLENETKSISSLKSGGSNSQDRSPKMTGSGILAGGGSGSGDTQGQEPILPAVLEFPETHQELFLRHIISELDVNVPHFKLAPVYSLYLCARYRASTHYRPELQPTERAHKLTMFLHHVANLVYSVVQEQYTDPRILAFWMANSSEFLHFLKSDRHISAFSVQAQEVLAEAVQTAFRNLVNCFRLELSQTLNQFLSENIDHDSAAGLVLTVLGSAMALLRRCRVNAALTIQLFSQLFHYINVICFNTIVANSQMCTGDWGKVMTERLQLLELWAERQGLELAADCHLAKINQCAQFLQAPKSSVEEIQQLACSCFRLNSLQMAALLQQEKLPRNLVDTAIRMAESVADELTRADGREVRLEESPELHLALLLPDDGFSCDVVRGIPTGLVDFLNPLQQQGMCRLAAQPTSIGLWTVYMHQFNARSSSAMSNKLPQPELQLIKLHKNSNGMGLSIVAAKGAGQEKLGIYIKSVVPGGAADADGRLQAGDQLLRVDGQSLIGITQERAADYLVRTGPVVSLEVAKQGAIYHGLATLLQQPSPVIQRGNRRMSERDLTRMGGAESTKSLGPLIANNHPNHSLSLSQHLNNSHNNTLGNSNNSSIINPLAAHLPNSKSVPALHHHTGSGTISLANSKSRSTHSLHNNTSGMGGIGGAAAGGMLGQPNGSQNNANGNGNGNEQGFYQNLSVYRAQNQSQPILNERPPIAAHAAMNAYNGSSPLAPQQQPQQQQQSPYQQQQQQQHMQANANLPPTRPVSAYYHSQQSAQQQLQQQQQQQQQHSLQQQQFALSSGNLNGQQQQQQQHQHQHQLTLNNRTKSQQNFQHTLRMQQMMAPSMPNISNMYHHQQQQQQQLPLQQQQQQQQQPLMSSSQSMQNVNDFAGGYQNGSLEYRRSQLHDPSTLYEIQQQQLQQQQQQQQQQQQQQQASPNFIALPPKPLGSLQSPNKPNVPPSTAPKPQQDKPPLPPTATHPLFKATQQIAPGMNYVASTLDPPKGSYVASNQGNNRPLHSGSNPWEREEREKDLEMRREHIRQWREQQISELSQIVSRSPMQEEQLKTLILERDFERRAQELQEQEEQDQEQQYDKENVQELFRLAGGGQVSAIQTPITSYRQTEIKLAEMPDSNSLVDSVPPQPPAPTAQPLSSNTQQPKSILKHNRYSEGGVGPSGAPSSPSKSQKSASFADERHLHTEHPISNLAKELNQLTMLDKDNNNETLDAVVPPPPPPERNSSYLIMSQQKLRGSTGNATSSMGLLKTATSNQAAAAVEIKKASLLNTQTNNNNNLSGSLNNNTMHGSPLSAMELNAAYVSATGTGIIGGLGTPPPPPPLMQRDNKRVSFHDEENNFVSGNSQQQQLQQQYIMDNYGMEHQDLDTIREDTSYLQHNLDASMLPSMPATPDAALWNTSVQSTPGVIGAQEVYRDPRTRRLAEKQQQQQQQRAGDAVPEKLSFKEKMKMFALESGEDKTPKDKLKISRAQRDIDAVH
Protein: Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase) (Q9GZX7)
Organism: Homo sapiens (Human)
Function: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:32484799}. Cytoplasm, cytosol {ECO:0000269|PubMed:18722174, ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:23166356, ECO:0000269|PubMed:32484799}. Note=Predominantly cytosolic (PubMed:21385873). In the presence of MCM3AP/GANP, relocalizes to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9WVE0, ECO:0000269|PubMed:21385873}.
Interaction partners:
- Uracil-DNA glycosylase
- Beta-catenin-like protein 1
- B-cell lymphoma 6 protein
- Immunoglobulin heavy variable 4-38-2
- Paired box protein Pax-5
- Putative C->U-editing enzyme APOBEC-4
- CD40 ligand
- G/T mismatch-specific thymine DNA glycosylase
- Cytochrome c oxidase subunit 5A, mitochondrial
- Tumor necrosis factor receptor superfamily member 5
Sequence:
MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL
Protein: Nicotinamide phosphoribosyltransferase (NAmPRTase) (Nampt) (EC 2.4.2.12) (Pre-B-cell colony-enhancing factor 1 homolog) (PBEF) (Visfatin) (Q99KQ4)
Organism: Mus musculus (Mouse)
Function: The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma (By similarity). Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P43490}. Cytoplasm {ECO:0000269|PubMed:12555668}. Secreted {ECO:0000250|UniProtKB:P43490}. Note=Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher concentrations compared to maternal serum. {ECO:0000250|UniProtKB:P43490}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide riboside kinase 1
- NAD-dependent protein deacetylase sirtuin-3
- NAD-dependent protein deacylase sirtuin-6
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- NAD-dependent protein deacetylase sirtuin-2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Sequence:
MNAAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKVRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKEVYREHFQDDVFNERGWNYILEKYDGHLPIEVKAVPEGSVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTEAPLIIRPDSGNPLDTVLKVLDILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKKWSIENVSFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGVNVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGHDLLHTVFKNGKVTKSYSFDEVRKNAQLNIEQDVAPH
Protein: Gibberellin 20 oxidase 5 (EC 1.14.11.-) (GA 20-oxidase 5) (Gibberellin C-20 oxidase 5) (Q4PT02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA skeleton.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 18
- At2g44240/F4I1.5
- Ent-kaur-16-ene synthase, chloroplastic
Sequence:
MCIYASRQTVCPYLTPFKVKRPKSREMNSSDVNFSLLQSQPNVPAEFFWPEKDVAPSEGDLDLPIIDLSGFLNGNEAETQLAAKAVKKACMAHGTFLVVNHGFKSGLAEKALEISSLFFGLSKDEKLRAYRIPGNISGYTAGHSQRFSSNLPWNETLTLAFKKGPPHVVEDFLTSRLGNHRQEIGQVFQEFCDAMNGLVMDLMELLGISMGLKDRTYYRRFFEDGSGIFRCNYYPPCKQPEKALGVGPHNDPTAITVLLQDDVVGLEVFAAGSWQTVRPRPGALVVNVGDTFMALSNGNYRSCYHRAVVNKEKVRRSLVFFSCPREDKIIVPPPELVEGEEASRKYPDFTWAQLQKFTQSGYRVDNTTLHNFSSWLVSNSDKKST
Protein: Selenoprotein K (SelK) (Q9JLJ1)
Organism: Mus musculus (Mouse)
Function: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration. Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins (By similarity). Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation. Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Plays a role in protection of cells from ER stress-induced apoptosis (By similarity). Protects cells from oxidative stress when overexpressed in cardiomyocytes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21220695}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9Y6D0}; Single-pass membrane protein {ECO:0000255}. Note=Probably mainly localized in the ER. {ECO:0000269|PubMed:21220695}.
Interaction partners:
- Selenoprotein S
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein F
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein N
- Selenoprotein M
- Palmitoyltransferase ZDHHC6
- Selenoprotein V
- Selenoprotein H
- Selenoprotein W
Sequence:
MVYISNGQVLDSRNQSPWRVSFLTDFFWGIAEFVVFFFKTLLQQDVKKRRGYGSSSDSRYDDGRGPPGNPPRRMGRISHLRGPSPPPMAGGUGR
Protein: Pou domain motif 3, isoform F (A0A0B4JD55)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAEGCEDSAGAAESTTSQSQYTTLDKMLGTVLPCEAAIGATPGGGSSSGNSSSNIGGNTTNSSNNGSNIVKREFCDGSLMPGAGASVNNNNANAANNNNNNSSSSNNNNNNNNTKMQAMICNKSSSTNNSSSSSSSSSSCSSSSSSSSSATSTLTSCTTAAVVPSNCSTNANKSPVSPYSQSLGMAIGIGAGAGSSPLREASPLPSSRSPLNAIASTIAAKSPCSGAAPASPPSASSNSSSHVLALNIKTESDFDKEISCHKIHSPSSSSHAHSLHHHHHHHHHPHHSSRSNNNDDEMEITDGHALLSPPPPSHSHSHSPFDSKDHVKELEFYKNLAAKAASLANQHSPPPMPLPLPLPMQIDGEEDENEGEGEGEGEAEEQSAEVMRLRREEQAQAKAFAAHLNGTMQDMINLQKLQNLATLQQQQQQQQQHPHPHHGHQHHHHHPATAAALASLQGLAASVFNSPLNLSVGGEPVATTGPSVAPTSPTHNGGKSKTAKGGSSGNGSGGSSANSGTSSAQQQQQPDNPSSSSSPHHPLSASSLANVLAAATASPPPSLQAPPASAQMPQLILASGQLVQGVQGAQLLIPTAQGIAVQTILTIPVSPQIPTTEQFLPNAFGAFASYQQQQQQQQQQRDLLPPSLAALQHATALPQLAQTPTNLLKPNLFSTGVQQLLTALHPELFAAAAATHQQQQQQQQQQVQQQREREREREREREREREREREQHLGIGHLPHSHLAADLRRSAERSPTAGSPTGGSPGLAAKGPQPPPPGAAFLLQQQLHIKPETQTHLHHHLQTQSTSAVSSTLPQISLRHPDELTAPQMDLKPLELSASTSPPAPPPRHHFGHSLRGSSTVSPKHSPQGRMGGSGGSTTTGMNLSQHHERHDRLERLERQERHERRSHTPTATATRASVSSSSSAGHHGGSLPSGRLSPPSSAPSNSAANSISDRGYTSPLFRTHSPQGHALSLGGSPRLERDYLGNGPSSGTATSTSSCGAPTAAGSSATANVLSSINRLNASNGELTITKSLGAPTATATRASSASPRDDSPGPGPSTSSVSHMQPLKLSPSSRSEPPHLSPNGNDNDNDLLMDSPNEPTINQATTNVVDGIDLDEIKEFAKAFKLRRLSLGLTQTQVGQALSVTEGPAYSQSAICSSALAAQMYAAQLSTQQQNMFEKLDITPKSAQKIKPVLERWMKEAEESHWNRYKSGQNHLTDYIGVEPSKKRKRRTSFTPQALELLNAHFERNTHPSGTEITGLAHQLGYEREVIRIWFCNKRQALKNTVRMMSKGMV
Protein: Lymphocyte-specific protein 1 (52 kDa phosphoprotein) (pp52) (Lymphocyte-specific antigen WP34) (S37 protein) (P19973)
Organism: Mus musculus (Mouse)
Function: May play a role in mediating neutrophil activation and chemotaxis.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Kinase suppressor of Ras 1
- CD209 antigen-like protein A
- Serine/threonine-protein kinase PLK3
- MAP kinase-activated protein kinase 2
- Rho guanine nucleotide exchange factor 12
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Ubiquitin carboxyl-terminal hydrolase CYLD
- CD209 antigen-like protein D
- CD209 antigen-like protein B
- CD209 antigen-like protein E
Sequence:
MAEAAIDPRCEEQEELHAEDSEGLTTQWREEDEEEAAREQRQRERERQLQDQDKDKEDDGGHSLEQPGQQTLISLKSSELDEDEGFGDWSQKPEPRQQFWGNEGTAEGTEPSQSERPEEKQTEESSHQAKVHLEESNLSYREPDPEDAVGGSGEAEEHLIRHQVRTPSPLALEDTVELSSPPLSPTTKLADRTESLNRSIKKSNSVKKSQPTLPISTIDERLQQYTQATESSGRTPKLSRQPSIELPSMAVASTKTLWETGEVQSQSASKTPSCQDIVAGDMSKKSLWEQKGGSKISSTIKSTPSGKRYKFVATGHGKYEKVLVDEGSAP