wanglab/gogpt-training-data huggingface dataset:
Protein: Protein AF-9 (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein homolog) (A2AM29)
Organism: Mus musculus (Mouse)
Function: Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr). Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3. In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones. Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me). Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than confering, HSC stemness. Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:11439343}. Chromosome {ECO:0000250|UniProtKB:P42568}. Note=Colocalizes with acylated histone H3. H3 Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr). {ECO:0000250|UniProtKB:P42568}.
Interaction partners:
- RNA polymerase II elongation factor ELL
- AF4/FMR2 family member 1
- AF4/FMR2 family member 4
- RNA polymerase II elongation factor ELL2
- Btk-PH-domain binding protein translocated to, 1)
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Protein AF-10
- ELL-associated factor 1
- Cyclin-dependent kinase 9
- RNA polymerase II elongation factor ELL3
Sequence:
MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPKKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKDSSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKADSNLLTVTSGQQDKKAPSKRPPASDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSMLPPFDDIVDPNDSDVEENMSSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEAEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS
Protein: T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (CD antigen CD4) (P01730)
Organism: Homo sapiens (Human)
Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12089508, ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:2823150, ECO:0000269|PubMed:2990730}; Single-pass type I membrane protein {ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:1708753}. Note=Localizes to lipid rafts (PubMed:12517957, PubMed:9168119). Removed from plasma membrane by HIV-1 Nef protein that increases clathrin-dependent endocytosis of this antigen to target it to lysosomal degradation. Cell surface expression is also down-modulated by HIV-1 Envelope polyprotein gp160 that interacts with, and sequesters CD4 in the endoplasmic reticulum.
Interaction partners:
- Tyrosine-protein kinase Lck
- C-C chemokine receptor type 5
- T-cell surface glycoprotein CD8 alpha chain
- Inter-alpha-trypsin inhibitor heavy chain H4
- C-X-C chemokine receptor type 4
- Pro-interleukin-16
- HLA class II histocompatibility antigen, DR alpha chain
- T-cell surface glycoprotein CD5
- T-cell surface antigen CD2
- Syncytin-1
Sequence:
MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI
Protein: Caspase recruitment domain-containing protein 6 (Q9BX69)
Organism: Homo sapiens (Human)
Function: May be involved in apoptosis.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 2
- Nucleotide-binding oligomerization domain-containing protein 1
- Caspase recruitment domain-containing protein 8
- Ubiquitin carboxyl-terminal hydrolase MINDY-3
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MATESTPSEIIERERKKLLEILQHDPDSILDTLTSRRLISEEEYETLENVTDLLKKSRKLLILVQKKGEATCQHFLKCLFSTFPQSAAICGLRHEVLKHENTVPPQSMGASSNSEDAFSPGIKQPEAPEITVFFSEKEHLDLETSEFFRDKKTSYRETALSARKNEKEYDTPEVTLSYSVEKVGCEVPATITYIKDGQRYEELDDSLYLGKEEYLGSVDTPEDAEATVEEEVYDDPEHVGYDGEEDFENSETTEFSGEEPSYEGSETSLSLEEEQEKSIEERKKVFKDVLLCLNMDRSRKVLPDFVKQFSLDRGCKWTPESPGDLAWNFLMKVQARDVTARDSILSHKVLDEDSKEDLLAGVENLEIRDIQTINPLDVLCATMLCSDSSLQRQVMSNMYQCQFALPLLLPDAENNKSILMLGAMKDIVKKQSTQFSGGPTEDTEKFLTLMKMPVISFVRLGYCSFSKSRILNTLLSPAQLKLHKIFLHQDLPLLVLPRQISDGLVEITWCFPDSDDRKENPFFQKPVALANLRGNLESFWTQFGFLMEVSSAVFFFTDCLGEKEWDLLMFLGEAAIERCYFVLSSQARESEEAQIFQRILNLKPAQLLFWERGDAGDRRKNMEGLQAALQEVMFSSCLRCVSVEDMAALARELGIQVDEDFENTQRIQVSSGENMAGTAEGEGQQRHSQLKSSSKSQALMPIQEPGTQCELSQNLQNLYGTPVFRPVLENSWLFPTRIGGNFNHVSLKASWVMGRPFGSEQRPKWFHPLPFQNAGAQGRGKSFGIQSFHPQIFYSGERFMKFSRVARGCHSNGTFGRLPRPICQHVQACPERPQMMGTLERSRAVASKIGHSYSLDSQPARAVGKPWPQQACTRVTELTEATGKLIRTSHIGKPHPQSFQPAAATQKLRPASQQGVQMKTQGGASNPALQIGSHPMCKSSQFKSDQSNPSTVKHSQPKPFHSVPSQPKSSQTKSCQSQPSQTKPSPCKSTQPKPSQPWPPQSKPSQPRPPQPKSSSTNPSQAKAHHSKAGQKRGGKH
Protein: Proline-rich receptor-like protein kinase PERK4 (EC 2.7.11.1) (Proline-rich extensin-like receptor kinase 4) (AtPERK4) (Q9ZNQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required during abscisic acid (ABA)-mediated activation of Ca(2+) channels. Regulates ABA signaling pathways. Modulates the expression of genes related to cell elongation and ABA signaling during root growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19566594}; Single-pass membrane protein {ECO:0000269|PubMed:19566594}.
Interaction partners:
- Serine/threonine-protein kinase KIPK2
- Serine/threonine-protein kinase KIPK1
Sequence:
MASSPESAPPTNSTSSPSPPSNTNSTTSSPPAPSPPSPTPPQGDSSSSPPPDSTSPPAPQAPNPPNSSNNSPSPPSQGGGGERGNGGNNGGNDTPPSRGSPPSPPSRSNGDNGGSRSSPPGDTGGSRSDNPPSSGGSSGGGGGGRSNTNTAIIVGVLVGAGLLMIVLIIVCLRRKKKRKDSFYPEPMKGNQYQYYGNNNNNNASQNYPNWHLNSQGQNQQSTGGWGGGGPSPPPPPRMPTSGEDSSMYSGPSRPVLPPPSPALALGFNKSTFTYQELAAATGGFTDANLLGQGGFGYVHKGVLPSGKEVAVKSLKAGSGQGEREFQAEVDIISRVHHRYLVSLVGYCIADGQRMLVYEFVPNKTLEYHLHGKNLPVMEFSTRLRIALGAAKGLAYLHEDCHPRIIHRDIKSANILLDFNFDAMVADFGLAKLTSDNNTHVSTRVMGTFGYLAPEYASSGKLTEKSDVFSYGVMLLELITGKRPVDNSITMDDTLVDWARPLMARALEDGNFNELADARLEGNYNPQEMARMVTCAAASIRHSGRKRPKMSQIVRALEGEVSLDALNEGVKPGHSNVYGSLGASSDYSQTSYNADMKKFRQIALSSQEFPVSDCEGTSSNDSRDMGTKSPTPPK
Protein: Protein MAEA homolog (Q9M2V9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
Interaction partners:
- Protein GID8 homolog
- ARM repeat superfamily protein
- Ran-binding protein M homolog
- Protein RMD5 homolog
- At2g22690
- At5g09630
- At4g09200
- WD repeat-containing protein 26 homolog
- SPla/RYanodine receptor
- Protein yippee-like At5g53940
Sequence:
MEIDSATNGNSDTVMTESAATITPSPVVVSSSRSNQFTESLKLEHQLLRVPFEHYKKTIRTNHRSFEKEVSTIVNGVGELADSDWSKDDTVSRLTCLVTRLQGLKRKLEEGSNVENLQAQRCRARIDHLDSVDVENITEWNNTKLKRILVDYMLRMSYFETATKLSESSNIMDLVDIDIFREAKKVIDALKNREVASALTWCADNKTRLKKSKSKFEFQLRLQEFIELVRVDTAESYKKAIQYARKHLASWGTTHMKELQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLYGMTMEPLLNIYLQAGLSALKTPYGLEEGCTKEDPLSQENFRKLALPLPFSKQHHSKLVCYISKELMDTENPPQVLPNGYVYSTKALKEMAEKNGGKITCPRTGLVCNYTELVKAYIS
Protein: ATP synthase F(0) complex subunit 8 (A6L) (F-ATPase subunit 8) (P03928)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MPQLNTTVWPTMITPMLLTLFLITQLKMLNTNYHLPPSPKPMKMKNYNKPWEPKWTKICSLHSLPPQS
Protein: Thiosulfate dehydrogenase (EC 1.8.2.2) (Tetrathionate synthase) (D3RVD4)
Organism: Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Function: Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.
Subcellular location: Periplasm {ECO:0000269|PubMed:16995898}.
Interaction partners:
- cytochrome-c peroxidase
- SoxX
- Cbb3-type cytochrome c oxidase subunit
- Transmembrane region and signal peptide prediction
- Oxidoreductase molybdopterin-binding domain-containing protein
- Cytochrome c domain-containing protein
Sequence:
MRGDVRVHTASPIAAAWLLAVGLVAHAEEPPTVALTVPAAALLPDGALGESIVRGRRYLSDTPAQLPDFVGNGLACRHCHPGRDGEVGTEANAAPFVGVVGRFPQYSARHGRLITLEQRIGDCFERSLNGRALALDHPALIDMLAYMSWLSQGVPVGAVVAGHGIPTLTLEREPDGVHGEALYQARCLACHGADGSGTLDADGRYLFPPLWGPRSFNTGAGMNRQATAAGFIKHKMPLGADDSLSDEEAWDVAGFVLTHPRPLFQEPTGD
Protein: GH12788p (Q95U25)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIARRIVKELLIQEVPAQRDYELPEDSDWCAQEKLPPDTLCKLDALKAMARWLLGLRTDEHAAQKTFRMLAAFVNQRGDLLGQNRLCGAEKSWLRLGAACAMLKVCEQKGVGDQYSAEQYLQLSQLMADPVPEVREIFARKLHKGLSRSLPRNCLPLDFMGLYVLAGLETERKLQDLVRHYAETDVNKRREYLKTVAMTSPDSSTESQSLHILPDYMLAFAIPVLVHDPRFTNHEDYVQLRKMEKCLRFILEPLMAKRETFVHSFYKQLLQLIKHREFSLGSDKRDNYKMWALCDLAMYIIDSKFSPFDGNTSTFSMPLALPEMYYKEPAVANFQNNDVYIPLDVYTLGAKSTSKAAATAMTTSRAAVAPKRPAEQSIMDDENPQENNLFDNIRAADTTEPMAKRTRAGAASAKS
Protein: Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL (ENR) (EC 1.3.1.104) (Enoyl-acyl carrier protein reductase III) (NADPH-dependent enoyl-ACP reductase) (P71079)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan.
Interaction partners:
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Enoyl-[acyl-carrier-protein] reductase FabI
- Uncharacterized protein YfhS
- Small, acid-soluble spore protein gamma-type
- Uncharacterized protein YcsD
- Octanoyltransferase LipM
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MEQNKCALVTGSSRGVGKAAAIRLAENGYNIVINYARSKKAALETAEEIEKLGVKVLVVKANVGQPAKIKEMFQQIDETFGRLDVFVNNAASGVLRPVMELEETHWDWTMNINAKALLFCAQEAAKLMEKNGGGHIVSISSLGSIRYLENYTTVGVSKAALEALTRYLAVELSPKQIIVNAVSGGAIDTDALKHFPNREDLLEDARQNTPAGRMVEIKDMVDTVEFLVSSKADMIRGQTIIVDGGRSLLV
Protein: Methyltransferase type 11 domain-containing protein (O06190)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MANKRGNAGQPLPLSDRDDDHMQGHWLLARLGKRVLRPGGVELTRTLLARAEVTDADVLELAPGLGRTAAEILARNPRSYVGAESDPNAANLVRHVLAGRGDVRVTDAADTGLSDASADVVIGEAMLTMQGNAAKHTIVAEAARVLRPGGRYAIHELALVPDDVAEQVRTDLRQSLARALKVNARPLTVAEWSHLLAGHGLVVEHVVTASMALLQPRRVIADEGLLGALRFAGNLLIHRAARRRVLLMRHTFRRHRERLTAVAIVAHKPHVDS
Protein: Histone demethylase SWIRM1 (Zinc finger protein LSD1) (F8RP38)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQSQLVCNGCRNMLLYPRGATNVCCALCNTISPVPPPGMDMSQLYCGGCRTLLMYTRGATSVRCSCCHTVNLAPVSNQVAHVPCANCRTTLMYPYGAPSVKCAVCHYITNINMSNGRVPVPANRPQGTTNLGTLPSTSTSMPQSQGQTVVVENPMSVDSSGKLVSNVVVGVTTDKK
Protein: Outer membrane protein, MSP2 family (Q2GJ73)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MKHVVCKNCVGYVKCFTVRCAYKRVLYMVSAILLMLIMGEDAKAVGDRAVQPKKFYVALDYTPAFSKVRDFYISGDENSALVMPYPKIKEEDVRAQGWGVDWNAPNPNIEFESNALMSWEGSLGYKIKGGRIEIEVGYEKFRARVSHDSGGEIHDAAVYVFMPPRALPYFVLRGSSERLKSELSSVTEEEILTFAKGLADQRPDINRKICYKARVGGTNSHNPHVRAACQDSTLGKYVGGLYAFLKGAIEEHSIWISEGSGGRVANVSDMVSHIRALTPEEKEALSGILAIATGYGRTVEVSSITTTSVMVNACYDRNIKKMQGIEAYACMGLGSNLVEVVDKHITYKFAYRLKAGLSYQILSGVSAFVGGFYHHVIGNGVYDELPLKRIGKDFRKADRNQYEAIANFDMSYMGTEFGVRFAF
Protein: Epidermal growth factor-like protein 7 (EGF-like protein 7) (Multiple epidermal growth factor-like domains protein 7) (Multiple EGF-like domains protein 7) (NOTCH4-like protein) (Vascular endothelial statin) (VE-statin) (Zneu1) (Q9UHF1)
Organism: Homo sapiens (Human)
Function: Regulates vascular tubulogenesis in vivo. Inhibits platelet-derived growth factor (PDGF)-BB-induced smooth muscle cell migration and promotes endothelial cell adhesion to the extracellular matrix and angiogenesis.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:23386126}.
Interaction partners:
- Neurogenic locus notch homolog protein 4
- Sprouty-related, EVH1 domain-containing protein 1
Sequence:
MRGSQEVLLMWLLVLAVGGTEHAYRPGRRVCAVRAHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPGLAPARPRYACCPGWKRTSGLPGACGAAICQPPCRNGGSCVQPGRCRCPAGWRGDTCQSDVDECSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLCVPKGGPPRVAPNPTGVDSAMKEEVQRLQSRVDLLEEKLQLVLAPLHSLASQALEHGLPDPGSLLVHSFQQLGRIDSLSEQISFLEEQLGSCSCKKDS
Protein: LysM domain-containing protein (A0A0K6FU48)
Organism: Rhizoctonia solani
Interaction partners:
Sequence:
MFTKLLIASALASAAFATECARTYTVKEGDWCDTISAANNASTYQLSTVNADKINDACTNLEVGQELCLGIKGQDCTITHNVVYGDTCDKIMQAANINATMLYTNNPQIDEYCSNIYIGEVLCVAGVYAAPEPIPDRQVGAPGGEPAGPPAATPYAEAKPKVVEAPASNQNTTSVYNDPVTPPAPSPENKQPDASSYNNGGSEDDDLPECEDPNDDGY
Protein: p-83/100 protein (Q6PS53)
Organism: Borreliella burgdorferi (Lyme disease spirochete) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MKKMLLIFSFFLIFLNGFPVSAREVDREKLKDFVNMDLEFVNYKGPYDSTNTYEQIVGIGEFLARPLTNSNSNSSYYGKYFINRFIDDQDKKASVDVFSIGSKSELDSILNLRRILTGYLIKSFDYDRSSAELIAKVITIYNAVYRGDLDYYKGFYIEAALKSLSKENAGLSRVYSQWAGKTQIFIPLKKDILSGNIESDIDIDSLVTDKVVAALLSENEAGVNFARDITDIQGETHKADQDKIDIELDNIHESDSNITETIENLRDQLEKATDEEHKKEIESQVDAKKKQKEELDKKAINLDKAQQKLDSAEDNLDVQRNTVREKIQEDINEINKEKNLPKPGDVSSPKVDKQLQIKESLEDLQEQLKETGDENQKREIEKQIEIKKSDEKLLKSKDDKASKDGKALDLDRELNSKASSKEKSKAKEEEITKGKSQKSLGDLNNDENLMMPEDQKLPEVKKLDSKKEFKPVSEVDKLDKISKSNNNVGELSPLDKSSYKDIDSKEETVNKDVNLQKTKPQVKDQVTSLNEDLTTMSIDSSSPVFLEVIDPITNLGTLQLIDLNTGVRLKESTQQGIQRYGIYEREKDLVVIKMDSGKAKLQILDKLKNLKVVSESNFEINKNSSLYVDSKMILVAIRDKDSSNDWRLAKFSPKNLDEFILSENKIMPFTSFSVRKNFIYLQDEFKSLVILDVNTLKKVK
Protein: Interstitial collagenase A (EC 3.4.24.7) (Matrix metalloproteinase-1a) (MMP-1a) (Mcol-A) (Q9EPL5)
Organism: Mus musculus (Mouse)
Function: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (By similarity). Able to degrade synthetic peptides and type I and II fibrillar collagen.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
Sequence:
MPSLPLLLLLWAASSYSFPVFHNGDRQNVETVWKYLENYYNLGKNMQAKNVNGKEMMAEKLRQMQQLFGLKVTGNSDPETLRAMKKPRCGVPDVAPYAITHNNPRWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQPGPGLGGDVHYDLDETWTNSSENFNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRIQDLYGPSPNPIQPTGATTPHPCNGDLTFDAITTFRGEVFFFKGRFYIRVNRFMPEPELNLIGILWPNLPVKLDAAYEASMIDQVRYFKGSKVWAVQEQSVLRGFPRDIHSFFGFPSNVTHIDAAVCEEETGKTYFFVDHMYWRYDENTQSMDPGYPRLTAEDFPGIDDKVDDVFQKGENFYFFHQSVQHRFNLQIRRVDDSRDSSTWFNC
Protein: PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK (EC 2.7.1.121) (P76015)
Organism: Escherichia coli (strain K12)
Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP. Binds covalently dihydroxyacetone in hemiaminal linkage. DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR.
Interaction partners:
- PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
- PTS-dependent dihydroxyacetone kinase operon regulatory protein
- Glycerol dehydrogenase
- Uncharacterized transcriptional regulator YjhU
- Transcriptional regulator LsrR
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Aerobic glycerol-3-phosphate dehydrogenase
- Anaerobic glycerol-3-phosphate dehydrogenase subunit B
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MKKLINDVQDVLDEQLAGLAKAHPSLTLHQDPVYVTRADAPVAGKVALLSGGGSGHEPMHCGYIGQGMLSGACPGEIFTSPTPDKIFECAMQVDGGEGVLLIIKNYTGDILNFETATELLHDSGVKVTTVVIDDDVAVKDSLYTAGRRGVANTVLIEKLVGAAAERGDSLDACAELGRKLNNQGHSIGIALGACTVPAAGKPSFTLADNEMEFGVGIHGEPGIDRRPFSSLDQTVDEMFDTLLVNGSYHRTLRFWDYQQGSWQEEQQTKQPLQSGDRVIALVNNLGATPLSELYGVYNRLTTRCQQAGLTIERNLIGAYCTSLDMTGFSITLLKVDDETLALWDAPVHTPALNWGK
Protein: Acyl-lipid (8-3)-desaturase (EC 1.14.19.30) (AN Delta(5)-fatty-acid desaturase) (Acyl-lipid 5-desaturase) (Delta-5 fatty acid desaturase) (Q8S3C1)
Organism: Thraustochytrium sp
Function: Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKGSEGRSAAREMTAEANGDKRKTILIEGVLYDATNFKHPGGSIINFLTEGEAGVDATQAYREFHQRSGKADKYLKSLPKLDASKVESRFSAKEQARRDAMTRDYAAFREELVAEGYFDPSIPHMIYRVVEIVALFALSFWLMSKASPTSLVLGVVMNGIAQGRCGWVMHEMGHGSFTGVIWLDDRMCEFFYGVGCGMSGHYWKNQHSKHHAAPNRLEHDVDLNTLPLVAFNERVVRKVKPGSLLALWLRVQAYLFAPVSCLLIGLGWTLYLHPRYMLRTKRHMEFVWIFARYIGWFSLMGALGYSPGTSVGMYLCSFGLGCIYIFLQFAVSHTHLPVTNPEDQLHWLEYAADHTVNISTKSWLVTWWMSNLNFQIEHHLFPTAPQFRFKEISPRVEALFKRHNLPYYDLPYTSAVSTTFANLYSVGHSVGADTKKQD
Protein: CDKN1A interacting zinc finger protein 1 (Q3UUV0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFNPQLQQQQQLQQQQQQLQQQLQQQQLQQQQQQILQLQQLLQQSPPQASLSIPVSRGLPQQSSPQQLLSLQGLHSTSLLNGPMLQRALLLQQLQGLDQFAMPPATYDGASLTMPTATLGNLRAFNVTAPSLAAPSLTPPQMVTPNLQQFFPQATRQSLLGPPPVGVPINPSQLNHSGRNTQKQARTPSSTTPNRKTVPLEDREDPTEGSEEATELQMDTCEDQDSLVGPDSMLSEPQVPEPEPFETLEPPAKRCRSSEESTEKGPTGQPQARVQPQTQMTAPKQTQTPDRLPEPPEVQMLPRIQPQALQIQTQPKLLRQAQTQTSPEHLAPQQDQVPTQAQSQEQTSEKTQDQPQTWPQGSVPPPEQASGPACATEPQLSSHAAEAGSDPDKALPEPVSAQSSEDRSREASAGGLDLGECEKRAGEMLGMWGAGSSLKVTILQSSNSRAFNTTPLTSGPRPGDSTSATPAIASTPSKQSLQFFCYICKASSSSQQEFQDHMSEAQHQQRLGEIQHSSQTCLLSLLPMPRDILEKEAEDPPPKRWCNTCQVYYVGDLIQHRRTQEHKVAKQSLRPFCTICNRYFKTPRKFVEHVKSQGHKDKAQELKTLEKETGSPDEDHFITVDAVGCFESGQEEDEDDDEEEEEEGEIEAEEEFCKQVKPRETSSEQGKGSETYNPNTAYGEDFLVPVMGYVCQICHKFYDSNSELRLSHCKSLAHFENLQKYKAKNPSPPPTRPVSRKCAINARNALTALFTSSHQPSPQDTVKMPSKVKPGSPGLPPPLRRSTRLKT
Protein: Sestrin-2 (EC 1.11.1.-) (Hypoxia-induced gene) (P58004)
Organism: Homo sapiens (Human)
Function: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1. May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress. Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein. Was originally reported to contribute to oxidative stress resistance by reducing PRDX1. However, this could not be confirmed.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15105503}.
Interaction partners:
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein WDR24
- GATOR2 complex protein MIOS
- GATOR2 complex protein WDR59
- E3 ubiquitin-protein ligase RBX1
- Nucleoporin SEH1
- Serine/threonine-protein kinase ULK1
- Protein SEC13 homolog
- Sequestosome-1
- Sestrin-1
Sequence:
MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT