wanglab/gogpt-training-data huggingface dataset:
Protein: Origin of replication complex subunit 6 (AtORC6) (Q9ZVH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y5N6}.
Interaction partners:
- Origin of replication complex subunit 1A
- DNA replication licensing factor MCM7
- Origin of replication complex subunit 1B
- Origin of replication complex subunit 2
- Origin of replication complex subunit 5
- Origin of replication complex subunit 3
- Origin of replication complex subunit 4
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM4
- Cell division control protein 6 homolog B
Sequence:
MDISDIGRKLSLDNNKLLIRKAAEIRRLCDAQFDSSIIGVGEICKAVICLEIAATRLQIIFDRQAAVKLSGMSEKAYSRSFNSLQNVIGIKIKLNVRELAVQFGCVRVIKSVQNVLSSYKERFLASLPASRRANADFTRPVFTAAAFYLCAKKQKLKVDKLRLIEVCGTSESEFSCVSTSMTDLCFDCVGISKEKKDAKDVKGNRDLLDVLPGKRRLEDGGYSSGDESSCYKRHKKMEEAKYEDWKSTVVNSIKKNPEKGTKRVIQASLNFPKKSETKELQVDS
Protein: Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) (Dihydroceramide desaturase-1) (Retinol isomerase) (EC 5.2.1.-) (Q5F3C1)
Organism: Gallus gallus (Chicken)
Function: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (By similarity). Catalyzes the equilibrium isomerization of retinols.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15121}.
Interaction partners:
- ceramide glucosyltransferase
- Acid ceramidase
- Ceramide synthase 3
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Sphingomyelin synthase 2
- sphingosine kinase
- Sphingomyelin phosphodiesterase 3.
- Ceramide synthase 6.
- DAGKc domain-containing protein.
- Phospholipid phosphatase 1
Sequence:
MGNTVAREDFEWVYTDQPHADRRKEILAKHPEIKALMKPDYNLIWVVMLMVAAQLTAFYLVRDLDWKWVVFWAYVFGSCISHSMTLAIHEISHNSAFGNGRAMWNRWFGIFANLPLGLPYSISFKRYHMDHHRYLGGDGIDVDIPTNFEGWFFCTRFRKFIWIVLQPFFYAIRPLCINPKPITRLEIINLLAQLFFDIVIYYLWGAKSIFYMLAGSVLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVKKIAAEYYDNLPQYNSWIKVLYDFVMDDTISPYSRMKRQLKGEVKQD
Protein: NAC domain-containing protein 101 (ANAC101) (Protein VASCULAR RELATED NAC-DOMAIN 6) (Q9LVA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to the secondary wall NAC binding element (SNBE), 5'-(T/A)NN(C/T)(T/C/G)TNNNNNNNA(A/C)GN(A/C/T)(A/T)-3', and to the tracheary elements (TE) specific regulating cis-element (TERE), 5'-CTTNAAAGCNA-3', in the promoter of target genes (e.g. genes involved in secondary wall biosynthesis, cell wall modification such as xylan accumulation, and programmed cell death). Involved in xylem formation in roots and shoots, especially regulating metaxylem vessel differentiation by promoting immature xylem vessel-specific genes expression, especially genes regulating programmed cell death (PCD) and secondary wall formation in tracheary elements (TE). Can activate MYB25, MYB46, MYB58, MYB63, MYB83, MYB103, CESA4, LBD15, LBD30, ERF115, XCP1, XCP2, NAC010/SND3, KNAT7, ASL19 and ASL20 expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:16103214}.
Interaction partners:
- At1g30260/F12P21_9
- Pirin-like protein At1g50590
- Cysteine protease XCP1
- Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 6
- Expansin-A22
Sequence:
MESLAHIPPGYRFHPTDEELVDYYLKNKVAFPGMQVDVIKDVDLYKIEPWDIQELCGRGTGEEREWYFFSHKDKKYPTGTRTNRATGSGFWKATGRDKAIYSKQELVGMRKTLVFYKGRAPNGQKSDWIMHEYRLETDENGPPHEEGWVVCRAFKKKLTTMNYNNPRTMMGSSSGQESNWFTQQMDVGNGNYYHLPDLESPRMFQGSSSSSLSSLHQNDQDPYGVVLSTINATPTTIMQRDDGHVITNDDDHMIMMNTSTGDHHQSGLLVNDDHNDQVMDWQTLDKFVASQLIMSQEEEEVNKDPSDNSSNETFHHLSEEQAATMVSMNASSSSSPCSFYSWAQNTHT
Protein: bZIP transcription factor 23 (OsBZIP23) (ABRE-binding factor 2) (OsABF2) (Abscisic acid responsive elements-binding factor 1) (OsAREB1) (Q6Z312)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional activator that mediates abscisic acid (ABA) signaling. Can regulate the expression of a wide spectrum of stress-related genes in response to abiotic stresses through an ABA-dependent regulation pathway. Confers ABA-dependent drought and salinity tolerance. Binds specifically to the ABA-responsive elements (ABRE) in the promoter of target genes to mediate stress-responsive ABA signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:18931143}.
Interaction partners:
- Serine/threonine-protein kinase SAPK2
- Serine/threonine-protein kinase SAPK6
- Serine/threonine-protein kinase SAPK10
- Serine/threonine-protein kinase SAPK9
- Serine/threonine-protein kinase SAPK1
- Serine/threonine-protein kinase SAPK8
- Serine/threonine-protein kinase SAPK7
- Serine/threonine-protein kinase SAPK3
- Serine/threonine-protein kinase SAPK4
- Os05g0433100 protein
Sequence:
MDFPGGSGRQQQLPPMTPLPLARQGSVYSLTFDEFQSTLGGVGKDFGSMNMDELLRSIWTAEESHAVGAATTTTATTASVAAAEHAAVGAPPVQRQGSLTLPRTLSQKTVDEVWRDMMCFGGGGASTAPAAAEPPPPAHRQQTLGEITLEEFLVRAGVVREDMSVPPVPPAPTPTAAAVPPPPPPQQQTPMLFGQSNVFPPMVPPLSLGNGLVSGAVGHGGGGAASLVSPVRPVSSNGFGKMEGGDLSSLSPSPVPYVFKGGLRGRKAPGIEKVVERRQRRMIKNRESAARSRQRKQAYMMELEAEVAKLKELNDELQKKQDEMLEQQKNEVLERMSRQVGPTAKRICLRRTLTGPW
Protein: Prohibitin (Q0E924)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|RuleBase:RU366048}.
Interaction partners:
Sequence:
MAQSKLNDLAGKLGKGGPPGLGIGLKVLAAVGAAAYGVSQSLYTVEGGHRAIIFSRLGGIQSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPTGSKDLQMINISLRVLSRPDSLNLPYLHKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAKQVAQQEAQRAVFFVERAKQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLRKLRAAQSIARTIASSQNKVYLSADSLMLNIQDSGFDDMTEKVYKSK
Protein: Stevor (Q8IBE5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNMYYLNMLLFTFLINTLVLPHYENYLNNHYNVGLIQNNTKRATINSRLLAQTKNHNPHYHNDPELKEIIDKMNEEAIKKYQQTHDPYKQLKDVVEKNGTKYTGGKDAEPMSTLEKELLETYEEMFGNESDMLKSGMSPNVDEKSSTCECTDINGVKLAKTKGRDKYLKHLKHRCIGGICSCTLGSALLTYIGTVAAKAAIIAKFAEVPKNCITSISILHMLTYDSMSSAIKSVGTAVCVADLAGEATTVSAIFVPCGIAALVLLILAVVLIILYIWLYRRRKNSWKHECKKHLCK
Protein: Baeyer-Villiger monooxygenase (BVMO) (EC 1.14.13.-) (Q9RL17)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept-2-en-6-one into the oxidative lactone products 2-oxabicyclo[3.3.0]oct-6-en-3-one and 3-oxabicyclo[3.3.0]oct-6-en-2-one. Is also able to catalyze the sulfoxidation of methyl phenyl sulfide (thioanisole).
Interaction partners:
- Flavin-dependent reductase
- Lipoprotein
Sequence:
MAHAQELTPEALAGLRERYRRERERRVRPDGTRQYLGADAEFGFYAADPWAGESDVREPVRDRVDVAVVGGGFGGVLAGARLRQQGVARVRVVEKGGDFGGTWYWNRYPGIHCDIEAHVYLPMLDETGYVPEWKYAPGEEIRRHAMRIAETFDLYTDVLFSTAVTSLSWDDTTGEWIVETDRHDAFRATYVITATGVLSELKLPGIPGIERFKGHTFHTSRWDYAYTGGGPDGGLTGLADKRVGVVGTGATGVQVIPKLAEDAGQLHVFQRTPSSVDVRANRRTTARDVGADRAGWASERRDNFLRVVSGEAVEEDLVADRWTATAGLLEKLLPSFRRPDDLAAFEAAYEVADAARMNDIRARVDDLVTDPATADRLKPWYRYACKRPTFSDLYLQAFNRDNVTLVDTADTHGIERMNERGVVVGDTEYPLDCLVFATGFSVGVSGVHSGRLPVRGRGGVRLRDAWSARGPRTLHGLTSNGFPNLIQLGGVQSASSVNHTHVLDEHAVHGAALVAAAEAKGAVVEPTREAEDAWIATLAEHAPDHAWFHAECTPGYYNAEGRGRPNGPTAYPHGAAAFHELLRRWREESMDELLAPRARVRAC
Protein: Voltage-dependent calcium channel gamma-8 subunit (Neuronal voltage-gated calcium channel gamma-8 subunit) (Transmembrane AMPAR regulatory protein gamma-8) (TARP gamma-8) (Q8VHW2)
Organism: Mus musculus (Mouse)
Function: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit. Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21127204, ECO:0000305|PubMed:21172611}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic density membrane {ECO:0000269|PubMed:21172611}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Protein cornichon homolog 2
- Voltage-dependent L-type calcium channel subunit beta-1
- Protein shisa-9
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Disks large homolog 4
- Voltage-dependent L-type calcium channel subunit beta-4
- Cation channel sperm-associated auxiliary subunit epsilon
- Voltage-dependent N-type calcium channel subunit alpha-1B
Sequence:
MESLKRWNEERGLWCEKGVQVLLTTIGAFSAFGLMTIAISTDYWLYTRALICNTTNLTAGDDGPPHRGGSGSSEKKDPGGLTHSGLWRICCLEGLKRGVCVKINHFPEDTDYDHDSAEYLLRVVRASSIFPILSAILLLLGGVCVAASRVYKSKRNIILGAGILFVAAGLSNIIGVIVYISANAGEPGPKRDEEKKNHYSYGWSFYFGGLSFILAEVIGVLAVNIYIERSREAHCQSRSDLLKAGGGAGGSGGSGPSAILRLPSYRFRYRRRSRSSSRGSSEASPSRDASPGGPGGPGFASTDISMYTLSRDPSKGSVAAGLASAGGGGSGAGVGAYGGAAGAAGGGGAGSERDRGSSAGFLTLHNAFPKEAASGVTVTVTGPPAAPAPAPAPPAPAAPAPGTLSKEAAASNTNTLNRKTTPV
Protein: Alpha-lactalbumin (Lactose synthase B protein) (B6V3I5)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL
Protein: Actin-binding LIM protein 1 (A0A8I5ZVV8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPSFLGLRCLEKLCSSEKGKGPSPERASLRGSHGRRLVIEDLSVPETPHPARHRHGTVTYLFYLYSSNRGPPELRFSSCDSSVAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEATCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQDRQSLGESPRTLSPTPSAEGFQDGRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQNKASEDIIKFSKFPAAQAPDPNEIPKIETDHWPGPPSLAAIGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKENRERASLLASRYDSPLHSASHAPSSKTSSLPGYGKSGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF
Protein: Nuclear receptor coactivator 2 (NCoA-2) (Class E basic helix-loop-helix protein 75) (bHLHe75) (Transcriptional intermediary factor 2) (hTIF2) (Q15596)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC1 expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-BMAL1 heterodimer (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8670870}.
Interaction partners:
- Estrogen receptor
- Androgen receptor
- Retinoic acid receptor RXR-alpha
- Peroxisome proliferator-activated receptor gamma
- Histone acetyltransferase p300
- Glucocorticoid receptor
- Nuclear receptor coactivator 3
- CREB-binding protein
- Nuclear receptor coactivator 1
- Histone-arginine methyltransferase CARM1
Sequence:
MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSIVNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLSSNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASSLSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESSSTAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAIINDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAGPFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSAVRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGGPQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQAQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQQNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQRTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQANTSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDTTRKYC
Protein: C2H2 type master regulator of conidiophore development brlA (Bristle A protein) (P10069)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation. They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes. Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3'. Controls the expression of the conidiophore-specific phenol oxidase ivoB. Controls the expression of the hydrophobin rodA. Mediates the developmental switch from the indeterminate, apical growth pattern of vegetative cells to the budding growth pattern of conidiophores. Expression of brlA leads to activation of abaA, wetA and stuA, cessation of vegetative growth, cellular vacuolization and spore formation.
Subcellular location: Nucleus.
Interaction partners:
- Conidiophore development regulator abaA
- Cell pattern formation-associated protein stuA
- Protein-methionine methyltransferase laeA
- Developmental regulatory protein wetA
- Spore development regulator vosA
- Developmental regulator flbA
- GATA-type domain-containing protein
- MYB family conidiophore development protein FlbD
- Protein fluG
- BZIP-type transcription factor
Sequence:
MRNQSSLSDRLTVEVDCSSLGSNECPSMTSSFSPLESPTPTPTSIYSQGSLESPGWHGAGSLPNNTYERTPGSASMRSAFRLAGMASTESLGLPYGSMEGQERMPMPDFLSGYDENIEQLWMPSEAPKSYDHVAQGLAYHQGMHQYPTMARNTNNNYRHQAAAYLPESTTNPCLSRSIFHQPERVPSSMSSSMSMNNMLPWMNLGDSIAPQTIAPSQVGPVTPPPSYTDFPTSLSAFKQHSPTTPIRSCSLGTGSGADTPLSRLSGGPCEYMDDFQPSPVYRDGFQRPHRVASRKMLRRQTSKQNLMLENLPQVIKQVQFKCKEPGCNGRFKRQEHLKRHMKSHSKEKPHVCWVPGCHRAFSRSDNLNAHYTKTHSKRGGRNRYVATLDENSPDYDPEFRGQLTPDGRPIYGSKLDDPIPGAGDMSLDGWDE
Protein: Mid1-interacting protein 1 (Gastrulation-specific G12-like protein) (Mid1-interacting G12-like protein) (Protein STRAIT11499) (Spot 14-related protein) (S14R) (Spot 14-R) (Q9NPA3)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQ20}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q9CQ20}.
Interaction partners:
- Thyroid hormone-inducible hepatic protein
- E3 ubiquitin-protein ligase Midline-1
Sequence:
MMQICDTYNQKHSLFNAMNRFIGAVNNMDQTVMVPSLLRDVPLADPGLDNDVGVEVGGSGGCLEERTPPVPDSGSANGSFFAPSRDMYSHYVLLKSIRNDIEWGVLHQPPPPAGSEEGSAWKSKDILVDLGHLEGADAGEEDLEQQFHYHLRGLHTVLSKLTRKANILTNRYKQEIGFGNWGH
Protein: Tripartite motif-containing protein 60 (RING finger protein 129) (RING finger protein 33) (Q495X7)
Organism: Homo sapiens (Human)
Interaction partners:
- Kinesin-like protein KIF3B
Sequence:
MEFVTALVNLQEESSCPICLEYLKDPVTINCGHNFCRSCLSVSWKDLDDTFPCPVCRFCFPYKSFRRNPQLRNLTEIAKQLQIRRSKRKRQKENAMCEKHNQFLTLFCVKDLEILCTQCSFSTKHQKHYICPIKKAASYHREILEGSLEPLRNNIERVEKVIILQGSKSVELKKKVEYKREEINSEFEQIRLFLQNEQEMILRQIQDEEMNILAKLNENLVELSDYVSTLKHLLREVEGKSVQSNLELLTQAKSMHHKYQNLKCPELFSFRLTKYGFSLPPQYSGLDRIIKPFQVDVILDLNTAHPQLLVSEDRKAVRYERKKRNICYDPRRFYVCPAVLGSQRFSSGRHYWEVEVGNKPKWILGVCQDCLLRNWQDQPSVLGGFWAIGRYMKSGYVASGPKTTQLLPVVKPSKIGIFLDYELGDLSFYNMNDRSILYTFNDCFTEAVWPYFYTGTDSEPLKICSVSDSER
Protein: Protein BASIC PENTACYSTEINE1 (AtBPC1) (Q9SKD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes. Negatively regulates the homeotic gene AGL11/STK, which controls ovule primordium identity, by a cooperative binding to purine-rich elements present in the regulatory sequence leading to DNA conformational changes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Polycomb group protein EMBRYONIC FLOWER 2
- Agamous-like MADS-box protein AGL11
- Telomere repeat-binding factor 1
- PLATZ transcription factor family protein
- Galactan beta-1,4-galactosyltransferase GALS1
Sequence:
MDDDGFRNWGYYEPAAASSFKGNLGLQLMSTIDRNTKPFLPGRESNLMIGSNGSYHSREQDMNYSWINQPKDNKFFNMLPISTPSYSNVLSETSGSNSIQMIHQPVLNSSRFEENPIPPPAPCEEQTGKKRKMRGSIATPTVPKAKKMRKPKEERDVTNNNVQQQQQRVKPVKKSVDLVINGVSMDISGLPVPVCTCTGTPQQCYRWGCGGWQSACCTTNISVYPLPMSTKRRGARISGRKMSQGAFKKVLEKLSTEGYSFGNAIDLKSHWARHGTNKFVTIR
Protein: Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (Inosine-5'-monophosphate dehydrogenase type II) (IMP dehydrogenase II) (IMPDH-II) (P12268)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000269|PubMed:14766016}. Cytoplasm, cytosol {ECO:0000269|PubMed:31337707}. Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine-nucleotide depletion. {ECO:0000269|PubMed:24477477, ECO:0000269|PubMed:31337707}.
Interaction partners:
- GMP synthase
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate synthetase isozyme 2
- Inosine-5'-monophosphate dehydrogenase 1
- Adenylosuccinate synthetase isozyme 1
- Inosine triphosphate pyrophosphatase
- Hypoxanthine-guanine phosphoribosyltransferase
- AMP deaminase 1
- AMP deaminase 2
- AMP deaminase 3
Sequence:
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Protein: Succinate-CoA ligase ADP-forming subunit beta (Q5T9Q5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SGRGHPSEPPASDGPAGCCSGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDK
Protein: Aprataxin (EC 3.6.1.71) (EC 3.6.1.72) (Forkhead-associated domain histidine triad-like protein) (FHA-HIT) (Q7TQC5)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity (By similarity). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q7Z2E3}. Note=Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage. Colocalizes with MDC1 at sites of DNA double-strand breaks. Interaction with NCL is required for nucleolar localization (By similarity). {ECO:0000250|UniProtKB:Q7Z2E3}.
Interaction partners:
- DNA repair protein XRCC1
- DNA repair protein XRCC4
- Aprataxin and PNK-like factor
- Tyrosyl-DNA phosphodiesterase 1
- DNA ligase 3
- DNA polymerase beta
- X-ray repair cross-complementing protein 5
- Poly [ADP-ribose] polymerase 2
- DNA ligase 1
- DNA ligase 4
Sequence:
MPEAVAKMRVCWLVRQDSRHQRIKLPHLEAVVIGRSPETKITDKKCSRQQVQLKAECNKGYVKVQQMGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEEVAESPNLTQRKRKRSDCDSEEMEAESGTGLAPGSSPSQCSVSPKKDKNGATKKESLGHWSQGLKMSMKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIADFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIKMVQEAGRVTVKDGTCELLKLPLRCHECQQLLPSIPQLKEHLRKHWGG