wanglab/gogpt-training-data huggingface dataset:
Protein: ADAMTS-like protein 4 (ADAMTSL-4) (Thrombospondin repeat-containing protein 1) (Q6UY14)
Organism: Homo sapiens (Human)
Function: Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:21989719}. Note=Colocalizes with FMN1 microfibrils in the eye ECM.
Interaction partners:
- Fibrillin-1
Sequence:
MENWTGRPWLYLLLLLSLPQLCLDQEVLSGHSLQTPTEEGQGPEGVWGPWVQWASCSQPCGVGVQRRSRTCQLPTVQLHPSLPLPPRPPRHPEALLPRGQGPRPQTSPETLPLYRTQSRGRGGPLRGPASHLGREETQEIRAARRSRLRDPIKPGMFGYGRVPFALPLHRNRRHPRSPPRSELSLISSRGEEAIPSPTPRAEPFSANGSPQTELPPTELSVHTPSPQAEPLSPETAQTEVAPRTRPAPLRHHPRAQASGTEPPSPTHSLGEGGFFRASPQPRRPSSQGWASPQVAGRRPDPFPSVPRGRGQQGQGPWGTGGTPHGPRLEPDPQHPGAWLPLLSNGPHASSLWSLFAPSSPIPRCSGESEQLRACSQAPCPPEQPDPRALQCAAFNSQEFMGQLYQWEPFTEVQGSQRCELNCRPRGFRFYVRHTEKVQDGTLCQPGAPDICVAGRCLSPGCDGILGSGRRPDGCGVCGGDDSTCRLVSGNLTDRGGPLGYQKILWIPAGALRLQIAQLRPSSNYLALRGPGGRSIINGNWAVDPPGSYRAGGTVFRYNRPPREEGKGESLSAEGPTTQPVDVYMIFQEENPGVFYQYVISSPPPILENPTPEPPVPQLQPEILRVEPPLAPAPRPARTPGTLQRQVRIPQMPAPPHPRTPLGSPAAYWKRVGHSACSASCGKGVWRPIFLCISRESGEELDERSCAAGARPPASPEPCHGTPCPPYWEAGEWTSCSRSCGPGTQHRQLQCRQEFGGGGSSVPPERCGHLPRPNITQSCQLRLCGHWEVGSPWSQCSVRCGRGQRSRQVRCVGNNGDEVSEQECASGPPQPPSREACDMGPCTTAWFHSDWSSKCSAECGTGIQRRSVVCLGSGAALGPGQGEAGAGTGQSCPTGSRPPDMRACSLGPCERTWRWYTGPWGECSSECGSGTQRRDIICVSKLGTEFNVTSPSNCSHLPRPPALQPCQGQACQDRWFSTPWSPCSRSCQGGTQTREVQCLSTNQTLSTRCPPQLRPSRKRPCNSQPCSQRPDDQCKDSSPHCPLVVQARLCVYPYYTATCCRSCAHVLERSPQDPS
Protein: Coiled-coil domain-containing protein 17 (Q96LX7)
Organism: Homo sapiens (Human)
Interaction partners:
- Vasculin-like protein 1
Sequence:
MDSHSGEPALLPCGTCDMVFRSSALLATHTQRFCIGHPTQEMTFGAQASVATEPQRAAVVPQEHQGVPQEPQGLPDQQASRSALKRLTEEVQWLRLSLQEMRPWITEVPRVFAGPWTRSEARPQSPMSEAVGSPSERLRALFRTRARRVAEMEAQSRALQLRGEELSRRLQVVACTRGGMSRLFGLEQEIRELQAEAGRTRGALEVLGARIQELQAEPGNPLSSRREAELYSPVQKANPGTLAAEIRALREAYIRDGGRDPGVLGQIWQLQVEASALELQRSQTRRGRAGATSGELPVVEAENRRLEAEILALQMQRGRAPLGPQDLRLLGDASLQPKGRRDPPLLPPPVAPPLPPLPGFSEPQLPGTMTRNLGLDSHFLLPTSDMLGPAPYDPGAGLVIFYDFLRGLEASWIWVQLRTGLARDGRDTGRTTALPPALCLPPPPAPGPMGNCAILASRQPVPRLPPSSSVSLVCELQVWQGLAWARAPQPKAWVSLGLFDQDQRVLSGRWRLPLRALPLDPSLSLGQLNGIPQAGQAELFLRLVNARDAAVQTLAEINPASVHEYQYPPPVSSTSSLEASFLTPAVGFADPPPRTEEPLSGVKDRDEGLGPHHSSDLPPVSF
Protein: Erythrocyte protein band 4.1-like 3 (A3E0T0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTTESGSDSESKPDQEAEPQEAAGPQEQAGAQAAPEPAGGNVEEQPGLEQFPEAAAHSTPVKREVSDKDRDFAAAAAKQLEYQQFEDDKLSQKSSSSKLSRSPLKIVKRPKSMQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKVISQTNLITTVTPEKKAEEEHVEEEDRRKKAEEATPVAALRHEGKTDSERTDTAADGETSATEELDKTQDELVKHQTNISELKRTFLETSTETALTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEEKLETKTETIETEVEPTPHPQPLSTEKVLQETVLVEERHVMNVHASGDASHTARDDVDATESAPADRHSGNGKEGSSVTEAAKEQRGEEADKSAPEQEQPATVSQEEDQVSAIHSSEGLEQKSHFESSTVKVESISVGSVSPGGVKLETSTKEVPVVHTETKTITYESSQVDPGADLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (G3V328)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESIFHEKVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDL
Protein: LD12333p (Q8SX88)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSQIIEYMLLRTQDTDEGVALEASEFWLSLAEQSICKDVLAPYLAQLAPVLVRGMRYSEVDIILLKGNVEEDDMVPDREEDIRPRFHKSRAHTIRSTQEGGAGATGDDDDDEFEDGMDDDSSLSEWNLRKCSAAALDVLANVFREDCLPVVLPILKETLFHQEWVIKESGVLALGAIAEGCMQGMIQHLPELIPYLISCLSDKKALVRSITCWTLSRYANWVVNQPHDQYLKPLMEELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLEYILKTLVFAFSKYQHKNLLILYDAVGTLADSVGHHLNKPQYIDILMPPLIDKWNLLKDDDKDLFPLLECLSSIATALQSGFLPYCDPVYRRCISLIEQTINQEMLCKQNQTYDHPDKERMIVALDLLSGLAEGLDRHIETLVANSNIMHLLYQCMQDVLPEVRQSSFALLGDLTKACFPHVHPFMADFFPILGQNLNPDFISVCNNATWAIGEICMKLGEETKQYIRLVLSDLFIIINRPNTPKTLLENTAITIGRLGYVCPVEVAPYLPEFVRQWCTSLRHIRDNDEKDSAFRGMCHMITVNPAGVVADFIFFCDAIASWVNPPEDLHQMIQKILHGFKTQVGEENWRRFVEQFPPTLAERLTTMYNI
Protein: STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) (Q3UUJ4)
Organism: Mus musculus (Mouse)
Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q7RTN6}.
Interaction partners:
- Serine/threonine-protein kinase STK11
- Calcium-binding protein 39
- Calcium-binding protein 39-like
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- STE20-related kinase adapter protein beta
- Serine/threonine-protein kinase 25
- 5'-AMP-activated protein kinase subunit gamma-1
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit gamma
Sequence:
MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKANEASSESIASFSKPEMMSSFLPEGGCYELLTIIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIGTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSIANPGLNDSLAAGSLRPSNGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEDLEVDDWEF
Protein: N-acetylneuraminate (7)9-O-acetyltransferase (EC 2.3.1.45) (CAS1 domain-containing protein 1) (CAS1 protein) (Cas1p) (Sialate O-acetyltransferase) (SOAT) (Q96PB1)
Organism: Homo sapiens (Human)
Function: O-acetyltransferase that catalyzes 9-O-acetylation of sialic acids. Sialic acids are sugars at the reducing end of glycoproteins and glycolipids, and are involved in various processes such as cell-cell interactions, host-pathogen recognition.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:26169044}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sialate O-acetylesterase
Sequence:
MAALAYNLGKREINHYFSVRSAKVLALVAVLLLAACHLASRRYRGNDSCEYLLSSGRFLGEKVWQPHSCMMHKYKISEAKNCLVDKHIAFIGDSRIRQLFYSFVKIINPQFKEEGNKHENIPFEDKTASVKVDFLWHPEVNGSMKQCIKVWTEDSIAKPHVIVAGAATWSIKIHNGSSEALSQYKMNITSIAPLLEKLAKTSDVYWVLQDPVYEDLLSENRKMITNEKIDAYNEAAVSILNSSTRNSKSNVKMFSVSKLIAQETIMESLDGLHLPESSRETTAMILMNVYCNKILKPVDGSCCQPRPPVTLIQKLAACFFTLSIIGYLIFYIIHRNAHRKNKPCTDLESGEEKKNIINTPVSSLEILLQSFCKLGLIMAYFYMCDRANLFMKENKFYTHSSFFIPIIYILVLGVFYNENTKETKVLNREQTDEWKGWMQLVILIYHISGASTFLPVYMHIRVLVAAYLFQTGYGHFSYFWIKGDFGIYRVCQVLFRLNFLVVVLCIVMDRPYQFYYFVPLVTVWFMVIYVTLALWPQIIQKKANGNCFWHFGLLLKLGFLLLFICFLAYSQGAFEKIFSLWPLSKCFELKGNVYEWWFRWRLDRYVVFHGMLFAFIYLALQKRQILSEGKGEPLFSNKISNFLLFISVVSFLTYSIWASSCKNKAECNELHPSVSVVQILAFILIRNIPGYARSVYSSFFAWFGKISLELFICQYHIWLAADTRGILVLIPGNPMLNIIVSTFIFVCVAHEISQITNDLAQIIIPKDNSSLLKRLACIAAFFCGLLILSSIQDKSKH
Protein: Cyclin-dependent kinase 4 (EC 2.7.11.22) (Cell division protein kinase 4) (P79432)
Organism: Sus scrofa (Pig)
Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
Interaction partners:
- Cyclin D1
- Cyclin-dependent kinase inhibitor 1
- Cyclin D3
- G1/S-specific cyclin-D2
- Retinoblastoma-associated protein
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase inhibitor 1B
- G1/S-specific cyclin-E1
- Cyclin dependant kinase inhibitor
- M-phase inducer phosphatase
Sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGNPE
Protein: Tobamovirus multiplication protein 3 (AtTOM3) (Q9ZUM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to the intracellular multiplication of tobamoviruses, probably being a membrane anchor promoting the formation of the replication complex.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Tobamovirus multiplication protein 2A
- Tobamovirus multiplication protein 2B
- Fasciclin-like arabinogalactan protein 17
- ADP-ribosylation factor-like protein 8b
- Heptahelical transmembrane protein 5
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- ADP-ribosylation factor-like protein 8a
- ADP-ribosylation factor-like protein 8c
- Heptahelical transmembrane protein 2
Sequence:
MRIGGVEVTKFASEMMSSSSSSAVEMLNLKEASNWWSDVNESPIWQDRIFHVLAVLYGIVSLVAVIQLVRIQLRVPEYGWTTQKVFHFLNFVVNGVRAVVFVFRRNVQFMQPEILQHILLDIPSLAFFTTYALLVLFWAEIYYQARAVSTDGLRPSFFTINAVVYVVQIALWLVLWWKPVRVMVILSKMFFAGVSLFAALGFLLYGGRLFLMLQRFPVESKGRRKKLQEVGYVTTICFTCFLIRCIMMCFAAFDEGANLDVLDHPILNFIYYLLVEILPSSLVLFILRKLPPKRGITQYHQIR
Protein: Paired zinc finger protein 1 (G5EGQ2)
Organism: Caenorhabditis elegans
Function: Possible transcriptional regulator (Probable). Involved in promoting segregation of chromosomes during meiosis, perhaps acting downstream of the let-60 RAS / mpk-1 MAPK signaling pathway.
Interaction partners:
- CNDH2_C domain-containing protein
- Uncharacterized protein
- AAA domain-containing protein
- Chondroitin proteoglycan 3
- EF-hand domain-containing protein
- Equilibrative nucleoside transporter 1
- Protein meg-1
- T-box transcription factor 18
- Choline transporter-like protein 1
Sequence:
MDYVNRNLDDKLLCGICGKYFSDDESLREHRRQRHMTCHMCLLCNRRIPENETLREHMKNKHNIWKLFICVCCNWSFGTEIYLKCHEECMKSTGRPGLLKPLAMPMTAPAREASALNTDPQNGSDDVPHSSPSPVPMIAENSIIQASSLKMEPIESADRSSASTSTPRTLVSGTPREKIPCGFCGKDFFHEGSLREHRRRFHMTGHTCLLCNRQIPENETVRDHMKSQHNIKKVYNCLCCNWTFLNQVHLISHKTCLKQTGKPCCRPGHMEPLAIPRTASIRQFFTLKTETQSGDDDSAAGSQLFSARLSCKSCGKFFYSERSLSKHHRQIHMSGHVCVLCNHQMPKTVTVQEHMEKEHNIRLVFNCRCCNWSFATRRCLMSHVECLKKAGDARNVKPVAIPRMAADSILQSLKESEAQEYPDFSAASTTSSGPASTLKTPRMDFKKNLKICTDAVQILVGNGLFSNEQLAQTETWVMIFSNANKLFHSMNSFGEPSVSRDIPM
Protein: Eukaryotic translation initiation factor 2 subunit 3 (EC 3.6.5.3) (Eukaryotic translation initiation factor 2 subunit gamma X) (eIF2-gamma X) (eIF2gX) (P41091)
Organism: Homo sapiens (Human)
Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09130}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2 subunit 2
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 3 subunit B
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 3 subunit G
Sequence:
MAGGEAGVTLGQPHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD
Protein: SKP1-like protein 18 (AtSK18) (Q9SY65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Putative cullin-like protein 1
- Putative cullin-like protein 2
- Cullin-like protein 3
- Cullin-2
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Putative F-box protein At3g22940
- Elongin-C
Sequence:
MSSNKILLTSSDGESFEIDEAVARKFLIIVHMMEDNCAGEAIPLENVTGDILSKIIEYAKMHVNEPSEEDEDEEAKKNLDSWDAKFMEKLDLETIFKIILAANYLNFEGLLGFASQTVADYIKDKTPEEVREIFNIENDFTPEEEEEIRKENAWTFNE
Protein: Floral homeotic protein AGAMOUS (P17839)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the control of organ identity during the early development of flowers. Is required for normal development of stamens and carpels in the wild-type flower. Plays a role in maintaining the determinacy of the floral meristem. Acts as C class cadastral protein by repressing the A class floral homeotic genes like APETALA1. Forms a heterodimer via the K-box domain with either SEPALATTA1/AGL2, SEPALATTA2/AGL4, SEPALLATA3/AGL9 or AGL6 that could be involved in genes regulation during floral meristem development. Controls AHL21/GIK, a multifunctional chromatin modifier in reproductive organ patterning and differentiation. Induces microsporogenesis through the activation of SPL/NZZ.
Subcellular location: Nucleus.
Interaction partners:
- Developmental protein SEPALLATA 3
- Protein CRABS CLAW
- Zinc finger protein KNUCKLES
- Developmental protein SEPALLATA 2
- Developmental protein SEPALLATA 1
- Floral homeotic protein APETALA 3
- Protein FLOWERING LOCUS T
- Floral homeotic protein PISTILLATA
Sequence:
MAYQSELGGDSSPLRKSGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYSNNSVKGTIERYKKAISDNSNTGSVAEINAQYYQQESAKLRQQIISIQNSNRQLMGETIGSMSPKELRNLEGRLERSITRIRSKKNELLFSEIDYMQKREVDLHNDNQILRAKIAENERNNPSISLMPGGSNYEQLMPPPQTQSQPFDSRNYFQVAALQPNNHHYSSAGRQDQTALQLV
Protein: NADH-dependent phenylglyoxylate dehydrogenase subunit gamma (EC 1.2.1.58) (Phenylglyoxylate:NAD oxidoreductase) (Phenylglyoxylate:acceptor oxidoreductase) (Q8L3B3)
Organism: Aromatoleum evansii (Azoarcus evansii)
Function: Involved in the anaerobic metabolism of phenylalanine and phenylacetate. Catalyzes the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO(2). It can also react slowly with 2-oxo-3-methylbutanoate and use different electron acceptors such as benzyl viologen, methyl viologen, FAD or FMN, but NAD seems to be the physiological electron acceptor. Also catalyzes an isotope exchange between CO(2) and the carboxyl group which proves partial or complete reversibility of the oxidative decarboxylation reaction.
Interaction partners:
Sequence:
MYEVRFHGRGGQGSVMASGMLAAAMVEEGKYAVSIPSFGFERRGAPVVSFLRMSDREIRQLTNIYQPDCIVCVDPTLTKSVDIFAGMKAGGTLVQATHHPLSELALPDCVSTVGLLDAVKIALEIFKRPITNTLMLGAFAKTTGVVSLESLKRALEDSEFRDAGLAQNMTALERGYAEVAVHHIERRAAA
Protein: Phospholipase D beta 1 (AtPLDbeta1) (PLD beta 1) (PLDbeta) (EC 3.1.4.4) (P93733)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Involved in regulating stomatal movement and plant-water status. Can use phosphatidylserine (PS) and phosphatidylethanolamine (PE) as substrates only in the presence of PIP2. Can use phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-acylphosphatidylethanolamine (NAPE) as substrates in the presence of PE and PIP2. Modulates defense responses to bacterial and fungal pathogens.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q38882}. Membrane {ECO:0000250|UniProtKB:Q38882}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q38882}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Non-specific phospholipase C1
- Non-specific phospholipase C6
- Non-specific phospholipase C2
- Non-specific phospholipase C5
- Non-specific phospholipase C4
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 3
- Phosphatidylserine decarboxylase proenzyme 2
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
Sequence:
MDNHGPRYPYPYGQYPYPYPYPAPYRPPSSEPYPPPPTNQYSAPYYPYPPPPYATPPPYASPPPPHQHTSGSHSGPLDYSHNPQPSSLAAAPPEYHRHSFDYQPSPYPYQPQGNFGAYGPPPPHYSYQEPAQYPPPETKPQEPLPPPQQTQGFQEYRRQDCLSTGGTGHDNVSNSGSSYPPVDELLGGLHISTNQPGPSVPQLSSLPSNSWQSRPGDLYGYPNSSFPSNSHLPQLGRVDSSSSYYASTESPHSADMQMTLFGKGSLKVLLLHGNLDIWIYHAKNLPNMDMFHKTLGDMFGRLPGKIEGQLTSKITSDPYVSVSVAGAVIGRTYVMSNSENPVWMQHFYVPVAHHAAEVHFVVKDSDVVGSQLIGLVTIPVEQIYSGAKIEGTYPILNSNGKPCKPGANLSLSIQYTPMDKLSVYHHGVGAGPDYQGVPGTYFPLRKGGTVRLYQDAHVPEGMLPGIRLDNGMSYEHGKCWHDMFDAIRQARRLIYITGWSVWHKVKLIRDKLGPASECTLGELLRSKSQEGVRVLLLIWDDPTSRSILGYKTDGVMATHDEETRRFFKHSSVQVLLCPRNAGKRHSWVKQREVGTIYTHHQKNVIVDADAGGNRRKIIAFVGGLDLCDGRYDTPQHPLFRTLQTIHKDDFHNPTFTGNLSGCPREPWHDLHSKIDGPAAYDVLTNFEERWLKAAKPSGIKKFKTSYDDALLRIDRIPDILGVSDTPTVSENDPEAWHVQIFRSIDSNSVKGFPKDPKDATCKNLVCGKNVLIDMSIHTAYVKAIRAAQHFIYIENQYFIGSSYNWNAHKDIGANNLIPMEIALKIAEKIRANERFAAYIVIPMWPEGVPTGAATQRILYWQHKTIQMMYETIYKALVETGLEGAFSPQDYLNFFCLGNREMVDGIDNSGTGSPSNANTPQALSRKSRRFMVYVHSKGMVVDDEYVVIGSANINQRSMEGTRDTEIAMGAYQPQHTWARKHSGPRGQIYGYRMSLWAEHMATLDDCFTQPESIECVRKVRTMGERNWKQFAAEEVSDMRGHLLKYPVEVDRKGKVRPLPGSETFPDVGGNIVGSFIAIQENLTI
Protein: Uncharacterized protein At2g33180 (O49317)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MELVSLPIHHRTAPPNFPPLETGNPVANRIGQALRFSNVRMRKPAYLGTILSEKSRARTLTTAEAVSGSGVSLPPLDLTEDNIHLVLSEARIELAQLFDSSVGITGQVELVELDGPFVTISLRGKFWHTRAMVLARLGNYLKQRIPEILEVNIEDEKQLDDSPANF
Protein: Dehydrogenase E1 component (O53855)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTRTSEGLAAFVVDQLEELYRRMWVLRLLDMALEQLRIEGLINGPLQGGFGQEAVSVGAAAALGEGDVIITTHRPHAQHVGTDAPLGPVIADMLGATAGDLEGADEDAHIADPRAGLPAAIRVVKQSPLLAIGHAYALWLRDTGRVTLCVTQDCDVDADAFNEAADLAAVWQLPVVILVENIRGALSVHLDRYTHEPRVYRRAVAYGMPGVSVDGNDVEAVRDCVANAVVRARAGGGPTLVQAITYRTTDFSGSDRGGYRDLAGSEQFLDPLIFARRRLIAAGTTRGRLDEQERAACQQVADAVAFAKARARPNGGGPISRPTSGWHQQPKTRF
Protein: Neuferricin (Cytochrome b5 domain-containing protein 2) (Q5SSH8)
Organism: Mus musculus (Mouse)
Function: Heme-binding protein which promotes neuronal but not astrocyte differentiation.
Subcellular location: Secreted {ECO:0000269|PubMed:19968755}.
Interaction partners:
- CD82 antigen
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Ganglioside GM2 activator
- Beta-1,3-galactosyltransferase 4
- Elongation factor 1-alpha 2
- Lactosylceramide alpha-2,3-sialyltransferase
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Sialidase-3
- Ceramide glucosyltransferase
- Beta-hexosaminidase subunit alpha
Sequence:
MLRICGLGVVLSLAVAAVAVMAVWLMDWWGPRPGIRLFLPEELARYRGGPGDPGLYLALLGRVYDVSSGRRHYEPGAHYSGFAGRDASRAFVTGDYSEAGLVDDINGLSSSEILTLHNWLSFYEKNYVFVGRLVGRFYRKDGLPTSELTQVEAMVTKGMEANEQEQREKQKFPPCNSEWSSAKGSRLWCSQKSGGVHRDWIGVPRKLYKPGAKEPHCVCVRTTGPPSDQQDNPRHSNHGDLDNPNLEEYTGCPPLATTCSFPL
Protein: Armadillo/beta-catenin-like repeat (Q388H0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCSLSPNMLNGRIAALVLVLSEGDEAGQCPLSKFVRSIRESSKAQQQRSSNGGLAHGDLSSRAASAMSHLSDIVAERSLALTNEEEAILRDMEAVRLTYDKLRAEVARVEAQLQSLERRAQEVAQQKAFCKTAMNMLVMGELPEFFEREVDVVGRSPRENVGATTEVAAAATIDGPNEVPTSSNSPRRSARSVVSGKFQQRMPAENGGDASSPDTTGEKRGEKVAPDESSEESSSSEGDIQARRSPPDKGNSSFRGSSGSGNNNCPSGNALLSMLRLPDVKETTLLHAIESYDEQNFRRSSWTLTQQKEVSTVLVGLLKHILHPRPPIQLAELRILGHVVRAAFGNQSTVDSPSVPMSRSPTLIPEAVAVSLLHTMLKDGAVVTTFIRLLQSVNDDVKCEVLECLSPLIINSNNNNNNSNANSGSRSLSSKVLDPAGEGRRQLPDGRKEFIAAGGLQPLVNIVASCTSEAVLERSLVLLWSLLARNDDEDKVRDEVRRLGGLRAVLDLLYTDSIPILENVAMTIGYITREEASKVAIREAGGLEKLTATLRHPYESIQTKVAGAVWNCASNAENRTYLRYIGCIPALIELLSSPQQFVQENAAGALWNLSVDSENKTQILEYGGITELAHLIAKSTSVSVVENASGTLWNCSAAVETRPAIRKAGAIPVLLSVLDRKSQTTNPRRSRNEAPTTSGSKDDLGGNLPISDKILDNVAGTLRNCAINDQNKPVIREAGGVELLLKKLEQGIVQQPSSIIMPTLDKIASTLWILTISPEIKHSVRLSGGIPLLTKILEISSTTAAKEKNAKVVVPVMLSVKEKIVGILRNCSTVQENRQTMVSAGVVRALVYVVDDCYQYPESCQNTRRSSSNTSQSQQQQQPSLQLKETVASALWYLSRDDKVVPREERGLELLCRFLLEPDQPSVVLEQAAGALSSLTVNSRENRAKLREFGGLHALLQLIAEKAPLAFPPQSAGASGAASAANTATATASTITVNRATTSSSTFGTGTVKKENTVSHAYAVLNGLLAVRNSTSSNDENLCCVAEWKDPNAKGNTAAASSFTNSLLYIIQHGSEDCAREAVLCVKNLCGHATALDSLIAQDAVEVLGGLAERGSTDSVRRAAAMTLHSLARARKR