wanglab/gogpt-training-data huggingface dataset:
Protein: Chlorophyll synthase, chloroplastic (EC 2.5.1.62) (Polyprenyl transferase) (Protein G4) (AtG4) (Q38833)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in one of the last steps of the biosynthesis of chlorophyll a. Catalyzes the esterification of chlorophillide a or b with a preference for geranylgeranyldiphosphate (GGPP) rather than for phytyldiphosphate (PhyPP).
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Nuclear/nucleolar GTPase 2
- 7-hydroxymethyl chlorophyll a reductase, chloroplastic
- Pescadillo homolog
- 60S ribosomal export protein NMD3
- Protochlorophyllide reductase C, chloroplastic
- Ribosome production factor 2 homolog
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
Sequence:
MTSILNTVSTIHSSRVTSVDRVGVLSLRNSDSVEFTRRRSGFSTLIYESPGRRFVVRAAETDTDKVKSQTPDKAPAGGSSINQLLGIKGASQETNKWKIRLQLTKPVTWPPLVWGVVCGAAASGNFHWTPEDVAKSILCMMMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISEPEVITQVWVLLLGGLGIAGILDVWAGHTTPTVFYLALGGSLLSYIYSAPPLKLKQNGWVGNFALGASYISLPWWAGQALFGTLTPDVVVLTLLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGTETAKWICVGAIDITQLSVAGYLLASGKPYYALALVALIIPQIVFQFKYFLKDPVKYDVKYQASAQPFLVLGIFVTALASQH
Protein: Cyclin-dependent kinase 5 activator (B3DH98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
Interaction partners:
- Cell division protein kinase 5
- Astrotactin 1
Sequence:
MGTVLSVSPSYRKAGLFDEIPPPLAHYTAVQNSKNAKDKGLKRQSLINVLPWKRIVAASAKRKGSKKLPSGDSQDEECVGTLNSQNLKKSQSCANLSGFTQEPAVSSIPTSKTTTNVTSTAKRTPITELVAQATNAGTPKRVIVQASTCELLRNLGDFLSRRCYRLKRFSPAEPIVWLRQVDRSLLLQGWQDQGFITPANLVFLYMLCREVISPEVSSERELQAEVLTCLYLSYSYMGNEISYPLKPFLVEMDKDVFWNRSLDIINRMSGKMLQLNSDPHYFTQVFADLKNEREITISQLCIGLDR
Protein: Basic phospholipase A2 10 (svPLA2) (EC 3.1.1.4) (Cdc-10) (Phosphatidylcholine 2-acylhydrolase) (P86806)
Organism: Crotalus durissus cumanensis (South American rattlesnake)
Function: Snake venom phospholipase A2 (PLA2) that has a strong dose-dependent anticoagulant effect. Intramuscular and intervenal injection causes muscle necrosis. Induces moderate edema in the mouse foot pad. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:19747981}.
Interaction partners:
Sequence:
SLLQFNKMIKFETRKSGVPFYAAYGCYCGWGGRRPKDPTDRCCFVHDCCYGKLTKCNTKWDIYSYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLNTYKNEYMFYPDSRCRGPPEYTC
Protein: Deuterosome assembly protein 1 (Coiled-coil domain-containing protein 67) (Q7M6Y5)
Organism: Mus musculus (Mouse)
Function: Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24240477}. Note=Localizes to the deuterosome.
Interaction partners:
- Serine/threonine-protein kinase PLK4
- Centrosomal protein of 152 kDa
- Multicilin
Sequence:
MENQAHTTAGASPCEAELQELMEQIDIMVSNKKLDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLVMTQNYEGQLQTLKAQFSKLTSNFEKLRLHQMKQNQIHRKESSSKEELPFELSSLNQKLEEFRAKSREWDKQEVLYQTHLVSLDAQQKLLSEKCSQFQKQAQNYQTQLNGKKQCAEDSSSEIPRLVCESDPGCEATQRDEFIIEKLKSAVSEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLHLHRELLRMGEVQTAQDNRKRVESSYSPSPKEAERKRKELFPMVSDQPNHEKELSKMRSQLYQEEGLCSEQERLRSEISELTQELHQKEVTIATVMKKAALLERQLKIELEIKERMLAKQQVSDRRYKAVRTENTHLKGMMGDLDPARYLAVDLSNKKHSQCTSINKLEYENERLRSDLAKLHGNGKAAWPNQSSYGEAGAYVFQSQLKTETSGDRISQDCELNRSPTPLSPLPFQTKEMASPLVGDNEVLALSPPDISFRASLAAQHFLMEEERRAKELEKLLNTHIDELQRHTEFTLNKYTKLKQSRHI
Protein: Succinylornithine transaminase (SOAT) (EC 2.6.1.81) (Carbon starvation protein C) (Succinylornithine aminotransferase) (P77581)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Is involved in the utilization of arginine as a nitrogen source, via the AST pathway, and seems also to play a role in ornithine catabolism.
Interaction partners:
- N-succinylglutamate 5-semialdehyde dehydrogenase
- N-succinylarginine dihydrolase
- Arginine N-succinyltransferase
- Succinylglutamate desuccinylase
- Acetylglutamate kinase
- Lysine/arginine/ornithine-binding periplasmic protein
- N-acetyl-gamma-glutamyl-phosphate reductase
- Amino-acid acetyltransferase
- Argininosuccinate lyase
- D-alanyl-D-alanine dipeptidase
Sequence:
MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPADIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPASNAFLQGLRELCNRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECARVMTVGTHGTTYGGNPLASAVAGKVLELINTPEMLNGVKQRHDWFVERLNTINHRYGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS
Protein: Calcium up-regulated protein D (Q54BF5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May play an important role in stabilizing and/or regulating the cell membrane during Ca(2+) stress or certain stages of development.
Subcellular location: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MINIEDISKSSNQSEEKQLKSTSTSSKPKYSFVAKSLFKGSNNITPYYLSTSNTFQCVASESIQTWLLSDDGHIFTSSGNFVLDVSSGGYFVELVQLNSNSKTQIWTIDTTNNKIQPGNGKYLDIDSLNICVAPLNGNATQKWTTFRRAPIPTGNWGYFQSKQLDSNNNYWGLSVLNNSTSYNTSVVMNKVQAKSIGQIWQMTNDGHILSRLDGNLVLDIGPSIDGSKTNYHLNTNVYKANDLMQQWGINENNQIFNQYYPNLCIGFVGELGVDSTVNCVLAQPSSASDINFQWIANPTYSLNQIVSEVPEPFPAYTSGDLLASYQYLSDDATNGYTDDIRSLYTSINVNLEIFYVNVTNATCPSSIHSTEDFSYVQNQIKNELTYAINVRLVFDNYSGFYSKLFSQGSTNLTNLANLINVDMSSDQVVNGDYTDAITSVFYAIISEIPIGGSIIANISESAVQFGELYAESNDSGPSTYQVTLSKLYDHLNENYENEMANAQRIKNTILQDWGMMSKTFALCFLPTNNPSSLNINGLDFQKISTIASLAYQTAIIQMLLPTNYQIYFTPAGYYAPVSSDDYSYTDSTGTYIMAEIDNCNSHPPKALTGFKTRSFHIFLWLEFSYLCDLLQYGR
Protein: Protein NATD1 (N-acetyltransferase domain-containing protein 1) (Q8N6N6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHSAAAVPLGALEQGCPIRVEHDRRRRQFTVRLNGCHDRAVLLYEYVGKRIVDLQHTEVPDAYRGRGIAKHLAKAALDFVVEEDLKAHLTCWYIQKYVKENPLPQYLERLQP
Protein: Protocadherin 7 (A2RS43)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLRMRTTGWARGWCLGCCLLLPLCFSLAAAKQLLRYRLAEEGPADVRIGNVASDLGIVTGSGEVTFSLESGSEYLKIDNLTGELSTSERRIDREKLPQCQMIFDENECFLDFEVSVIGPSQSWVDLFEGRVIVLDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELLQEPGGGGGSGEGRRLGPADSAPYPGGGGNSASGGGSGGSKRRLDAPEGGGGTSPSGRSSVFELQVADTPDGEKQPQLIVKGALDREQRDSYELTLRVRDGGDPPRSSQAILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRATDLDVGVNGQIEYVFGAATESVRRLLRLDETSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPSIEIRKIGRIPLKDGVANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDTEGDQNKKKYFLHTSAPLDYETTREFNVVIVAVDSGSPSLSSNNSLVVKVGDTNDNPPVFGQSVVEVYFPENNIPGERVATVLATDADSGKNAEIAYSLDSSVMGTFAIDPDSGDILVNTVLDREQTDRYEFKVNAKDKGIPVLQGSTTVIVQVADKNDNDPKFMQDVFTFYVKENLQPNSPVGMVTVMDADKGRNAEMSLYIEENSNIFSIENDTGTIYSTMSFDREHQTTYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPTVTLPRNISYTLLPPSSNVRTVVATVLATDSDDGINADLNYSIVGGNPFKLFEIDSTSGVVSLVGKLTQKHYGLHRLVVQVNDSGQPSQSTTTLVHVFVNESVSNATVIDSQIVRSLHTPLTQDIAGDPSYEISKQRLSIVIGVVAGIMTVILIILIVMMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQMRVHPYITVFG
Protein: Cell surface glycoprotein CD200 receptor 2 (CD200 cell surface glycoprotein receptor-like 2) (CD200 receptor-like 2) (HuCD200R2) (CD200 cell surface glycoprotein receptor-like a) (CD200RLa) (Cell surface glycoprotein CD200 receptor 1-like) (Cell surface glycoprotein OX2 receptor 2) (Q6Q8B3)
Organism: Homo sapiens (Human)
Function: May be a receptor for the CD200/OX2 cell surface glycoprotein.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSAPRLLISIIIMVSASSSSCMGGKQMTQNYSTIFAEGNISQPVLMDINAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETKETNCTVERITWVSRPDQNSDLQIRPVDTTHDGYYRGIVVTPDGNFHRGYHLQVLVTPEVNLFQSRNITAVCKAVTGKPAAQISWIPEGSILATKQEYWGNGTVTVKSTCPWEGHKSTVTCHVSHLTGNKSLSVKLNSGLRTSGSPALSLLIILYVKLSLFVVILVTTGFVFFQRINHVRKVL
Protein: Dentin matrix acidic phosphoprotein 1 (DMP-1) (Dentin matrix protein 1) (AG1) (P98193)
Organism: Rattus norvegicus (Rat)
Function: May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Matrix extracellular phosphoglycoprotein
- Matrix metalloproteinase-9
- Phosphate regulating endopeptidase X-linked
- Dentin sialophosphoprotein
- Integrin-binding sialoprotein
- Fibroblast growth factor 23
- Osteopontin
- Sclerostin
- Amelotin
- Parathyroid hormone
Sequence:
MKTVILLTFLWGLSCALPVARYQNTESESSEERTGNLAQSPPPPMANSDHTDSSESGEELGSDRSQYRPAGGLSKSAGMDADKEEDEDDSGDDTFGDEDNGPGPEERQWGGPSRLDSDEDSADTTQSSEDSTSQENSAQDTPSDSKDHHSDEADSRPEAGDSTQDSESEEYRVGGGSEGESSHGDGSEFDDEGMQSDDPGSTRSDRGHTRMSSAGIRSEESKGDHEPTSTQDSDDSQDVEFSSRKSFRRSRVSEEDDRGELADSNSRETQSVSTEDFRSKEESRSETQEDTAETQSQEDSPEGQDPSSESSEEAGEPSQESSSESQEGVASESRGDNPDNTSQTGDQRDSESSEEDRLNTFSSSESQSTEEQGDSESNESLSLSEESQESAQDEDSSSQEGLQSQSASRESRSQESQSEQDSRSEENRDSDSQDSSRSKEESNSTGSTSSSEEDNHPKNIEADNRKLIVDAYHNKPIGDQDDNDCQDGY
Protein: T-box transcription factor TBX3 (T-box protein 3) (Q7TST9)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor involved in developmental processes (By similarity). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (By similarity). Probably plays a role in limb pattern formation (By similarity). Required for mammary placode induction, involved in maintenance of the mammary buds during development and branching morphogenesis in embryonic and adult glands; partially redundant with TBX2 (By similarity). Involved in modulating early inner ear development, acting independently of, and also redundantly with, TBX2 in different subregions of the developing ear (By similarity). Acts as a negative regulator of PML function in cellular senescence (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Steroid hormone receptor ERR2
- Homeobox protein Nkx-2.5
- Homeobox protein NANOG
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- POU domain protein
- Short stature homeobox protein 2
- KLF transcription factor 4
- Transcription factor GATA-4
Sequence:
MSLSMRDPVIPGTSMAYHPFLPHRAPDFAMSAVLGHQPPFFPALTLPPNGAAALSLPGALAKPIMDQLVGAAETGIPFSSLGPQAHLRPLKTMEPEEDVEDDPKVHLEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFTLAFPSDHATWQGNYSFGTQTILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLQSMRVFDERHKKETGTSDESSSEQAAFNCFAQASSPAVSTVGTSNLKDLCPSEAESDAEAESKEEHGPEACDTAKISTTTAEEPGRDKGSPATRAQLFPAEPSRARDTARLDKASPDSRHSPATISSSTRVPGADEHRSPGREGPVSAKVDEARALPAKDAFAPLSVQTDATAHLTQGPLPGLGFAPGLAGQQFFNGHPLFLHPGQFAMGGAFSSMAAGMGPLLATVSGASTGVSGLDSTAMASAAAAQGLSGASAATLPFHLQQHVLASQGLAMSPFGSLFPYPYTYMAAAAAASSAAASSSVHRHPFLNLNSMRPRLRYSPYSIPVPVPDSSSLLATALPSMASAAGPLDGKSAVLAASPASVAVDSGSELNSRSSTLSSGSVSLSPKLCSEKEAATSELQSIQRLVSGLEAKPDRSCSGSP
Protein: Dipeptidase 1 (EC 3.4.13.19) (Beta-lactamase) (EC 3.5.2.6) (Microsomal dipeptidase) (Renal dipeptidase) (P31430)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P16444}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P16444}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}.
Interaction partners:
- Methyl-CpG-binding protein 2
- Histone deacetylase 1
- Histone deacetylase 1
- Chromodomain-helicase-DNA-binding protein 4
Sequence:
MLIIWWFWSLLAICASDSFRNQAENIMRTTPVIDGHNDLPWQMLTLFNNQLRKSEANLSALAETHTNIPKLRAGFVGGQFWSAYMPCDTQNKDAVKRILEQIDVIHRMCQLYPETFECVTNSSDILQAFRRGKVASLIGVEGGHLIDSSLGVLRTLYHLGMRYLTLTHNCNTPWADNWLVDKGDDEAESQGLSPFGKLVLNEMNRLGVMIDLSHVSVATMKDALQLSKAPVIFSHSSAYSVCPHRRNVPDDVLQLVKSTNSLVMVNFYNQFVSCSDSATLSQVADHLDHIKKVAGAGAVGLGGDYDGVTNLPVGLEDVSKYPDLIAELLRRNWTETEVRGLLAENLLRVFSAVELVSNIMQVPEEETIPVEKLDGSCRTFYGHSRAPSIHLQIGALLASLASLVFSLHLL
Protein: Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2) (F8VQW8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSPVRRCVYFSEDICDCFDLVSVFFRLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH
Protein: Large ribosomal subunit protein mL50 (39S ribosomal protein L50, mitochondrial) (L50mt) (MRP-L50) (Q8N5N7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL63
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein mL53
- Large ribosomal subunit protein bL19m
Sequence:
MAARSVSGITRRVFMWTVSGTPCREFWSRFRKEKEPVVVETVEEKKEPILVCPPLRSRAYTPPEDLQSRLESYVKEVFGSSLPSNWQDISLEDSRLKFNLLAHLADDLGHVVPNSRLHQMCRVRDVLDFYNVPIQDRSKFDELSASNLPPNLKITWSY
Protein: SWR1-complex protein 3 (P31376)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Vacuolar protein sorting-associated protein 71
- Vacuolar protein sorting-associated protein 72
- SWR1-complex protein 5
- Helicase SWR1
- RuvB-like protein 1
- SWR1-complex protein 7
- Actin-like protein ARP6
- SWR1-complex protein 4
- RuvB-like protein 2
- Protein AF-9 homolog
Sequence:
MPAVLRTRSKESSIEQKPASRTRTRSRRGKRGRDDDDDDDDEESDDAYDEVGNDYDEYASRAKLATNRPFEIVAGLPASVELPNYNSSLTHPQSIKNSGVLYDSLVSSRRTWVQGEMFELYWRRPKKIVSESTPAATESPTSGTIPLIRDKMQKMCDCVMSGGPHTFKVRLFILKNDKIEQKWQDEQELKKKEKELKRKNDAEAKRLRMEERKRQQMQKKIAKEQKLQLQKENKAKQKLEQEALKLKRKEEMKKLKEQNKNKQGSPSSSMHDPRMIMNLNLMAQEDPKLNTLMETVAKGLANNSQLEEFKKFIEIAKKRSLEENPVNKRPSVTTTRPAPPSKAKDVAEDHRLNSITLVKSSKTAATEPEPKKADDENAEKQQSKEAKTTAESTQVDVKKEEEDVKEKGVKSEDTQKKEDNQVVPKRKRRKNAIKEDKDMQLTAFQQKYVQGAEIILEYLEFTHSRYYLPKKSVVEFLEDTDEIIISWIVIHNSKEIEKFKTKKIKAKLKADQKLNKEDAKPGSDVEKEVSFNPLFEADCPTPLYTPMTMKLSGIHKRFNQIIRNSVSPMEEVVKEMEKILQIGTRLSGYNLWYQLDGYDDEALSESLRFELNEWEHAMRSRRHKR
Protein: At5g11330 (FAD/NAD(P)-binding oxidoreductase family protein) (Q9LFM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGKKKGKAIIVGGSIAGLSCAHSLTLACWDVLVLEKSSEPPVGSPTGAGLGLDPQARQIIKSWLTTPQLLDEITLPLSIDQNQTTDSEKKVTRILTRDEDFDFRAAYWSDIQSLLYNALPQTMFLWGHKFLSFTMSQDESNVKVKTLVVETQETVEIEGDLLIAADGCLSSIRKTFLPDFKLRYSGYCAWRGVFDFSGNENSETVSGIKKVYPDLGKCLYFDLGEQTHSVFYELFNKKLNWIWYVNQPEPDLKSNSVTLKVSQEMINKMHQEAETIWIPELARLMSETKDPFLNVIYDSDPLERIFWGNIVLVGDAAHPTTPHGLRSTNMSILDAEVLGKCLENCGPENVSLGLEEYQRIRLPVVSEQVLYARRLGRIKQGLDHDGIGDGVFGLEQRNMPFFSCAPLI
Protein: V-type proton ATPase subunit E (V-ATPase subunit E) (V-ATPase 26 kDa subunit) (Vacuolar proton pump subunit E) (P54611)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit G
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase subunit F 1
- Probable V-type proton ATPase subunit d 2
Sequence:
MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQQQRLKIMEYYEKKEKQVELQKKIQSSNMLNQARLKVLKVREDHVSSVLDDARKRLGEVTKNQSEYETVLTKLIVQGLFQIMEPKVILRCREVDVPLVRNVLPAAVEQYKAQINQNVELFIDEKDFLSADTCGGVELLALNGRIKVPNTLESRLDLISQQLVPEIRNALFGRNVNRKFTD
Protein: Homeobox protein Hox-D9 (Homeobox protein Hox-4C) (Homeobox protein Hox-5.2) (P28356)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-D10
- Homeobox protein Hox-D8
- Homeobox protein Hox-D3
- Homeobox protein Hox-D11
- Homeobox protein Hox-D13
Sequence:
MLGGSAGRLKMSSSGTLSNYYVDSLIGHEGDEVFAARFGPPGPGAQGRPAGVADGPAATAAEFASCSFAPRSAVFSASWSAVPSQPPAAAAMSGLYHPYVPPPPLAASASEPGRYVRSWMEPLPGFPGGAGGGGGGGGGGPGRGPSPGPSGPANGRHYGIKPETRAAPAPATAASTTSSSSTSLSSSSKRTECSVARESQGSSGPEFSCNSFLQEKAAAATGGTGPGAGIGAATGTGGSSEPSACSDHPIPGCSLKEEEKQHSQPQQQQLDPNNPAANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARILNLTERQVKIWFQNRRMKMKKMSKEKCPKGD
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 (Complex I-B17) (NADH-ubiquinone oxidoreductase B17 subunit) (A0A087WZX2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298}; Matrix side {ECO:0000256|ARBA:ARBA00004298}.
Interaction partners:
Sequence:
MTGYTPDEKLRLQQLRELRRRWLKDQELSPREPVLPPQKMGPMEKFWNKFLENKSPWRKMEKPYGIVEKKSRIFPGDTILETGEVIPPMKEFPDQHH
Protein: Zinc finger protein 819 (D3Z4F2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAADMNFCQKLQRLGTEEQDGPCERLVSFEDVTVNFSQEEWQHLDSAQRRLYQDVLLEIYSHLLVVGYSRPEVILKMKKVKDSPMGKVDFPHQRCGQGE
Protein: PWP2 periodic tryptophan protein homolog (Yeast) (PWP2 small subunit processome component) (Q7ZUV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MKFAYKFSNLLGAFYRQGNISFSKNGDSVISPVGNRISVFDLKNNKSETLPVSTSKNIACFDISPDGNLAILIDEDGAAILVSLVTRAVLHHHHFHNPVHNVSFSPDGRKFVVTKENVALMYHAPGRNKEFNAFALNKTFYGPFDEMTCIDWTDDSKCFAVGSKDMTTWIFGAERWANLIYYSLGGHKDIIVGCFFEKDSLDMYTVSQEGTLCIWESDTDLEGLRKGPKYAERKEKEQKKLRVLEMEEDEANDIEIMGEDEETRGDVIKGSAETPEEVEGIKNVRYLQKSKYYFNKEGDFNKLTAAAFHKRTHILVTGFASGAFHLHELPGFDLIHSLSISDQRISAISLNPTGDWISFGCSGLGQLLVWEWQSESYVFKQQGHFNNMNSLAYSPDGQYLATGGDDGKVKVWNTNSGLCFVTFTEHSSGVTEVAFTSSGFVVVSASLDGTVRAFDLHRYRNFRTMTSPRPAQFSSLAVDGSGELVCAGSQDSFEIFLWSMQTGRLLEVLSGHEGPVSNLCFSPVQSVLASVSWDKTVRLWDMLDSWQTKETLQLTSDGLAVTYHPNGMELAVASLDGEITFWNPQTGRQTGSITGRHDLQMGRKESEKITAKQSAKGKSFTTLCYSADGESILTGGKSKFVCIYNIKEHLLMKKFEISCNLSLDAMEEFLDRRKMTEFGSLSLVDEGTGDGNGVELSLPGVKKGDMSTRCFKPEISVSSLRFSPTGRSWAAASTEGLLIYSLDAALVFDPYDLDIDVTPTSIRQQITKKEWASAILLFFRLNEILLIREVLEAIPFDQITVVCSSLPDVYVDKLLNFVASTLEKSNHLQFYLTWAQCLLTLHGQKLKNRPGFVLPTVQQLLKSIQRHSDDLSKLCDWNIYNIRYAAALAKQRGLKRTASEIYGAEKEDSSEAMDSEGDEENVTNEPIMLENAIQLSD
Protein: F5O8.30 protein (Nucleic acid-binding, OB-fold-like protein) (Q9ZUC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F11M21.26 protein
- Uncharacterized protein At4g28440
- Nucleic acid-binding, OB-fold-like protein
- Expressed protein
- Replication protein A 70 kDa DNA-binding subunit A
- Replication protein A 70 kDa DNA-binding subunit B
- Replication protein A 70 kDa DNA-binding subunit C
- Replication protein A 70 kDa DNA-binding subunit D
- Replication protein A 14 kDa subunit A
- Replication protein A1
Sequence:
MADSTKAGLKKPAFTKVDQLRPGTSGHNVNVKIVSTKMVLQKGRADGPQARQLRISECIVGDETGVIVFTARNDQVDLMKEGSTVTLRNAKIDMYKGSMRLAVDKWGRVEVTEPASFKVKEDTNMSLIEYELVNVVE
Protein: Proteasome subunit alpha type-6 (20S proteasome subunit alpha-1) (Q9XZJ4)
Organism: Drosophila melanogaster (Fruit fly)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- Proteasome subunit beta
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-2
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit beta
Sequence:
MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAIAQENITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVVSKSDPTFRILDEREIEEHLTKIAEKD