wanglab/gogpt-training-data huggingface dataset:
Protein: Senescence-associated protein AAF, chloroplastic (Protein ARABIDOPSIS A-FIFTEEN) (Q9C8Y4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in modulation of redox homeostasis to regulate leaf senescence mediated by age and stress factors during plant development. Its function is dependent of EIN2, a central factor of ethylene signaling.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21940719}.
Interaction partners:
- IQ-domain 21
- Quinolinate synthase, chloroplastic
Sequence:
MALNVSKVVPNSPILVKSVNASRSRRVLLAYVHHPLAANKGSSIEELKQGLCCTKTVTFVSSRRCSTLCFVGKSQDTETNSQVVQKEGEKQVMPRRKSSNSSQLLVEYVSNDAKFVNERARNDFVLLSRGIMRLDARARQDVAILGSGFLKLDARAREDTEKIDRDVKRKAERLHHIATIFKNIAESKLKNAADKHWSDGALEADLRRADFRAKQRAMEDALMALEFIKNIHDMMVNKMVDSLVTSETGTTDRISLEKNGIALGFFPGEVSSDRISAIEEAYKSMASALSEADGIDYTDPEELELLVTTLIDLDAMDGKSSASLLAECSSSPDVNTRKALANALAAAPSMWTLGNAGMGALQRLAEDSNPAIAAAASRAINALKKQWEVEEGDSLRFMMNFERPNDDDDVDSDLDEI
Protein: 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Liver perchloric acid-soluble protein) (L-PSP) (Reactive intermediate imine deaminase A homolog) (Translation inhibitor L-PSP ribonuclease) (UK114 antigen homolog) (rp14.5) (P52759)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P52758}. Nucleus {ECO:0000250|UniProtKB:P52758}. Peroxisome {ECO:0000269|PubMed:11003673}. Mitochondrion {ECO:0000269|PubMed:17416349}. Note=Mostly cytoplasmic but, in less differentiated cells occasionally nuclear. {ECO:0000250|UniProtKB:P52758}.
Interaction partners:
- YTH domain-containing family protein
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 4
- CCR4-NOT transcription complex subunit 1
- L-serine dehydratase/L-threonine deaminase
- Serine dehydratase-like
- Exosome component 7
Sequence:
MSSIIRKVISTSKAPAAIGAYSQAVLVDRTIYVSGQIGMDPSSGQLVPGGVAEEAKQALKNLGEILKAAGCDFTNVVKTTVLLADINDFGTVNEIYKTYFQGNLPARAAYQVAALPKGSRIEIEAIAVQGPFTTAGL
Protein: Ceramide-1-phosphate transfer protein (Glycolipid transfer protein domain-containing protein 1) (J3KST3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004150}. Nucleus outer membrane {ECO:0000256|ARBA:ARBA00004509}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004509}.
Interaction partners:
Sequence:
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSKLRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHW
Protein: Phospholamban (PLB) (P61012)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. Controls intracellular Ca(2+) levels in elongated spermatids. May play a role in germ cell differentiation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:A4IFH6}; Single-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P61014}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HAX1 at the endoplasmic reticulum. Colocalizes with DMPK at the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:P26678}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Calcium-transporting ATPase
- Calcium-transporting ATPase
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein kinase cAMP-activated catalytic subunit beta
- cGMP-dependent protein kinase.
- cGMP-dependent protein kinase.
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Sequence:
MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLILICLLLICIIVMLL
Protein: Troponin C, slow skeletal and cardiac muscles (TN-C) (P63316)
Organism: Homo sapiens (Human)
Function: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
Interaction partners:
- Troponin T, cardiac muscle
- Troponin I, fast skeletal muscle
- Troponin I, cardiac muscle
- Troponin I, slow skeletal muscle
- Troponin T, slow skeletal muscle
- Troponin T, fast skeletal muscle
- Tropomyosin alpha-1 chain
- Tropomyosin alpha-3 chain
- Actin, alpha skeletal muscle
- Troponin C, skeletal muscle
Sequence:
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Protein: Divalent metal ion transporter (Q5ACZ8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Mitochondrial thiamine pyrophosphate carrier 1
- Ccc1p
Sequence:
MNQQQQQPLLKRVAHSVKKYATFIGPGLVVSVSYMDPGNYSTSVSSGSMYQYKLCFIIFMANLFAIILQALCVKLGTITGLDLAEMCRLHLNPKLNLFMYFCAEIAIIATDLAEVVGTAISLEILFGIPLLYGVVITVLDVLIILMAYHKDGSMKQTKFFEILVSILVAATCVCFILELFKCNFEPGSGWKIFKGFLPVNKEIFKESMALFLSCAIVGSTVMPHSLFLGSALVQPRLKEYDETHGTKANVLPVENEDTTRLVPPHQPVEGSRLRRISDGSLLTNKYKPSYAAIKYCLNYSYVELVSSLFIVAVFVNSAILIVAGSTLYGKPDAADADLLSIYEMLSYYISPAAGLVFALSMLFSGQSAGIVCTMAGQIISEGFINWTLEPWKRRIITRVLAIVPVIVVVGILGREGVSKVMNSSQVVLSFILPIVSAPLIYFTSKKEFMTVIDTSSTDESTPLLEENDLDEQIPVKKISFENGSLLRNASILTWVIITGLNVYLIIAFANGADI
Protein: Rhodopsin (F1P3Y2)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MNGTEGQDFYVPMSNKTGVVRSPFEYPQYYLAEPWKFSALAAYMFMLILLGFPVNFLTLYVTIQHKKLRTPLNYILLNLAVADLFMVFGGFTTTMYTSMNGYFVFGVTGCYIEGFFATLGGEIALWSLVVLAVERYVVVCKPMSNFRFGENHAIMGVAFSWIMAMACAAPPLFGWSRYIPEGMQCSCGIDYYTLKPEINNESFVIYMFVVHFMIPLAVIFFCYGNLVCTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTNQGSDFGPIFMTIPAFFAKSSAIYNPVIYIVMNKQFRNCMITTLCCGKNPLGDEDTSAGKTETSSVSTSQVSPA
Protein: Secretory 31, isoform D (A0A0B4LEZ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- small monomeric GTPase
- Secretory 24AB, isoform A
- Protein SEC13 homolog
- Protein transport protein SEC23
- Secretory 16, isoform I
- Secretory 24CD, isoform C
- FI09914p
- Coatomer subunit alpha
- LD21067p)
- Transport and Golgi organization protein 1
Sequence:
MKIKELQKTVNIAWSPAQQQQILLAAGTAAQQFDSNANSTLELYSPNFSDATYDLELRASVSSQYKFQKLIWSPVGPHPSGLIVGGCEAGQINIYSADKLLAGKEEPLLKRQDKHTGAVSGLDFNPFQNNLLASCASESEILIWDLNNPETSMSPGTKTQPLEDVKNVAWNRQVQHILASVFSTRCVIWDLRKSQQIIKLSDSQSRVRWHAIEWHPEAATQVWLASEDDQAPVVQLWDLRYATAPAKTYQIHERGVLGMSWCLQDNDLMVSCGKDNRIYCWNPNTKIPEGEILSEVATTASWYSDVQFCPRNPALIASASLEGAVSIYSLHGGTHHLVQTANKIADSFPGMDQFAQEPIPQQATQVVYHDLAHAPKWMKRPCGVAFGFGGKLVSFNGTSKTVKVQQLTTESALVDRANALERSLVDANYSDYCRQRADETPDQHGRYIWYFIKANFELNPKEEMLNLLGYNKDDIDSKFNKFIKETDGNSHSDVDTLTTRISTLTHSDSSEVECDQSTNYSTDNSQTQDNKFDGNAIDSQNHNDFATPPRPQFKVPSGDHSDSLIAEAILTGNVDAAVELCLEAQRIPEALIIASTAGIETLNRTQTRYLLQQKNELSHVISALVSRDWLDFVNRCTVDSWKEALVAALKHSERKVVDICERLGDRLLSECASSAEFTRNAMLCYICAGSIDKLVTAWYQLKRLEQQNPGYKPNTTELQDLAEMVMLMCKSLEQQGISVDLAGRFAGFLTEYGGLLASQGALTAALQYITTLGGGAAASESDVLQSLRDRINNAVNLDYTQPQAAVAAAPHGYQPTRGRGSFSQPQPSAPMPYGQPPNQYAQPSWPAQVPPLQTSYPGAQQPQAPPQIFNPQPVKPEPLAQPPRPLSNASSSGGPPPAGGASSSGGSGLSGRSKYVLDPSVAAPTSSYGMPYNPVPAPVPSAVPFGGGGVPGPAPQPASVPTYNSNAFNTNPIAAAQPYNPSPLMPAQQNQFVPGVNPIETMPPPAVPPVIQNVQRNPTPPPGWNDPPALKSSRAPKPKPVVEPSAAIFHPLFPVDPNQNQNGYVDPSQYQHAAPLGGVPNTYYNPAAFNNNPQQQQQHQQSYLQPQQPAPGIQQPNWQGQQQTIGYTEQPAPIQQQRQPAPPKEKPPLPEEYIYLQTVLEELKNRCLGATNDPRTKRKFVDVVKRLENLYDCLRDGKLTPTTVQYLNQIVQYIQISDYANAMEIHTQIAFGTDFAQCAGFMQGLKVLLQSASELQLVLR
Protein: Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2) (O55026)
Organism: Mus musculus (Mouse)
Function: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity).
Subcellular location: [Isoform Long]: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Cancer-related nucleoside-triphosphatase homolog
- Ectonucleoside triphosphate diphosphohydrolase 1
- Adenylate kinase isoenzyme 1
- Nucleoside diphosphate kinase 3
- Adenylate kinase 8
- Nucleoside diphosphate kinase homolog 7
- Adenylate cyclase type 5
- Adenylate kinase isoenzyme 5
- Adenylate cyclase type 4
- Adenylate cyclase type 8
Sequence:
MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL
Protein: MHC class I alpha chain 2 (MHC class I glycoprotein) (MHC class I molecule) (O46790)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPCGALGLGLLLAAVCGAAAELHTLRYIRTAMTDPGPGQPWFVTVGYVDGELFVHYNSTARRYVPRTEWIAANTDQQYWDGQTQIGQLNEQINRENLGIRQRRYNQTGGSHTVQWMFGCDILEDGTIRGYRQSAYDGRDFIALDKDMKTFTAAVPEAVPTKRKWEEESEPERWKNYLEETCVEWLRRYVEYGKAELGRRERPEVRVWGKEADGILTLSCRAHGFYPRPIVVSWLKDGAVRGQDAHSGGIVPNGDGTYHTWVTIDAQPGDGDKYQCRVEHASLPQPGLYSWEPPQPNLVPIVAGVAVAIVAIAIVVGVGFIIYRRHAGKKGKGYNIAPDREGGSSSSSTGSNPTI
Protein: Protein CROWDED NUCLEI 1 (Protein KAKU2) (Protein LITTLE NUCLEI 1) (F4HRT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape).
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}; Peripheral membrane protein {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:24667841}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (PubMed:24667841). Mostly localized at the nuclear periphery and, to a lesser extent, in the nucleoplasm (PubMed:17873096). Localized on the condensing chromatin during prometaphase to anaphase, but transferred from the decondensing chromatin to the reassembling nuclear envelope during early telophase. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}.
Interaction partners:
- SUN domain-containing protein 1
- SUN domain-containing protein 2
- Protein KAKU4
- Protein NTM1-like 9
- Nuclear pore complex protein NUP1
- Nuclear envelope-associated protein 1
- SUN domain-containing protein 3
- WPP domain-interacting tail-anchored protein 1
- WPP domain-interacting tail-anchored protein 2
- SUN domain-containing protein 4
Sequence:
MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEWSSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANALVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQEGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKARELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALDRKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTEEERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERLKKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLFEEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSRFLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKMLKLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVAADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRKRGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEEGIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKVSIGKKLWTFLTT
Protein: Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1) (A2A5K6)
Organism: Mus musculus (Mouse)
Function: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23178126}.
Interaction partners:
- Ankyrin repeat and LEM domain-containing protein 2
Sequence:
MEENEVESSSDAAPRPGQPEEPSESGLGVCTSEAVSADSSDAATVPGLTEADDSGVGQSSDGGNHSVEEVSESISTDPLPHGCLPDSSSVSRGPVAEMPGGPPALVHSSVLPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSACLEPPEEPQGDPSSVAQQPPAPVTEELDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAAAAAATGKRGRVRKWGTSTKTTEEDRPEEEEEDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTPRPRRRPGRPRKLPRLETSDLHDGVGQPLVSSQSTQSPPELQDLEAPSSSGLRALGKVGRGLVESGVSQSDAENAAPSCQDEADAPPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPYLCRICGSRFLSHEDLRFHVNSHEAGDPQLFRCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSQDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHANSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSTAPGPPLSSPGPEAPQEPAPFQSPETPPLLCPDALGGTTIIYQQGAEESTAVATQTALDLLLNMSAQRELGATALQVAVVKSEGIEAELTSTGGQPSPEDTTPRVVTLHMAESGSSVAAESQLGPSDLQQIALPSGPFGGASYSVITAPPVEGRTSASGPPYREEPPGEAAQAVVVSDTLKEAGTHYIMAADGTQLHHIELTADGSISFPSPDTLAPGTKWPLLQCGGPPRDGSEVLSPTKTHHMGGSQGSSTPPPAASHTLGLVVPQSPPSAAASSTKKFSCKVCSEAFPSRAEMESHKRAHAGPAAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCNQCSFASKNKKDLRRHMLTHTNEKPFSCHVCGQRFNRNGHLKFHIQRLHSIDGRKTGTSTARAPAQTIILNSEEETLATLHTAFQSSHGVLGTERLQQALSQEHIIVAQEQTVTNQEEATYIQEITADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPDGHHIQVQEGQITHIQYEQGTPFLQESQIQYVPVSPSQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTEEAVPEQIHQLQHQGIEYDVITLSDD
Protein: Embryonic abundant protein 1 (P46520)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Em protein may act as a cytoplasm protectant during desiccation.
Interaction partners:
- Os01g0314700 protein
- Kinesin-like protein KIN-14I
Sequence:
MASGQQQQGRSELDRMAREGQTVVPGGTGGKSLEAQENLAEGRSRGGQTRKEQMGEEGYREMGRKGGLSTGDESGGERAAREGIDIDESKYKTKS
Protein: Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2) (Q9LSZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1 constitutes the catalytic core. Involved in the regulation of the programmed cell death (PCD) signaling pathway. Plays an important role during male gametogenesis and embryogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11726713}; Single-pass membrane protein {ECO:0000269|PubMed:11726713}.
Interaction partners:
- Long chain base biosynthesis protein 1
- 3-dehydrosphinganine reductase TSC10B
- 3-dehydrosphinganine reductase TSC10A
- At5g42000
- ORMDL family protein
- Ceramide kinase
- Alkaline ceramidase
- Ceramide synthase LOH2
- Sphinganine C4-monooxygenase 1
- Sphinganine C4-monooxygenase 2
Sequence:
MITIPYLTAVSTYFSYGLLFAFGQLRDFFRRFIDWWFTSNLQGYAPICLGHEDFYIRRLYHRIQDCFERPISSAPDAWFDVVERYSNDNNKTLKRTTKTSRCLNLGSYNYLGFGSFDEYCTPRVIESLKKFSASTCSSRVDAGTTSVHAELEECVTRFVGKPAAVVFGMGYATNSAIIPVLIGKGGLIISDSLNHSSIVNGARGSGATIRVFQHNTPSHLERVLREQIAEGQPRTHRPWKKIIVVVEGIYSMEGEICHLPEVVAICKKYKAYVYLDEAHSIGAIGKTGKGICELLGVDTADVDVMMGTFTKSFGSCGGYIAGSKELIQYLKHQCPAHLYATSIPTPSAQQIISAIKVILGEDGSNRGAQKLARIRENSNFFRAELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLRQKVAVVVVGFPATPLLLARARICISASHSREDLIRALKVISKVGDLSGIKYFPAEPKKIEQSKNDIKLD
Protein: Sodium/hydrogen exchanger 4 (Na(+)/H(+) exchanger 4) (NHE-4) (Solute carrier family 9 member 4) (Q6AI14)
Organism: Homo sapiens (Human)
Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying cell volume in response to extreme fluctuations of hyperosmolar-stimulated cell shrinkage. Is relatively amiloride and ethylisopropylamiloride (EIPA) insensitive. Can be activated under conditions of hyperosmolar-induced cell shrinkage in a sustained intracellular acidification-dependence manner. Activated by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) in a sustained intracellular acidification-dependence manner. Affects potassium/proton exchange as well as sodium/proton and lithium/proton exchange. In basolateral cell membrane, participates in homeostatic control of intracellular pH, and may play a role in proton extrusion in order to achieve transepithelial HCO3(-) secretion. In apical cell membrane may be involved in mediating sodium absorption. Requires for normal levels of gastric acid secretion, secretory membrane development, parietal cell maturation and/or differentiation and at least secondarily for chief cell differentiation (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:P26434}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q8BUE1}; Multi-pass membrane protein {ECO:0000255}. Zymogen granule membrane {ECO:0000250|UniProtKB:P26434}; Multi-pass membrane protein {ECO:0000255}. Note=Enrichment at apical or basolateral membrane may be tissue-dependent. {ECO:0000250|UniProtKB:P26434}.
Interaction partners:
- Sodium/hydrogen exchanger 1
Sequence:
MALQMFVTYSPWNCLLLLVALECSEASSDLNESANSTAQYASNAWFAAASSEPEEGISVFELDYDYVQIPYEVTLWILLASLAKIGFHLYHRLPGLMPESCLLILVGALVGGIIFGTDHKSPPVMDSSIYFLYLLPPIVLEGGYFMPTRPFFENIGSILWWAVLGALINALGIGLSLYLICQVKAFGLGDVNLLQNLLFGSLISAVDPVAVLAVFEEARVNEQLYMMIFGEALLNDGITVVLYNMLIAFTKMHKFEDIETVDILAGCARFIVVGLGGVLFGIVFGFISAFITRFTQNISAIEPLIVFMFSYLSYLAAETLYLSGILAITACAVTMKKYVEENVSQTSYTTIKYFMKMLSSVSETLIFIFMGVSTVGKNHEWNWAFICFTLAFCQIWRAISVFALFYISNQFRTFPFSIKDQCIIFYSGVRGAGSFSLAFLLPLSLFPRKKMFVTATLVVIYFTVFIQGITVGPLVRYLDVKKTNKKESINEELHIRLMDHLKAGIEDVCGHWSHYQVRDKFKKFDHRYLRKILIRKNLPKSSIVSLYKKLEMKQAIEMVETGILSSTAFSIPHQAQRIQGIKRLSPEDVESIRDILTSNMYQVRQRTLSYNKYNLKPQTSEKQAKEILIRRQNTLRESMRKGHSLPWGKPAGTKNIRYLSYPYGNPQSAGRDTRAAGFSDDDSSDPGSPSITFSACSRIGSLQKQEAQEIIPMKSLHRGRKAFSFGYQRNTSQEEYLGGVRRVALRPKPLFHAVDEEGESGGESEGKASLVEVRSRWTADHGHGRDHHRSHSPLLQKK
Protein: Alpha/beta hydrolase domain-containing protein 17B (Abhydrolase domain-containing protein 17B) (EC 3.1.2.22) (Q6AY17)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards DLG4/PSD95. Has depalmitoylating activity towards GAP43. Has depalmitoylating activity towards MAP6. Has depalmitoylating activity towards NRAS.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Recycling endosome membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Cell projection, dendritic spine {ECO:0000269|PubMed:27307232}. Postsynaptic density membrane {ECO:0000269|PubMed:27307232}.
Interaction partners:
- Acyl-protein thioesterase 1
- GTPase NRas
Sequence:
MNNLSFSELCCLFCCPPCPGKIASKLAFLPPDPTYTLMCDESGSRWTLHLSERADWQYSSREKDAIECFMTRTSKGNRIACMFVRCSPNAKYTLLFSHGNAVDLGQMSSFYIGLGSRINCNIFSYDYSGYGASSGKPTEKNLYADVEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYESAAVILHSPLTSGMRVAFPDTKKTYCFDAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHNDVELYGQYLERLKQFVSQELVNL
Protein: Chlorite dismutase (B1AAM3)
Organism: Stutzerimonas chloritidismutans (Pseudomonas chloritidismutans)
Interaction partners:
Sequence:
MTNMSIRSFKLSLAATAIGAAIAMASSPVVAQQAMQPMQPMKIERGTILTQPGVFGVFTMFKLRPDWSKVPAMERKSAAEEVKKLIEKHKDNVLVDLYLTRGLETNSDFFFRIHAYDLAKAQTFMREFRSTTVGKNADVFETLVGVTKPLNYISKDKSPELNAGLTSATYSGPAPRYVIVIPVKKNAEWWNMSPEERLKEMEVHTTPTLAYLVNVKRKLYHSTGLDDTDFITYFETDDLTAFNNVVLSLAQVKENKFHVRWGSPTTLGTIHSPEDVIKALAE
Protein: F2J10.10 protein (Tubulin alpha-6 chain) (Q9LPM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 16S rRNA
- Beta-glucosidase 14
- Beta-glucosidase 15
- Probable serine/threonine-protein kinase PBL19
- At2g42780/F7D19.22
- BTB/POZ domain-containing protein At3g44820
- Mitogen-activated protein kinase kinase kinase 3
- Lysine-specific demethylase JMJ26
Sequence:
MASSSLEIVKLCGSPVSFPRHKSPIKLECRKRVFRLPNSRSWHRLRVSSSALNGGDNQSKGEEPPESLFMKELKRRGMTPTSLLQDYEVDQDEIKTGKETGNSSKTTATTPAFDKSLLNQRERSLALNSEGLEGLIPRARILLTIGGTFFLGFWPLIVLTLGAFSALYLYFGADFIHDGSRTPVSPPPYIDPYALLEDERISGMDPRLN