wanglab/gogpt-training-data huggingface dataset:
Protein: Plasma membrane ATPase (EC 7.1.2.1) (A0A1D8PJ01)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362083}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Inorganic pyrophosphatase
- inorganic diphosphatase
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Actin
- Lysine/arginine permease CAN1
Sequence:
MSATEPTNEKVDKIVSDDEDEDIDQLVADLQSNPGAGDEEEEEENDSSFKAVPEELLQTDPRVGLTDDEVTKRRKRYGLNQMAEEQENLVLKFVMFFVGPIQFVMEAAAVLAAGLEDWVDFGVICALLLLNAFVGFIQEYQAGSIVDELKKTLANSALVVRNGQLVEIPANEVVPGDILQLEDGTVIPTDGRIVSEDCLLQVDQSAITGESLAVDKRSGDSCYSSSTVKTGEAFMIVTATGDSTFVGRAAALVNKASAGTGHFTEVLNGIGTTLLVFVIVTLLVVWVACFYRTVRIVPILRYTLAITIIGVPVGLPAVVTTTMAVGAAYLAKKQAIVQKLSAIESLAGVEILCSDKTGTLTKNKLSLHEPYTVEGVEPDDLMLTACLAASRKKKGLDAIDKAFLKSLINYPRAKAALPKYKVIEFQPFDPVSKKVTAIVESPEGERIICVKGAPLFVLKTVEDDHPIPEDVHENYQNTVAEFASRGFRSLGVARKRGEGHWEILGIMPCMDPPRDDTAATVNEARRLGLRVKMLTGDAVGIAKETCRQLGLGTNIYDADRLGLSGGGDMAGSEIADFVENADGFAEVFPQHKYNAVEILQSRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLELFLGLWIAILNRSLDINLIVFIAIFADVATLAIAYDNAPYDPKPVKWNLPRLWGMSIVLGVILAIGTWITLTTMLLPKGGIIQNFGGLDGILFLQISLTENWLIFVTRAQGPFWSSIPSWQLSGAVLIVDIIATCFTLFGWWSQNWTDIVTVVRTWIWSFGVFCVMGGAYYLMSTSEAFDNFCNGRKPQQHTDKRSLEDFLVSMQRVSTQHEKST
Protein: ATP-dependent helicase wrn-1 (EC 5.6.2.4) (DNA 3'-5' helicase wrn) (Werner syndrome protein homolog) (Q19546)
Organism: Caenorhabditis elegans
Function: Essential for the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity. May be involved in the control of genomic stability (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14191}.
Interaction partners:
- Exonuclease 1
- DNA repair protein RAD51 homolog
- Crossover junction endonuclease MUS81
- Ku domain-containing protein
- DNA repair endonuclease XPF
- DNA mismatch repair protein S5 domain-containing protein
- Serine/threonine-protein kinase ATR
- DNA topoisomerase 3
- RAD51-like protein 1
- Serine/threonine-protein kinase ATM
Sequence:
MISDDDDLPSTRPGSVNEELPETEPEDNDELPETEPESDSDKPTVTSNKTENQVADEDYDSFDDFVPSQTHTASKIPVKNKRAKKCTVESDSSSSDDSDQGDDCEFIPACDETQEVPKIKRGYTLRTRASVKNKCDDSWDDGIDEEDVSKRSEDTLNDSFVDPEFMDSVLDNQLTIKGKKQFLDDGEFFTDRNVPQIDEATKMKWASMTSPPQEALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGIDAVKLDGHSTQIEWDQVANNMHRIRFIYMSPEMVTSQKGLELLTSCRKHISLLAIDEAHCVSQWGHDFRNSYRHLAEIRNRSDLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNLYISVHSSKDMAEDLGLFMKTDEVKGRHFGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSICRVFWAPKDLNTIKFKLRNSQQKEEVVENLTMMLRQLELVLTTVGCRRYQLLKHFDPSYAKPPTMQADCCDRCTEMLNGNQDSSSSIVDVTTESKWLFQVINEMYNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGKHIPDKWWKALAASLRIAGYLGEVRLMQMKFGSCITLSELGERWLLTGKEMKIDATPILLQGKKEKAAPSTVPGASRSQSTKSSTEIPTKILGANKIREYEPANENEQLMNLKKQEVTGLPEKIDQLRSRLDDIRVGIANMHEVAPFQIVSNTVLDCFANLRPTSASNLEMIDGMSAQQKSRYGKRFVDCVVQFSKETGIATNVNANDMIPPELISKMQKVLSDAVRRVYTEHLISRSTAKEVATARGISEGTVYSYLAMAVEKGLPLHLDKLNVSRKNIAMALNAVRVHLGSNVAVLTPWVEAMGVVPDFNQLKLIRAILIYEYGLDTSENQEKPDIQSMPSTSNPSTIKTVPSTPSSSLRAPPLKKFKL
Protein: Signal-regulatory protein gamma (SIRP-gamma) (CD172 antigen-like family member B) (Signal-regulatory protein beta-2) (SIRP-b2) (SIRP-beta-2) (CD antigen CD172g) (Q9P1W8)
Organism: Homo sapiens (Human)
Function: Probable immunoglobulin-like cell surface receptor. On binding with CD47, mediates cell-cell adhesion. Engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation.
Subcellular location: Membrane {ECO:0000269|PubMed:15383453}; Single-pass type I membrane protein {ECO:0000269|PubMed:15383453}.
Interaction partners:
- Leukocyte surface antigen CD47
- Tyrosine-protein phosphatase non-receptor type substrate 1
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein kinase SYK
- Triggering receptor expressed on myeloid cells 2
Sequence:
MPVPASWPHPPGPFLLLTLLLGLTEVAGEEELQMIQPEKLLLVTVGKTATLHCTVTSLLPVGPVLWFRGVGPGRELIYNQKEGHFPRVTTVSDLTKRNNMDFSIRISSITPADVGTYYCVKFRKGSPENVEFKSGPGTEMALGAKPSAPVVLGPAARTTPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPTGQSVAYSIRSTARVVLDPWDVRSQVICEVAHVTLQGDPLRGTANLSEAIRVPPTLEVTQQPMRVGNQVNVTCQVRKFYPQSLQLTWSENGNVCQRETASTLTENKDGTYNWTSWFLVNISDQRDDVVLTCQVKHDGQLAVSKRLALEVTVHQKDQSSDATPGPASSLTALLLIAVLLGPIYVPWKQKT
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (SMARCE1-related protein) (BRCA2-associated factor 35) (HMG box-containing protein 20B) (HMG domain-containing protein 2) (HMG domain-containing protein HMGX2) (Sox-like transcriptional factor) (Structural DNA-binding protein BRAF35) (Q9P0W2)
Organism: Homo sapiens (Human)
Function: Required for correct progression through G2 phase of the cell cycle and entry into mitosis. Required for RCOR1/CoREST mediated repression of neuronal specific gene promoters.
Subcellular location: Nucleus. Chromosome. Note=Localized to condensed chromosomes in mitosis in conjunction with BRCA2.
Interaction partners:
- REST corepressor 1
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- PHD finger protein 21A
- Histone deacetylase 1
- Histone deacetylase 2
- Genetic suppressor element 1
- Zinc finger protein 217
- Breast cancer type 2 susceptibility protein
- High mobility group protein 20A
- REST corepressor 3
Sequence:
MSHGPKQPGAAAAPAGGKAPGQHGGFVVTVKQERGEGPRAGEKGSHEEEPVKKRGWPKGKKRKKILPNGPKAPVTGYVRFLNERREQIRTRHPDLPFPEITKMLGAEWSKLQPTEKQRYLDEAEREKQQYMKELRAYQQSEAYKMCTEKIQEKKIKKEDSSSGLMNTLLNGHKGGDCDGFSTFDVPIFTEEFLDQNKAREAELRRLRKMNVAFEEQNAVLQRHTQSMSSARERLEQELALEERRTLALQQQLQAVRQALTASFASLPVPGTGETPTLGTLDFYMARLHGAIERDPAQHEKLIVRIKEILAQVASEHL
Protein: Adenosine deaminase (EC 3.5.4.4) (F5GWI4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296}; Extracellular side {ECO:0000256|ARBA:ARBA00004296}. Cytoplasmic vesicle lumen {ECO:0000256|ARBA:ARBA00004321}.
Interaction partners:
Sequence:
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL
Protein: Integral membrane protein (A0A0H2UR43)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKQTKTTKIALVSLLTALSVVLGYFLKIPTPTGILTLLDAGVFFAAFYFGSREGAVVGGLASFLIDLLSGYPQWMFFSLVNHGLQGFFAGFKGKSQWLGLILATIAMVGGYALGSALMNGWAAALPEILPNFMQNMVGMIVGFILSQSIKKIK
Protein: Diphtheria toxin repressor (Iron-dependent diphtheria tox regulatory element) (Tox regulatory factor) (P0DJL7)
Organism: Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Function: Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess.
Subcellular location: Cytoplasm.
Interaction partners:
- Heme oxygenase
- HTH-type transcriptional regulator RipA
- UDP-glucose 4-epimerase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Glutamyl-tRNA reductase
- RNA polymerase sigma factor SigB
- Cytochrome c oxidase subunit 3
- Ferric uptake regulatory protein
- histidine kinase
Sequence:
MKDLVDTTEMYLRTIYELEEEGVTPLRARIAERLEQSGPTVSQTVARMERDGLVVVASDRSLQMTPTGRTLATAVMRKHRLAERLLTDIIGLDINKVHDEACRWEHVMSDEVERRLVKVLKDVSRSPFGNPIPGLDELGVGNSDAAVPGTRVIDAATSMPRKVRIVQINEIFQVETDQFTQLLDADIRVGSEVEIVDRDGHITLSHNGKDVELIDDLAHTIRIEEL
Protein: Beta-ketoacyl-[acyl-carrier-protein] synthase III (Beta-ketoacyl-ACP synthase III) (KAS III) (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase 3) (3-oxoacyl-[acyl-carrier-protein] synthase III) (EcFabH) (P0A6R0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain. Can also use propionyl-CoA, with lower efficiency.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
Interaction partners:
- Phosphate acyltransferase
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Malonyl CoA-acyl carrier protein transacylase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Biotin carboxylase
- Enoyl-[acyl-carrier-protein] reductase FabI
Sequence:
MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (Q6E0V2)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Subcellular location: Cytoplasm. Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
- Kelch-like protein 42
- Kelch-like family member 9
- Cullin-3
- Kelch-like protein 12
- Gigaxonin
- Kelch-like protein 41
- Kelch-like family member 8
- Katanin regulatory subunit B1 like 1
- Speckle-type POZ protein, isoform CRA_a.
Sequence:
MSLLMITENVKLAREYALLGNYDSAMVYYQGVLDQINKYLYSVKDTHLHQKWQQVWQEINVEAKHVKEIMKTLESFKLDSTSLKAAQHELPSSEGEVWSLPVPVERRPLPGPRKRQSTQHSDPKPHSNRPGAVVRAHRPSAQSLHSDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDSTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIVEFGSC
Protein: Spexin (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2 (NPQ 53-70)] (Q9BT56)
Organism: Homo sapiens (Human)
Function: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity).
Subcellular location: Secreted. Secreted, extracellular space. Cytoplasmic vesicle, secretory vesicle. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide (PubMed:17284679, PubMed:19193193). Localized extracellularly surrounding the villous trophoblastic cells. Detected in the serum.
Interaction partners:
- Galanin receptor type 2
- Galanin receptor type 3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- ATP-dependent clpX-like chaperone, mitochondrial
- Galanin peptides
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Galectin-2
Sequence:
MKGLRSLAATTLALFLVFVFLGNSSCAPQRLLERRNWTPQAMLYLKGAQGRRFISDQSRRKDLSDRPLPERRSPNPQLLTIPEAATILLASLQKSPEDEEKNFDQTRFLEDSLLNW
Protein: Uncharacterized protein Rv1419 (P9WLX9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Molybdenum import ATP-binding protein ModC
- Beta-D-galactosidase Rv1717
Sequence:
MGELRLVGGVLRVLVVVGAVFDVAVLNAGAASADGPVQLKSRLGDVCLDAPSGSWFSPLVINPCNGTDFQRWNLTDDRQVESVAFPGECVNIGNALWARLQPCVNWISQHWTVQPDGLVKSDLDACLTVLGGPDPGTWVSTRWCDPNAPDQQWDSVP
Protein: Chromosomal replication initiator protein DnaA (EC 3.6.4.-) (P05648)
Organism: Bacillus subtilis (strain 168)
Function: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. DnaA can inhibit its own gene expression as well as that of other genes.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377, ECO:0000269|PubMed:10844689}. Cytoplasm, nucleoid {ECO:0000269|PubMed:19081080}. Note=Forms 1 or rarely 2 (in large cells) tight foci on the nucleoid which usually coincide with replicative DNA polymerase (PubMed:19081080, PubMed:28166228). Induction of SirA disrupts localization of DnaA (PubMed:19682252). Some accumulation is seen at oriC after replication initiation (PubMed:28166228). The protein is bound to oriC and replication forks with a half-life of about 2.5 seconds, independent of transcription (PubMed:28166228). In the absence of yabA (or soj) more protein binds to oriC, leading to greater replication initiation (PubMed:28166228). {ECO:0000269|PubMed:10844689, ECO:0000269|PubMed:19081080, ECO:0000269|PubMed:19682252, ECO:0000269|PubMed:28166228}.
Interaction partners:
- Beta sliding clamp
- Sporulation initiation inhibitor protein Soj
- DNA replication and repair protein RecF
- Sporulation inhibitor of replication protein SirA
- Replicative DNA helicase DnaC
- Replicative helicase loader DnaI
- Replicative helicase loading/DNA remodeling protein DnaB
- Stage 0 sporulation protein J
- DNA gyrase subunit B
- Replicative helicase loading/DNA remodeling protein DnaD
Sequence:
MENILDLWNQALAQIEKKLSKPSFETWMKSTKAHSLQGDTLTITAPNEFARDWLESRYLHLIADTIYELTGEELSIKFVIPQNQDVEDFMPKPQVKKAVKEDTSDFPQNMLNPKYTFDTFVIGSGNRFAHAASLAVAEAPAKAYNPLFIYGGVGLGKTHLMHAIGHYVIDHNPSAKVVYLSSEKFTNEFINSIRDNKAVDFRNRYRNVDVLLIDDIQFLAGKEQTQEEFFHTFNTLHEESKQIVISSDRPPKEIPTLEDRLRSRFEWGLITDITPPDLETRIAILRKKAKAEGLDIPNEVMLYIANQIDSNIRELEGALIRVVAYSSLINKDINADLAAEALKDIIPSSKPKVITIKEIQRVVGQQFNIKLEDFKAKKRTKSVAFPRQIAMYLSREMTDSSLPKIGEEFGGRDHTTVIHAHEKISKLLADDEQLQQHVKEIKEQLK
Protein: D-xylonate dehydratase YagF (EC 4.2.1.82) (P77596)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dehydration of D-xylonic acid to form 2-dehydro-3-deoxy-D-pentonate.
Interaction partners:
- Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagE
- Probable 2-dehydro-3-deoxy-D-pentonate aldolase YjhH
- Putative glycoside/cation symporter YagG
- D-xylonate dehydratase YjhG
- 3-isopropylmalate dehydratase large subunit
- Uncharacterized protein YiiE
- Glutamate synthase large chain
- 3-isopropylmalate dehydratase small subunit
- Acetolactate synthase isozyme 1 large subunit
- Acetolactate synthase isozyme 3 large subunit
Sequence:
MTIEKIFTPQDDAFYAVITHAAGPQGALPLTPQMLMESPSGNLFGMTQNAGMGWDANKLTGKEVLIIGTQGGIRAGDGRPIALGYHTGHWEIGMQMQAAAKEITRNGGIPFAAFVSDPCDGRSQGTHGMFDSLPYRNDAAIVFRRLIRSLPTRRAVIGVATCDKGLPATMIALAAMHDLPTILVPGGATLPPTVGEDAGKVQTIGARFANHELSLQEAAELGCRACASPGGGCQFLGTAGTSQVVAEALGLALPHSALAPSGQAVWLEIARQSARAVSELDSRGITTRDILSDKAIENAMVIHAAFGGSTNLLLHIPAIAHAAGCTIPDVEHWTRINRKVPRLVSVLPNGPDYHPTVRAFLAGGVPEVMLHLRDLGLLHLDAMTVTGQTVGENLEWWQASERRARFRQCLREQDGVEPDDVILPPEKAKAKGLTSTVCFPTGNIAPEGSVIKATAIDPSVVGEDGVYHHTGRVRVFVSEAQAIKAIKREEIVQGDIMVVIGGGPSGTGMEETYQLTSALKHISWGKTVSLITDARFSGVSTGACFGHVSPEALAGGPIGKLRDNDIIEIAVDRLTLTGSVNFIGTADNPLTPEEGARELARRQTHPDLHAHDFLPDDTRLWAALQSVSGGTWKGCIYDTDKIIEVINAGKKALGI
Protein: ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Q9VKY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Caseinolytic protease chaperone subunit, isoform C
- 10 kDa heat shock protein, mitochondrial
- Lon protease homolog, mitochondrial
- NADH dehydrogenase 23 kDa subunit
- GrpE protein homolog, mitochondrial
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- 10 kDa heat shock protein, mitochondrial
- Serine protease HTRA2, mitochondrial
- Heat shock 70 kDa protein cognate 5
- Mitochondrial ribosomal protein S11
Sequence:
MLKTAVSRFLQISSVQCGGRANSVRNINLIPMVVEQTGRGERAYDIFSRLLKERIICLMGNITDDISSTVVAQLLFLQSENVNKPIHLYINSPGGVVTAGLAIYDTMQYVKPPIATWCVGQACSMGSLLLAAGAPGMRYSLPNARIMIHQPSGGAQGQATDILIHAEEIIKIKRQLTNIYVKHAKNTYEEMSGRMERDHFMTPEEAKVLGIIDHVLEHPPETVSETGPASDGGVTSGKAVPEECEKKRSKQAA
Protein: Protein MAINTENANCE OF MERISTEMS (Q9LMT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the organization of the root apical meristem (RAM) and the shoot apical meristem (SAM). Required to maintain genome stability and cell division activity in meristematic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:23607329}.
Interaction partners:
- 3-ketoacyl-CoA synthase 19
- Serine/threonine-protein phosphatase 7
- Protein MICRORCHIDIA 6
- DNA
- 3-ketoacyl-CoA synthase 20
- 3-ketoacyl-CoA synthase 17
Sequence:
MPVLYEQDKHVSSAILTGQERGVLRCQERTSLLHHWKLTKEQIALVEKAGFGWFRLVGSISLNNSLISALVERWRRETNTFHFPCGEMTITLDEVSLILGLAVDGKPVVGVKEKDEDPSQVCLRLLGKLPKGELSGNRVTAKWLKESFAECPKGATMKEIEYHTRAYLIYIVGSTIFATTDPSKISVDYLILFEDFEKAGEYAWGAAALAFLYRQIGNASQRSQSIIGGCLTLLQCWSYFHLNIDRPKRTTRQFPLALLWKGRQQSRSKNDLFKYRKALDDLDPSNVSWCPFEGDLDIVPQSFKDNLLLGRSRTKLIGPKVVEWHFPDRCMKQFGLCQVIPGEVPPRKNEKNHDEDLLEDMNTADEEWMRRRENIVENGGGNGDESEYMQWFNSITVPKLHRDTSLEADIMNVQAAILQFDEVASTLSLEDLHPEEREAIEEAVMSMSNALRVGDWYEASTTNKRKRREEQQQTDWSE
Protein: Src kinase-associated phosphoprotein 1 (SKAP55 adapter protein) (Src family-associated phosphoprotein 1) (Src kinase-associated phosphoprotein of 55 kDa) (SKAP-55) (pp55) (Q4V7G1)
Organism: Rattus norvegicus (Rat)
Function: Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway (By similarity). Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86WV1}. Nucleus {ECO:0000250|UniProtKB:Q86WV1}. Cell membrane {ECO:0000250|UniProtKB:Q86WV1}. Note=Upon T-cell stimulation, translocates to lipid rafts at the cell membrane. {ECO:0000250|UniProtKB:Q86WV1}.
Interaction partners:
- FYN-binding protein 1
- Lymphocyte cytosolic protein 2
- Linker for activation of T-cells family member 1
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- Tyrosine-protein kinase
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- T-cell surface glycoprotein CD3 zeta chain
- T cell receptor associated transmembrane adaptor 1
- T-cell surface glycoprotein CD3 epsilon chain
Sequence:
MQAIALPEEICWLLEDAEDFLAEGLQNENLSPGAQDQRDHILRGFQQIKSRYCWDFQPQGDDLGQDGSDENLSGTHGPALASDASFWSDYQEEGIDDIIRGAQELDNVIKQGYLEKKSKDHSFFGSEWQKRWCVISRGLFLYYANEKSKQPKGTFLIKGYNVRMAPHLRKDSKKDSCFELTSQDRRSYEFTAFSPAEARDWVDQISFLLKDLSSLTIPFEEEEEEEEEDKEQEEMYNDIDGFDSARSGSQGRAMALPEPLDKEEDVYEVLPDEDDLEEDACGAHRRRVDYADYYQGLWDCHGDQPDELSFQRGDLIRILSKEYNMYGWWVGELNSIIGIVPKDYLTTAFEMEGR
Protein: Alkylbase DNA glycosidase-like protein mag2 (O94468)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Alkylbase DNA glycosidase-like protein that shows no DNA glycosylase activity for alkylated bases. The molecular role of mag2 appears to be abasic (AP) site recognition and protection, while possibly facilitating damage signaling by structurally sculpting the DNA substrate. Stimulates AP site binding to mismatch repair protein mutS.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23245849}.
Interaction partners:
- Endonuclease III homolog lyase)
- Adenine DNA glycosylase
- DNA repair protein rad16
- DNA-
- G/U mismatch-specific uracil DNA glycosylase
- Uracil-DNA glycosylase
Sequence:
MSKDSDYKRAEKHLSSIDNKWSSLVKKVGPCTLTPHPEHAPYEGIIRAITSQKLSDAATNSIINKFCTQCSDNDEFPTPKQIMETDVETLHECGFSKLKSQEIHIVAEAALNKQIPSKSEIEKMSEEELMESLSKIKGVKRWTIEMYSIFTLGRLDIMPADDSTLKNEAKEFFGLSSKPQTEEVEKLTKPCKPYRTIAAWYLWQIPKLHRKGQ
Protein: Cysteine desulfurase IscS (EC 2.8.1.7) (O25008)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
Interaction partners:
- Nitrogen fixation protein NifU
- Thiamin biosynthesis protein
- Acyl carrier protein
- Acyl carrier protein
- Conserved hypothetical nifU-like protein
- Cysteine synthase
Sequence:
MLQRIYLDNNATTRIDPKVKEIMDPFLRDHYGNPSSLHQFGTETHPAIAEALDKLYKGINARDIDDVIITSCATESNNWVLKGVYFDECLKKGKNHIVTTVAEHPAVRSTCNFLESLGVEVTYLPINEHGSITAEQVKEAITEKTALVSVMWANNETGLIFPIEEIGAICKEKGVLFHTDAVQAIGKIPVDVLKANADFLSFSAHKFHGPKGIGGLYIRSGVGLTPLFHGGEHMNGRRSGTLNVPYIVGMGEAMKLAVEHLDYEKEVVGKLRDKLEEALLKIPDVMVVGDRIHRVPNTTLVSVRGIEGEAMLWDLNRSNIAASTGSACASEDLEANPVMVAIGASKELAHTAIRLSLSRFNTEAEIDKTIEVFSQAAVRLRNISSSY
Protein: LIM zinc-binding domain-containing protein (O17833)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGLLTENMRGDPLMIRFMHKAGEFFRKTKNNWLIDVEEYMSQLPNNVVPRTNSNGEKLREKQLLLQLPRQDLSVAYCRHLTSQTERKVYEEFVNARNEIALDIGYVSSNINKAMECHKCSGILETNEMAVIAPKLGDSTGWHPACFTCQACEQLLVDLTYCVKDNQIYCERHYAELHKPRCSACDELIFAGEYTKAMNKDWHSDHFCCWQCDQTLTGQRYIMRDEQPYCIKCYEDVFANQCDECAKPIGIDSKDLSYKDKHWHEHCFLCSMCKISLVDMPFGSKNDRIFCSNCYDQAFATRCDGCNEIFRAGMKKMEYKGKQWHDKCFCCAHCKLAIGTKSFIPKNDDVFCGPCYEEKFATRCSKCKKVITAGGVTYKNEPWHRECFCCTNCNSSLAGQRFTSKDEKPYCANCYGDLFAKRCNACTKPITGIGGAKFISFEDRHWHNDCFICAQCTTSLVGKGFITDGHEILCPECAKARLMAANS