wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter C family member 10 (ABC transporter ABCC.10) (AtABCC10) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 14) (Glutathione S-conjugate-transporting ATPase 14) (Multidrug resistance-associated protein 14) (Q9LYS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates.
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter G family member 39
- UPF0481 protein At3g47200
Sequence:
MIENYWTSFCGNHHTSSNCTVRFLQICFGITLSFLTLCICLFHKEPPKRIHQFFCLRLVSALFNGIIGSLDLVLGIWVLRENHSKPLILWLVILIQGFTWLFINLIICVRGTRIRKSSLRLLSIFSFFYGLVSSCLSVNNAVFGDELAVRTILDVLLLPGSVLLLLSAYKGYRFDESGESSLYEPLNAGDSNGFSEKADFDNRVSQFAKAGLFSTLSFWWLNSLIKRGNVKDLEEEDIPELRKEERAETCYSLFEENLIEQKRRLGSSCQPSILKVTVLCVWRELLTSGFFAFMKIVAVSAGPLLLNAFILVAEGNASFRYEGLVLAVLLFFSKMIESLSQRQWYFRCRIVGLRVRSLLTAAINKKQLRLNNSSRLIHSGSEIMNYATVDAYRIGEFPYWFHQLWTTSFQLLIALGILFHSVGVATFSALAVIILTVLCNAPIAKLQNKFQSELMTSQDERLKACNESLVNMKVLKLYAWESHFKKVIEKLRNIELKSLKAVQMRKAYNAVLFWSSPVFVSAATFATCYFLDIPLRASNVFTFVATLRLVQDPVRMIPDVIGVTIQAKVAFSRIATFLEAPELQGGERRRKQRSEGNQNAIIIKSASFSWEEKGSTKPNLRNVSLEVKFGEKVAVCGEVGSGKSTLLAAILGETPCVSGTIDFYGTIAYVSQTAWIQTGTIRDNILFGGVMDEHRYRETIQKSSLDKDLELLPDGDQTEIGERGVNLSGGQKQRIQLARALYQDADIYLLDDPFSAVDAHTASSLFQEYVMDALAGKAVLLVTHQVDFLPAFDSVLLMSDGEITEADTYQELLARSRDFQDLVNAHRETAGSERVVAVENPTKPVKEINRVISSQSKVLKPSRLIKQEEREKGDTGLRPYIQYMNQNKGYIFFFIASLAQVTFAVGQILQNSWMAANVDNPQVSTLKLILVYLLIGLCSVLCLMVRSVCVVIMCMKSSASLFSQLLNSLFRAPMSFYDSTPLGRILSRVSSDLSIVDLDVPFGLIFVVASSVNTGCSLGVLAIVTWQVLFVSVPMVYLAFRLQKYYFQTAKELMRINGTTRSYVANHLAESVAGAITIRAFDEEERFFKKSLTLIDTNASPFFHSFAANEWLIQRLETVSAIVLASTAFCMILLPTGTFSSGFIGMALSYGLSLNMGLVYSVQNQCYLANWIISVERLNQYTHLTPEAPEVIEETRPPVNWPVTGRVEISDLQIRYRRESPLVLKGISCTFEGGHKIGIVGRTGSGKTTLISALFRLVEPVGGKIVVDGVDISKIGVHDLRSRFGIIPQDPTLFNGTVRFNLDPLCQHSDAEIWEVLGKCQLKEVVQEKENGLDSLVVEDGSNWSMGQRQLFCLGRAVLRRSRVLVLDEATASIDNATDLILQKTIRREFADCTVITVAHRIPTVMDCTMVLSISDGRIVEYDEPMKLMKDENSLFGKLVKEYWSHYNSADSR
Protein: NAC domain-containing protein 102 (ANAC102) (Q8H115)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in regulation of seed germination under flooding.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cysteine/Histidine-rich C1 domain family protein
Sequence:
MDFALFSSISIFEINHKDPPIRRFIKTQNRILSTRKQQGTFPKMKAELNLPAGFRFHPTDEELVKFYLCRRCASEPINVPVIAEIDLYKFNPWELPEMALYGEKEWYFFSHRDRKYPNGSRPNRAAGTGYWKATGADKPIGKPKTLGIKKALVFYAGKAPKGIKTNWIMHEYRLANVDRSASTNKKNNLRLDDWVLCRIYNKKGTMEKYLPAAAEKPTEKMSTSDSRCSSHVISPDVTCSDNWEVESEPKWINLEDALEAFNDDTSMFSSIGLLQNDAFVPQFQYQSSDFVDSFQDPFEQKPFLNWNFAPQG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8VQA0)
Organism: Streptococcus agalactiae
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MIQIGKLFAGRYRILKSIGRGGMADVYLARDLILDNEEVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVMEYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKATAKKLTDRYKTTYEMGRDLSTALSWKSHREPKLVFNDTESTKTLPKVTSTVSSLTTEQLLRNQKQAKTTEKITPDSASNDKTKSKKKASHRLLGTIMKLFFALCVVGIIVFAYKILVSPTTIRVPDVSNKTVAQAKMTLENSGLKVGAIRNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYIATPNKSFTLGNYKEHNYKDILKDLQGKGVKKSLIKVKRKINNDYTTGTILAQSLPEGTSFNPDGNKKLTLTVAVNDPMIMPDVTGMTVGEVIETLTDLGLDADNLVFYQMQNGVYQTVVTPPSSSKIASQDPYYGGEAGLRRGDKVKLYLLGSKTTNNSSSTPIDSSASSSTGTTTSDSVSSSTDASTSDSSSTSTSKFNTTK
Protein: RNA pseudouridine synthase 1 (EC 5.4.99.-) (RNA pseudouridylate synthase 1) (RNA-uridine isomerase 1) (Q7XA65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein Iojap-related
- Pseudouridine synthase family protein
- WPP domain-containing protein 3
- At4g38020 family protein)
- Short integuments 2, mitochondrial
- Proton pump-interactor 2
- LOB domain-containing protein 32
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein mL43
Sequence:
MSLLRNFFSFTFSANSIITKPYFAIPIKAMEATSELNLNYPKPISAPPPPISKDIELRRAMEASSKSSLFNLTRDDILYEDEYLMAVNKPKGVYCEAVLRSAPQIVLDSSSEYHLANRLDRDTSGVMIITKSHKVAAKLVKAFTEHKIRKSYIALCIGSSPNWRRVTVSSGHGRSKHGAWRVYAALDVGRVLPGGSFVRDMETTFEVVSVNSVKNESCELEDVNHVIVAEGERELSCGGDDDDVVVVVRAFPRSGRTHQIRLHCQYLGIPIRGDVKYHGVYEWNGRTFEGHELHAECLSLDHPVTGDSIVIRAPLPYWAAGD
Protein: ADP-ribosylhydrolase ARH3 (ADP-ribose glycohydrolase ARH3) (LchARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-) (H3BCW1)
Organism: Latimeria chalumnae (Coelacanth)
Function: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NX46}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX46}. Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NX46}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}.
Interaction partners:
- poly
- Macro domain-containing protein
- Calcium/calmodulin dependent serine protein kinase
- Histone PARylation factor 1
Sequence:
MSAVGRLAAVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAGTLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVVQVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVIKFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMERIEGGEMSASDAGEHDRPNEVKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFLHCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQVTPSWKRSCEAIVETEESAVKLYELYCKQLKTP
Protein: ribonucleoside-diphosphate reductase (EC 1.17.4.1) (A0A023ZUP0)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Interaction partners:
Sequence:
MSTVFNTNPVDVLNEPMFFGSGLGLARYDIQRHRVFEELIERQISFFWRPEEVNLMMDAAQFNKLPQYQQNIFTNNLKYQSLLDSIQGRAPSAVLMSLISDPSLDTWVATWTFSETIHSRSYTHIMRNLYTDPSKVFDEIVLDEAIMKRAESIGRYYDDVLVKTREWENAKDMVEYYKDQGLILADKDVEQRAKRDLMKSLYLCLHVINALEAIRFYVSFACTFNFHKNMEIMEGNAKIMKFIARDEQLHLKGTQYIIRQLQSGTDGDEWVKIAQECEQEAVDIFMEVNRQEKDWAVHLFKDGDVPGLNTNSMWSFIDYLTVSRMKQCGLPCPITDAPVKHPYPWIREYLNSDNVQSAPQEVELSSYLVAQIDNDVDDKVMMSFKKYF
Protein: Glycogen [starch] synthase (GS) (EC 2.4.1.11) (Q9U2D9)
Organism: Caenorhabditis elegans
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Interaction partners:
- Glycogenin-1
- 1,4-alpha-glucan branching enzyme
- Alpha-1,4 glucan phosphorylase
- glycogenin glucosyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Protein phosphatase 1 regulatory subunit
- phosphoglucomutase
- Glycogen debranching enzyme
- Nucleotide-diphospho-sugar transferase
- Alpha,alpha-trehalose-phosphate synthase 1
Sequence:
MPDHARMPRNLSSNKIAKTIAGEDLDEEEVLEMDAGQSAREEGRFVFECAWEVANKVGGIYTVLRSKAQISTEELGDQYCMFGPMKDGKWRLEVDPIEPENRTIRAAMKRFQADGFRCMYGRWLIEGYPKVILFDLGSGAVKMNEWKHELFEQCKIGIPHEDIESNDAVILGFMVALFLKHFRESVTSYTPLVVAHFHEWQAGVGLLMTRLWKLDIATVYTTHATLLGRHLCAGGADLYNNLDSFDLDAEAGKRKIYHQYCLERAACQTAHIFTTVSEITGLEAEHFLCRKPDVLTPNGLNVVKFAALHEFQNLHAQNKEKINQFIRGHFHGHLDFDLDKTLYFFTAGRYEFSNKGGDMFIESLARLNHYLKTTSDPRHMGVTVVAFLIYPAPANSFNVESLKGQAVTKQLKEAVDRIKEKVGQRIFDICLQGHLPEPEELMSPADNILLKRCIMSLHNSSLPPICTHNMIRADDPVLESLRRTSLFNKPEDRVKVVFHPEFLSSVSPLIGLDYEDFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVSTNLSGFGCFMQEHVEDHEQKGIYVIDRRHKAAEESVQELAQVMYDFCGQSRRQRIILRNSNEGLSALLDWQNLGVFYRDCRRLALERLHPDVDKIMRDNEGKVPSAATSRRPSIHSSDGEDDE
Protein: Target of rapamycin complex 1 subunit TCO89 (TORC1 subunit TCO89) (89 kDa TOR complex 1 protein) (Q08921)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. Note=Also localizes to membranous structures both proximal to, yet distinct from, the plasma membrane as well as within the cell interior, probably endosomal or Golgi membranes.
Interaction partners:
- Target of rapamycin complex subunit LST8
- Serine/threonine-protein kinase TOR1
- Serine/threonine-protein kinase TOR2
- Target of rapamycin complex 1 subunit KOG1
- Target of rapamycin complex 2 subunit BIT61
- Target of rapamycin complex 2 subunit AVO1
- Target of rapamycin complex 2 subunit AVO2
- Nuclear cap-binding protein complex subunit 1
- Target of rapamycin complex 2 subunit TSC11
- GTP-binding protein GTR1
Sequence:
MVHRGRTLKSDTDVTSLNASTVSHQSKPFRQFSTRSRAKSNASFKGLRRVLTHDGTLDNDYFNKHNVSQKCKSSDALFRKRTISGLNMTALTRVKSNQGKRSASFHSPVHNTLLSPKNSSHSNTGTAGFGLKPRRSKSTQSVLSLRDAQESKKSESTTDEEVECFSEDNIEDGKVNNDKVIAEHVMPEEKKNVQQLNQNELQSPDSIDEQEEDKSGTDGKENHRAVSLPLPHLSSNNYFGESSHSIEHQKDGETSPSSIETKLNATSVINEEGQSKVTKEADIDDLSSHSQNLRASLVKAGDNISEAPYDKEKKILDVGNTLAAHKSNQKPSHSDEQFDQEDHIDAPRSNSSRKSDSSFMSLRRQSSKQHKLLNEEEDLIKPDDISSAGTKDIEGHSLLENYAPNMILSQSTGVERRFENSSSIQNSLGNEIHDSGEHMASGDTFNELDDGKLRKSKKNGGRSQLGQNIPNSQSTFPTIANIGSKDNNVPQHNFSTSISSLTNNLRRAAPESFHGSRMNNIFHKKGNQNLLLRSNDLNKNSAAPASPLSNEHITSSTNSGSDANRQSNSGAKFNSFAQFLKSDGIDAESRTQRKLWLQRENSIMDLSSQNDGSDSIFMAGNIDAKREFERISHEYSNVKRFYNPLDEALLRVQPIITGNANNIRKKSHNDAQSIAHSSSDTDHKDEDDLLFTNYDKKFDDLYPHLASAKIQAVLSGIWKSESYLFNKDVNPINKNRTTSTNHSVGHTASQNARNLLRGPMGSSTTLHHQRVINSLQPTTRAVNRRMENVGYMHTQPQQR
Protein: Chromatin modification-related protein MEAF6 (MYST/Esa1-associated factor 6) (Esa1-associated factor 6 homolog) (Protein EAF6 homolog) (hEAF6) (Sarcoma antigen NY-SAR-91) (Q9HAF1)
Organism: Homo sapiens (Human)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced activity toward histone H4. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:18794358}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.
Interaction partners:
- Enhancer of polycomb homolog 1
- Transformation/transcription domain-associated protein
- YEATS domain-containing protein 4
- Inhibitor of growth protein 4
- DNA methyltransferase 1-associated protein 1
- Histone acetyltransferase KAT5
- Mortality factor 4-like protein 1
- Histone acetyltransferase KAT7
- Peregrin
- Inhibitor of growth protein 5
Sequence:
MAMHNKAAPPQIPDTRRELAELVKRKQELAETLANLERQIYAFEGSYLEDTQMYGNIIRGWDRYLTNQKNSNSKNDRRNRKFKEAERLFSKSSVTSAAAVSALAGVQDQLIEKREPGSGTESDTSPDFHNQENEPSQEDPEDLDGSVQGVKPQKAASSTSSGSHHSSHKKRKNKNRHRIDLKLNKKPRADY
Protein: WD repeat-containing protein 72 (Q3MJ13)
Organism: Homo sapiens (Human)
Function: Plays a major role in formation of tooth enamel. Specifically required during the maturation phase of amelogenesis for normal formation of the enamel matrix and clearance of enamel proteins. May be involved in localization of the calcium transporter SLC24A4 to the ameloblast cell membrane.
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:D3YYM4}.
Interaction partners:
- Matrix metalloproteinase-20
- Kallikrein-4
- Protein FAM83H
- Odontogenesis associated phosphoprotein
- Enamelin
- Amelogenin, X isoform
- Ameloblastin
- Pseudokinase FAM20A
- Laminin subunit beta-3
Sequence:
MRTSLQAVALWGQKAPPHSITAIMITDDQRTIVTGSQEGQLCLWNLSHELKISAKELLFGHSASVTCLARARDFSKQPYIVSAAENGEMCVWNVTNGQCMEKATLPYRHTAICYYHCSFRMTGEGWLLCCGEYQDVLIIDAKTLAVVHSFRSSQFPDWINCMCIVHSMRIQEDSLLVVSVAGELKVWDLSSSINSIQEKQDVYEKESKFLESLNCQTIRFCTYTERLLLVVFSKCWKVYDYCDFSLLLTEVSRNGQFFAGGEVIAAHRILIWTEDGHSYIYQLLNSGLSKSIYPADGRVLKETIYPHLLCSTSVQENKEQSRPFVMGYMNERKEPFYKVLFSGEVSGRITLWHIPDVPVSKFDGSPREIPVTATWTLQDNFDKHDTMSQSIIDYFSGLKDGAGTAVVTSSEYIPSLDKLICGCEDGTIIITQALNAAKARLLEGGSLVKDSPPHKVLKGHHQSVTSLLYPHGLSSKLDQSWMLSGDLDSCVILWDIFTEEILHKFFLEAGPVTSLLMSPEKFKLRGEQIICCVCGDHSVALLHLEGKSCLLHARKHLFPVRMIKWHPVENFLIVGCADDSVYIWEIETGTLERHETGERARIILNCCDDSQLVKSVLPIASETLKHKSIEQRSSSPYQLGPLPCPGLQVESSCKVTDAKFCPRPFNVLPVKTKWSNVGFHILLFDLENLVELLLPTPLSDVDSSSSFYGGEVLRRAKSTVEKKTLTLRKSKTACGPLSAEALAKPITESLAQGDNTIKFSEENDGIKRQKKMKISKKMQPKPSRKVDASLTIDTAKLFLSCLLPWGVDKDLDYLCIKHLNILKLQGPISLGISLNEDNFSLMLPGWDLCNSGMIKDYSGVNLFSRKVLDLSDKYTATLPNQVGIPRGLENNCDSLRESDTIVYLLSRLFLVNKLVNMPLELACRVGSSFRMESIHNKMRGAGNDILNMSSFYSCLRNGKNESHVPEADLSLLKLISCWRDQSVQVTEAIQAVLLAEVQQHMKSLGKIPVNSQPVSMAENGNCEMKQMLPKLEWTEELELQCVRNTLPLQTPVSPVKHDSNSNSANFQDVEDMPDRCALEESESPGEPRHHSWIAKVCPCKVS
Protein: Dihydroneopterin triphosphate 2'-epimerase (EC 5.1.99.7) (D-erythro-7,8-dihydroneopterin triphosphate epimerase) (A0A0H2ZEG5)
Organism: Pseudomonas aeruginosa (strain UCBPP-PA14)
Interaction partners:
Sequence:
MPRLEPGMARIRVKDLRLRTFIGIKEEEILNKQDVLINLTILYPAADAVEVNDIEHALNYRTITKAIIRHVEENRFALLERMTQEILDLVMENPAVRYAEVEVDKPHALRFAESVSITLAGHR
Protein: Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Rab geranyl-geranyltransferase subunit beta) (Rab GG transferase beta) (Rab GGTase beta) (Rab geranylgeranyltransferase subunit beta) (Type II protein geranyl-geranyltransferase subunit beta) (Q08603)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Rab proteins geranylgeranyltransferase component A 1
- Protein prenyltransferase alpha subunit repeat containing 1
- Protein tyrosine phosphatase type IVA 2
- small monomeric GTPase
- Ras-related protein Rab-1B
- Synaptobrevin homolog YKT6
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Ras-related protein Rab-9A
- Ras-related protein Rab-8A
Sequence:
MGTQQKDVTIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAVQILTLYDSIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRVNVQPELVS
Protein: FlbE (Q5BFF9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- MYB family conidiophore development protein FlbD
- BZIP-type transcription factor
- C2H2-type domain-containing protein
- C2H2 type master regulator of conidiophore development brlA
- Protein fluG
- Developmental regulator flbA
Sequence:
MPVYMLYGFRWPRAGFTGIRVYIVLHNLEDATAEYIQRPITNKSLLDSFRKTEPDIMSNLPELRFIEQYDPEDESDEAVSKPYAYVAAKTISIPEAGSPNAGSSWNTDIFQENPLDPASSEALAKFRDKYAAGERIGWWIVYNGDPERYFPHDEDEDGMMEDDGYDDDDDEYDRDGSSSNTPSTPTIRLPETLTRFFNKTFS
Protein: Dentin sialophosphoprotein (Dentin matrix protein 3) (DMP-3) [Cleaved into: Dentin phosphoprotein (Dentin phosphophoryn) (DPP); Dentin sialoprotein (DSP)] (P97399)
Organism: Mus musculus (Mouse)
Function: DSP may be an important factor in dentinogenesis. DPP may bind high amount of calcium and facilitate initial mineralization of dentin matrix collagen as well as regulate the size and shape of the crystals.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Integrin beta-1
- Integrin beta-6
- Integrin alpha-V
- Dentin matrix acidic phosphoprotein 1
- Enamelin
- Lipid droplet-regulating VLDL assembly factor AUP1
- Ameloblastin
- Amelogenin, X isoform
- Matrix extracellular phosphoglycoprotein
- Bone morphogenetic protein 4
Sequence:
MKMKIIIYICIWATAWAIPVPQLVPLERDIVENSVAVPLLTHPGTAAQNELSINSTTSNSNDSPDGSEIGEQVLSEDGYKRDGNGSESIHVGGKDFPTQPILVNEQGNTAEEHNDIETYGHDGVHARGENSTANGIRSQVGIVENAEEAESSVHGQAGQNTKSGGASDVSQNGDATLVQENEPPEASIKNSTNHEAGIHGSGVATHETTPQREGLGSENQGTEVTPSIGEDAGLDDTDGSPSGNGVEEDEDTGSGDGEGAEAGDGRESHDGTKGQGGQSHGGNTDHRGQSSVSTEDDDSKEQEGFPNGHNGDNSSEENGVEEGDSTQATQDKEKLSPKDTRDAEGGIISQSEACPSGKSQDQGIETEGPNKGNKSIITKESGKLSGSKDSNGHQGVELDKRNSPKQGESDKPQGTAEKSAAHSNLGHSRIGSSSNSDGHDSYEFDDESMQGDDPKSSDESNGSDESDTNSESANESGSRGDASYTSDESSDDDNDSDSHAGEDDSSDDSSGDGDSDSNGDGDSESEDKDESDSSDHDNSSDSESKSDSSDSSDDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSNSSSDSSDSSGSSDSSDSSDTCDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSSSSDSSDSSSCSDSSDSSDSSDSSDSSDSSDSSSSDSSSSSNSSDSSDSSDSSSSSDSSDSSDSSDSSDSSGSSDSSDSSASSDSSSSSDSSDSSSSSDSSDSSDSSDSSDSSESSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSNSSDSSDSDSKDSSSDSSDGDSKSGNGNSDSNSDSNSDSDSDSEGSDSNHSTSDD
Protein: Tryptase beta-2 (Tryptase-2) (EC 3.4.21.59) (Tryptase II) (P20231)
Organism: Homo sapiens (Human)
Function: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity.
Subcellular location: Secreted. Note=Released from the secretory granules upon mast cell activation.
Interaction partners:
Sequence:
MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP
Protein: Splicing factor 3B subunit 1 (Pre-mRNA-splicing factor SF3b 155 kDa subunit) (SF3b155) (Spliceosome-associated protein 155) (SAP 155) (Q99NB9)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75533}. Nucleus speckle {ECO:0000250|UniProtKB:O75533}. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm. {ECO:0000250|UniProtKB:O75533}.
Interaction partners:
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 2
- ATP-dependent RNA helicase DDX42
- Splicing factor U2AF 65 kDa subunit
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 4
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 3
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 2
Sequence:
MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYDLDYIL
Protein: Kinesin-like protein (Q9VRK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Kinesin associated protein 3, isoform G
- Kinesin-like protein Klp68D
- No mechanoreceptor potential B, isoform D
- Protein smoothened
- Kinesin-like protein
- Suppressor of fused homolog
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 57 homolog
- Kurtz arrestin
- Reduced mechanoreceptor potential A, isoform B
Sequence:
MPQEEANAGTTAQLDDEIENVRVVVRTRPMDKNELSAGALSAISVDKINRAITVMKPNATANEPPKTYYFDNVFDGGSNQMDLYVDTARPIVDKVLEGYNGTILAYGQTGTGKTYTMSGNPDSPQTKGIIPNAFAHIFGHIAKAKENQKFLVRVSYMEIYNEEVRDLLGKDVGKSLEVKERPDIGVFVKDLSGYVVHNADDLENIMRLGNKNRAVGATKMNQESSRSHAIFSITVERSELGEGDVQHVRMGKLQLVDLAGSERQSKTQASGQRLKEATKINLSLSVLGNVISALVDGKSTHIPYRNSKLTRLLQDSLGGNSKTVMCATISPADSNYMETISTLRYASRAKNIQNRMHINEEPKDALLRHFQEEIARLRKQLEEGDSLEEEPPSSEEEEDTADDELEAPLEIELESSTIQAVEKKPKKKREKTDAEKEELAKRKNEHQKEIEHAKTEQETLRNKLVSLEGKILVGGENLLEKAQTQELLLEQSIAELEQHEKSEEALKQTLQQKATERIDIEERYSTLQDASTGITKKIHRVMQMLMGVKSELADQQQEHQREKEGIYENIRSLSRELALCELVLNSYVPKEYQSMINQYTHWNEDIGEWQLKCVAYTGNNMRKHISAHKTSGKEPDFLDLSHVYLSYNTDGVSNPMRSKSARPRTSGVPRPTTARRY
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8Y6M7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKLGLPTGHFVMAAQRQKRGK