wanglab/gogpt-training-data huggingface dataset:
Protein: PR domain zinc finger protein 8 (EC 2.1.1.-) (PR domain-containing protein 8) (Q9NQV8)
Organism: Homo sapiens (Human)
Function: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 (By similarity). Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR (By similarity). Forms with BHLHE22 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation (By similarity). In the retina, it is required for rod bipolar and type 2 OFF-cone bipolar cell survival (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:22961547}.
Interaction partners:
- Class E basic helix-loop-helix protein 22
- E3 ubiquitin-protein ligase NHLRC1
Sequence:
MEDTGIQRGIWDGDAKAVQQCLTDIFTSVYTTCDIPENAIFGPCVLSHTSLYDSIAFIALKSTDKRTVPYIFRVDTSAANGSSEGLMWLRLVQSARDKEEQNLEAYIKNGQLFYRSLRRIAKDEELLVWYGKELTELLLLCPSRSHNKMNGSSPYTCLECSQRFQFEFPYVAHLRFRCPKRLHSADISPQDEQGGGVGTKDHGGGGGGGKDQQQQQQEAPLGPGPKFCKAGPLHHYPSPSPESSNPSAAAGGSSAKPSTDFHNLARELENSRGGSSCSPAQSLSSGSGSGGGGGHQEAELSPDGIATGGGKGKRKFPEEAAEGGGGAGLVGGRGRFVERPLPASKEDLVCTPQQYRASGSYFGLEENGRLFAPPSPETGEAKRSAFVEVKKAARAASLQEEGTADGAGVASEDQDAGGGGGSSTPAAASPVGAEKLLAPRPGGPLPSRLEGGSPARGSAFTSVPQLGSAGSTSGGGGTGAGAAGGAGGGQGAASDERKSAFSQPARSFSQLSPLVLGQKLGALEPCHPADGVGPTRLYPAAADPLAVKLQGAADLNGGCGSLPSGGGGLPKQSPFLYATAFWPKSSAAAAAAAAAAAAGPLQLQLPSALTLLPPSFTSLCLPAQNWCAKCNASFRMTSDLVYHMRSHHKKEYAMEPLVKRRREEKLKCPICNESFRERHHLSRHMTSHN
Protein: Inositol polyphosphate-5-phosphatase A (EC 3.1.3.56) (Type I inositol 1,4,5-trisphosphate 5-phosphatase) (5PTase) (Q7TNC9)
Organism: Mus musculus (Mouse)
Function: Phosphatase that specifically hydrolyzes the 5-phosphate of inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate, and inositol 1,3,4,5-tetrasphosphate to inositol 1,3,4-trisphosphate. Plays a crucial role in the survival of cerebellar Purkinje cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14642}; Lipid-anchor {ECO:0000250|UniProtKB:Q14642}. Cell projection, dendrite {ECO:0000269|PubMed:26051944}.
Interaction partners:
Sequence:
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVLHTHKPHFMALHCQEFGGKNYEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQFDFKAKKYKKVTGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDLVNIHLFHDASNLVAWETSPSVYSGVRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSKSVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVVLQLEKKLFDYFNQDVFRDNNGTALLEFDKELSVFKDRLYELDISFPPSYPYSEDSSQGEQYMNTRCPAWCDRILMSLSAKELVLKSESEEKVATYDHIGPNVCMGDHKPVFLAFRIAPGAGKPHAHVHKCCVVQ
Protein: Eukaryotic release factor 3 (Q7YZN6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
KSTISGHLLMEKGLVDQREMEKLRREAEVHHREGWEYAYVMDVSEDERTKGITRETGAAYVETEKRRITVLDAPGHKAFVPSMIGGATQADVCVLVISSRTGEFETGFEKGGQTREHAMLVRTCGVKQMICVINKMDEVNWSKERYDAILGKLKPFLRQNGYDEEKAKNLIFIPIAGLTGDNLIRETAEGVCPWYKGPTMMSFIDELVLPETKSENDVLCIPLVGSYKDEGRVFVYGKVESGSVAVGEKIQILPSKQEAVVEGISIEATEFEKCYPGDNVHLRVRGVDEGDVHAGYVGTSVPTSLRAVEYFQARVVILDVKNIICAGSRVMLHAHAAQEEVSFHKLLAKVDKKTGEVVQKDPTHVKAGDVVIARMELERALVLEPHKDFDKMGRFMLREDGKTIAIGLVMKLYESTRESLANAGKA
Protein: Rho GDP-dissociation inhibitor 1 (AtRhoGDI1) (Rho GDI-1) (Q9SFC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Rac-like GTP-binding protein ARAC4
- Rac-like GTP-binding protein ARAC5
- Rac-like GTP-binding protein ARAC11
- Rac-like GTP-binding protein ARAC3
- Rac-like GTP-binding protein ARAC8
- Rac-like GTP-binding protein ARAC10
- Rac-like GTP-binding protein ARAC6
- Rac-like GTP-binding protein ARAC7
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Ras-related protein RABB1a
Sequence:
MSLVSGARDMGFDDNNNNKNNKDGDDENSSSRTRADDDALSRQMSESSLCATEEEEDDDSKLQLGPQYTIKEHLEKDKDDESLRKWKEQLLGSVDVTNIGETLDPEVRIDSLAIISPGRPDIVLLVPENGNPKGMWFTLKEGSKYNLKFTFHVNNNIVSGLRYTNTVWKTGVKVDRAKEMLGTFSPQLEPYNHVMPEETTPSGMFARGSYSARTKFLDDDNKCYLEINYSFDIRKEWPAL
Protein: Sialyltransferase-like protein 1 (EC 2.4.-.-) (Protein MALE GAMETOPHYTE DEFECTIVE 2) (Q8VZJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal pollen grain germination and pollen tube growth. May not be required for pollen development and female gametophytic function.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20738727}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Embryo defective 1381
- Beta-1,6-galactosyltransferase GALT29A
- 2-dehydro-3-deoxyphosphooctonate aldolase 1
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase MGP4
- 2-dehydro-3-deoxyphosphooctonate aldolase 2
- BTB/POZ domain-containing protein SETH6
- Nuclear pore complex protein GP210
- Protein GAMETE EXPRESSED 3
- Pectinesterase 5
- At1g19710
Sequence:
MRSHQAGRKLPLLQLLGCVAVFSVFVFTIQSSFFADNNRKLDLQPEDIQILSDFQSSVQQCVANRGLGLSAHIIDHCNLILKFPEGTNSTWYNAQFKVFEALEFKYNVCEAVLLWEQYRNMTTVLTREYLDVRPDGWLDYAAMRIAQLGADKCYNRTLCEEHLNVILPAKPPFHPRQFHKCAVVGNSGDLLKTEFGEEIDSHDAVFRDNEAPVNEKYAKYVGVKRDFRLVVRGAARNMIKILNGSDNEVLIIKSVTHRDFNEMIKRIPNPVYLFQGIVLRRGAKGTGMKSIELALSMCDIVDIYGFTVDPGYTEWTRYFSTPRKGHNPLQGRAYYQLLECLGVIRIHSPMRSERKEDWSSVPSREMISRAHTAALRLQRSQQPTSSKRDGSGQFGNCKVWGDADPTKGPVSGSPDMSETRKKSNYKKWEVMPFRSLRKEARDHYIQMKGVSQYKMDGNKLDDLVCVRHPLKLDT
Protein: GH11935p (Oligosaccharide transferase gamma subunit) (Q8SY53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Mannosyl-oligosaccharide glucosidase
- Inactive rhomboid protein 1
- Dol-P-Glc:Glc
- Protein transport protein Sec61 subunit beta
Sequence:
MRLLHKTLLSGLLVVALFAIYAAAQSKSKTGLSLSEKVQNLVDMNAKKPLLRFNGPKFREYVKSAPRNYSMIVMLTALAPSRQCQICRHAHDEFAIVANSYRFSSTYSNKLFFAMVDFDDGSEVFQLLRLNTAPVFMHFPAKGKPKGADTMDIHRVGFAADSIAKFVAERTDITIRIFRPPNYSGTVAMITLVALVGSFLYIRRNNLEFLYNKNLWGAIAVFFCFAMISGQMWNHIRGPPLVHKSQNGGVAYIHGSSQGQLVVETYIVMFLNAMIVLGMILLIESGTPKAHNKNRIMAMTGLVLLTVFFSFLLSVFRSKAQGYPYSFLFK
Protein: GAF domain-containing protein (Q57ZZ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDFVEVLPDAQDPLLQRLQMKHAELRVKQVMELKKTLEIEHSAMSKKIHKLPTTLDLVSDEISFTLNEIAVRCEEYAVPHVGQLLKDVHTMMNQQLREAYRHVEAGYRSAFHKMEEANEVQYRQQKSASSLGVSPQKPDKSPPHQAPANVECPPMAKGKNGKRGTGMKGTSEVRVLSVTEAMSATTGLFAESIAVSLRCEVVRIYLYDEYGNLNCCARFPFSATKGDPLAGTNLELILAKEVHRTVCQSCIAVNGRKRQEITMIERDRKEADEEIEQSGWKAMNSCLIFPVISNERGKQTHGMIHAMNKQGTSVNLVGEFDETDENFLFTAACLLGCLLSRYPGKCFMRPVGNLIHQHLGLHPVHGNDTSFLPQLIEDEVEDAAIAGNKALQMRPRVLVHRAPINVIYQARAERRKTRKLEVLHMVDRALSSVEFDLNALEELWRVGHEENRIMYEHCQHTNEQLNTLQVLLQNVLDGIGASRNMGTLEEVRRYLRALELHARQENTLQIKELISKALLHSDIEEIPPQLKEEVKSGRLTLEEAIQMERRLEAVESKLKFGASPVPQVRIYSYNPQLRREQARFFNANAEKRERLFNYANMAGDGPGYKGKTVSAVTKEVNLNPSLRLCFGTTDYASRRPFRLQGGRSVSPR
Protein: Zinc metalloproteinase dpy-31 (EC 3.4.24.-) (Nematode astacin 35) (Procollagen C-proteinase) (Tollish protein 2) (P98060)
Organism: Caenorhabditis elegans
Function: Metalloprotease which cleaves the carboxyl terminus of procollagens, such as sqt-3, to mature collagens (By similarity). Involved in cuticular collagen maturation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cuticle collagen 1
- Peptidase metallopeptidase domain-containing protein
- Peptidase metallopeptidase domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MHKIFIIFGLLSLCAAHSLRDLSNKDEEDPPSSAPGVRKRRMMSEEDQKTVDYYMDKLNKLADEKHPEEIERHKNPELVAWDRKRDSVLNPEEQGKFFQGDIVLYPEQAKALYEQALTEGKTRVKRKFIGSNLRRWDASRPIIYAFDGSHTQREQRIIELALEHWHNITCLNFQRNDQANSGNRIVFTDVDGCASNVGRHPLGEEQLVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDQYVTVRWENIDKDSKGQFLKEDPDDVDNAGVPYDYGSIMHYRSKAFSKFDDLYTISTYVTDYQKTIGQRDQLSFNDIRLMNKIYCSAVCPSKLPCQRGGYTDPRRCDRCRCPDGFTGQYCEQVMPGYGATCGGKISLTRSTTRISSPGYPREFKEGQECSWLLVAPPGHIVEFQFIGEFEMYCKIRHSLCMDYVEVRNSTDFANTGMRYCCYGTPPTRIRSATTDMVVLFRSFYRGGKGFEARARAVPEAGNWNSWSPWTACSATCGACGSRMRTRTCPPGNACSGEPVETQICNTQACTGMCAQKREEEGQCGGFLSLLRGVRCRQEKTVMAPCENACCPGFTLQRGRCVR
Protein: Polyglutamine-binding protein 1 (PQBP-1) (38 kDa nuclear protein containing a WW domain) (Npw38) (Polyglutamine tract-binding protein 1) (O60828)
Organism: Homo sapiens (Human)
Function: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species. May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules. Also acts as an innate immune sensor of infection by retroviruses, such as HIV, by detecting the presence of reverse-transcribed DNA in the cytosol. Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production.
Subcellular location: Nucleus {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:23512658}. Nucleus speckle {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule {ECO:0000269|PubMed:21933836}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2 (PubMed:10332029). Colocalized with ATXN1 in nuclear inclusion bodies (PubMed:12062018). Localizes to cytoplasmic stress granules (PubMed:21933836). {ECO:0000250|UniProtKB:Q91VJ5, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:21933836}.
Interaction partners:
- WW domain-binding protein 11
- Thioredoxin-like protein 4A
- Ataxin-1
- WW domain-binding protein 4
- Ubiquitin-like protein 5
- Zinc finger matrin-type protein 2
- Microfibrillar-associated protein 1
- WD40 repeat-containing protein SMU1
- Pre-mRNA-splicing factor 38A
- tRNA
Sequence:
MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD
Protein: Ras-related protein Ral-A (EC 3.6.5.2) (P63321)
Organism: Mus musculus (Mouse)
Function: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells (By similarity). The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (By similarity). During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B-CDK1 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11233}; Lipid-anchor {ECO:0000250|UniProtKB:P11233}; Cytoplasmic side {ECO:0000250|UniProtKB:P11233}. Cleavage furrow {ECO:0000250|UniProtKB:P11233}. Midbody, Midbody ring {ECO:0000250|UniProtKB:P11233}. Mitochondrion {ECO:0000250|UniProtKB:P11233}. Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles. May colocalize with CNTRL/centriolin at the midbody ring. However, localization at the midbody at late cytokinesis was not confirmed. Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission. {ECO:0000250|UniProtKB:P11233}.
Interaction partners:
- RalA-binding protein 1
- Exocyst complex component 2
- Exocyst complex component 8
- Ral guanine nucleotide dissociation stimulator
- Exocyst complex component 4
- Phospholipase D1
- Ral guanine nucleotide dissociation stimulator-like 2
- Ral guanine nucleotide dissociation stimulator-like 1
- Phospholipase D2
- Exocyst complex component 5
Sequence:
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRADQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL
Protein: Nuclear pore complex protein An-Nup49 (Eurofung) (Q5BAJ9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- Nucleoporin NSP1
- Nuclear pore complex protein AN-Nup192
- Nuclear pore complex protein An-Nic96
- Nuclear pore complex protein An-Nup170
- Nuclear pore complex protein
- Protein transport protein sec13
- Nuclear pore complex protein An-Nup57
- WD40 repeat protein poxJ
- Nuclear pore complex protein An-Nup159
- Nuclear pore complex protein An-Nup133
Sequence:
MFSSKPATPSTGLSINTNSANSLFGGNTNQSANTPATTSSGGGLFGTAATQSKPAGSLFGNTGMGTTQQTQSSGSSLFSGLGGQQNSTSGSGLFGNTTATTTQQQPGGLFSGTTGTNNQANSSGGLFGNTASGATSQAQSKPTFGLGATSTTNNIFGTNPGAGQQQQQQQQQQAQKPTLSLFGTQNTTSQQPTQQTPAAGSNTVIQGVKVDITNLLPTTKYESCADEVKAELERFDTFIVNQINMCNEVASILPLVASQGSTIPNDVEYVQGKLETMQHALENDASDIDQLRSLVSRDAAEAQVAFRAIDTLKLPLQYQSTGGSGWWSAQDQKVSDSQSLRSTRKSTLALPDDVEGEPSMSTINGVPVNLVEYFSQRSDEMGVVLERYTRNLKEIEDHLHGVESTLERQIHEFTTSRNRDSAGNGAPKTVLNDLAAVLADVETGILGVASRLGAVTEQAQEVVLGAPSGLRQA
Protein: fructose-bisphosphatase (EC 3.1.3.11) (Q586C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transketolase
- Ribulose-phosphate 3-epimerase
- Malate dehydrogenase
Sequence:
MMRQNLTSDSLITDTLRKAGVPCDVVGIVETVAGACRAIAAGLRNDGVTAAKSKNNFGDDVLSVDVMADKIISEALNSCQHVASYVSEESPSLASTAHSGKATYSVSYDPLDGSSIITSNFTVGSIFAVWPGNTPIGLTVRDMAASVVAVYGPRVVLFVGQEELGVAEFFCGADGEWKLAKRVWAGVCTPRTATVTAAGRGVKLKATVFSPGNLRAVRHLPWYKQLITMYMQEGATLRYTGGMVPDVCQIIVKGDGIYMTPASPQHKMKLRLLFEAAPMAFLIHCAGGRSTTGLTNMMNVRVVSMEQTTPIALGCARDVERYERMCRGCSKL
Protein: Degenerin-like protein unc-105 (Uncoordinated protein 105) (Q09274)
Organism: Caenorhabditis elegans
Function: Ion channel which is permeable to small monovalent cations. Shown not to be H+-ion gated. May be mechanosensitive and is required for growth and muscle development.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Acid-sensing ion channel 1-like
- Acid-sensing ion channel 1
- Voltage-dependent T-type calcium channel subunit alpha
- DEgenerin Like
- DEgenerin Like
- Innexin unc-9
Sequence:
MAEDRIKSKLRRPASIESTMSSRTKPRHKPSPMSILMPHLMVGESFRKYRPHGLRNIRMNGHLDWNQLRKSFEKQSTFHGISHAATADGKWRWFWYTAFTICLLALLIQIFFLISKYRQYGKTVDLDLKFENAPFPSITICNLNPYKKSAIQSNPNTKAMMEAYSRRIGSGDKTEGIAAALSATGGLHAKVRRAKRKAKGKPRLRDRRYHQAFAQCLCDIEQLTGDRKGSCFAAFKGKIEIDTNNTAGFMNLHTSRCLCQLDTVSKALWPCFPYSSWKEKLCSECVDNTGHCPMRFYKGNELYENIKEQVDLCLCHKEYNHCVSTRDDGIILEISPNDELNDLDIGKKIASQLSAQQEKQAEVTTTEAPTVTQALGFEELTDDIAITSQAQENLMFAVGEMSEKAKESMSYELDELVLKCSFNQKDCQMDRDFTLHYDNTFGNCYTFNYNRTAEVASHRAGANYGLRVLLYANVSEYLPTTEAVGFRITVHDKHIVPFPDAFGYSAPTGFMSSFGVRMKQFIRLEPPYGHCRHGGEDAATFVYTGFQYSVEACHRSCAQKVIVEACGCADPMYPVAEMFGNNTKPCQAVNMDQRECLRNTTLWLGELYSKGKEAIIPDCYCHQPCQETNYEVTYSSARWPSGSAKVMECLPGDFLCLEKYRKNAAMVQIFYEELNYETMQESPAYTLTSVLADLGGLTGLWIGASVVSLLEIVTLIVFATQAYVRKRKGSISAQSHHSVPVHRASRVSLNTLHKSSTTQSVKLSVMDIRSIKSIHSNHSSKSKQSILIEDLPPAIQEQSDDEEETTESSRTNGSCRYLAPGEDLPCLCKYHPDGSIRIMKALCPVHGYMVRRNYDYSVSNSEEEDAEDEVHREPEPFYSAPYEHRKK
Protein: Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R) (Q68EJ0)
Organism: Rattus norvegicus (Rat)
Function: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS).
Subcellular location: Endoplasmic reticulum. Note=Soluble protein. {ECO:0000250}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Uridine monophosphate synthetase, isoform CRA_a.
- Cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Cytochrome b5
- Cytochrome b5 type B
- Sulfite oxidase, mitochondrial
- Cytochrome b5 domain-containing protein 1
- Fatty acid desaturase 6
Sequence:
MLNVPSQAFPAPGSQQRVASQGRSKVPLKQGRSLMDWFRLTKSGKDFTGLKGGLIEVTEEELKKHNKKDDCWICIRGFVYNVSPYMEYHPGGEDELMRAAGADGTDLFNEVHRWVNYESMLKECLVGRMAVKPAVPKDCHEGKRVLNGMLPKSQVTDTLPREGPSSPSYDWFQTESSVTIVIYTKQKNINLDSVIVDLQDDSLRAEAVIKDHSYLIHIGLSHEVQENFSVRVIENVGKIEIVLQKKETVSWKCLGDPLEKHDSFIPKKDTGLYYRQCQLISKEDVTHDTRLFCLMLPPSTHLQVPVGQHVYLKLSVTGAEIVKPYTPVSESLLSDFKEPVLSPNKYIYFLIKIYPAGLFTPELDRLQIGDFVSVSGPEGNFKVSKLQEVEDLFLLAAGTGFTPMVTVLNHALTHMSSLRKVKLMFFNKTEDDIIWRCQLEKLALKDKRFHVEYVLSAPSPEWNGKQGHVSRALLSEFLQRSLENSKVFLCICGPTPFTDEGIRLLHDLNFSDDEIHGFTA
Protein: A-kinase anchor protein 2 (Q8C9L6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
MEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNGVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKEAKFELRAFHEDKKPSKLFEEDEREKEQFCVRKVRPSEEMIELEKERRELIQSQAVKKNPGIAAKWWNPPQEKTIEEQLDEEHLESHRKYKERKEKRAQQEQLQLQQQQQQQLQQQQLQQQQLQQQQLQQQLQQQQLSTSQPCTAPAAHKHLDGIEHTKEDVVTEQIDFSAARKQFQLMENSRQTLAKGQSTPRLFSIKPYYKPLGSIHSDKPPTILRPATVGGTLEDGGTQAAKEQKAPCVSESQSAGAGPANAATQGKEGPYSEPSKRGPLSKLWAEDGEFTSARAVLTVVKDEDHGILDQFSRSVNVSLTQEELDSGLDELSVRSQDTTVLETLSNDFSMDNISDSGASNETPSALQENSLADFSLPQTPQTDNPSEGREGVSKSFSDHGFYSPSSTLGDSPSVDDPLEYQAGLLVQNAIQQAIAEQVDKAEAHTSKEGSEQQEPEATVEEAGSQTPGSEKPQGMFAPPQVSSPVQEKRDILPKNLPAEDRALREKGPSQPPTAAQPSGPVNMEETRPEGGYFSKYSEAAELRSTASLLATQESDVMVGPFKLRSRKQRTLSMIEEEIRAAQEREEELKRQRQVRQSTPSPRAKNAPSLPSRTTCYKTAPGPGGHTG
Protein: ATP synthase mitochondrial F1 complex assembly factor 1 (Q38CY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MLAATRSLGGLYKVPGRKSLGEICKLSLLEATPEPQLATIWNEHHKQFVQYWGRTISADAYYALQPRLKQSPYFVIPVFRTKGLFNVVTNWDRDLVGVAPLAEWQEKQDSAQVHMTIQFFTELARTKRMVMVRCEIKDKVFVRQDCVFVTQMLLKYYSDPQLYEMWVEVFNKRPTQFDYHMYLRNMKDEAKRDDIRIEDKKAQVRMDAYGPVIDTPPDAIAQQILKSVDSGAPPPGESLNGCNGYRKE
Protein: Hepatoma-derived growth factor-related protein 2 (HRP-2) (Hepatoma-derived growth factor 3) (HDGF-3) (Q925G1)
Organism: Rattus norvegicus (Rat)
Function: Acts as an epigenetic regulator of myogenesis in cooperation with DPF3a (isoform 2 of DPF3/BAF45C) (By similarity). Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (By similarity). Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (By similarity). Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2 (By similarity). Involved in cellular growth control, through the regulation of cyclin D1 expression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26252862}. Cytoplasm {ECO:0000269|PubMed:26252862}.
Interaction partners:
Sequence:
MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNPHASYSAPLPVSSSDSEAPEADLGGGSDADKEKEARRVMTVTAVTTTATSGRTESDSDSDKNSDHSGLKRKTPVLKMSVSKRARKASSDLDQASVSPSEEDSESPSESEKTSDQDFTPEKKTIARAPRRAPLGGRKKKKVPSASDSDSRADSDGAKEEPVVTAQPSPSSSSSSSSSSASDSDVSIKKPPRGRKPAEKPPPKPRGRRSKPERPPSTSSSDSDSDSGEVDRISEWKRRDEERRRELEARRRREQEEELRRLREQEREEKERRKERAERGGSSGEELEDEEPVKKRSRKARGRGTPSSSDSEPEGELGKEGKKLAKKSQLQGSESARKPGQKEKRGRPDEKPRARPVKVERTRKRSEGLSLDRKGEKKKEPSVEERLQKLHSEIKFALKVDNPDVRRCLSALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDVMAKAAEVYTRLKSRVLGPKVEALQKVNKAGAEKERADGEKVEEQPGEQAPRELAEDEPSTDRSAPVNGEAASQKGENTEDGAQEDGQDLEDGPRGGSSEELHDSPQDSSDPARPGNEHQDHERMQLASESADDDDEDS
Protein: Inner membrane protein YgjV (P42603)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable D,D-dipeptide transport system permease protein DdpC
- Inner membrane protein YiaB
- Inner membrane protein YigG
Sequence:
MTAYWLAQGVGVIAFLIGITTFFNRDERRFKKQLSVYSAVIGVHFFLLGTYPAGASAILNAIRTLITLRTRSLWVMAIFIVLTGGIGLAKFHHPVELLPVIGTIVSTWALFCCKGLTMRCVMWFSTCCWVIHNFWAGSIGGTMIEGSFLLMNGLNIIRFWRMQKRGIDPFKVEKTPSAVDERG
Protein: ATP-dependent DNA helicase RecG (EC 5.6.2.3) (EC 5.6.2.4) (DNA 3'-5'/5'-3' helicase RecG) (DNA branch migration protein RecG) (P9WMQ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Interaction partners:
- Conserved hypothetical alanine rich protein
- Possible conserved membrane or exported protein
- ATP-dependent DNA helicase UvrD1
- Holliday junction branch migration complex subunit RuvB
- RecBCD enzyme subunit RecC
- Protein RecA
- UvrABC system protein A
- DhaL domain-containing protein
- UvrABC system protein B
- DNA polymerase I
Sequence:
MASLSDRLDRVLGATAADALDEQFGMRTVDDLLRHYPRSYVEGAARVGIGDARPEAGEHITIVDVITDTYSFPMKKKPNRKCLRITVGGGRNKVTATFFNADYIMRDLTKHTKVMLSGEVGYYKGAMQLTHPAFLILDSPDGKNHGTRSLKSIADASKAISGELVVEEFERRFFPIYPASTKVQSWDIFKCVRQVLDVLDRVDDPLPAELRAKHGLIPEDEALRAIHLAESQSLRERARERLTFDEAVGLQWALVARRHGELSESGPSAAWKSNGLAAELLRRLPFELTAGQREVLDVLSDGLAANRPLNRLLQGEVGSGKTIVAVLAMLQMVDAGYQCALLAPTEVLAAQHLRSIRDVLGPLAMGGQLGGAENATRVALLTGSMTAGQKKQVRAEIASGQVGIVIGTHALLQEAVDFHNLGMVVVDEQHRFGVEQRDQLRAKAPAGITPHLLVMTATPIPRTVALTVYGDLETSTLRELPLGRQPIATNVIFVKDKPAWLDRAWRRIIEEAAAGRQAYVVAPRIDESDDTDVQGGVRPSATAEGLFSRLRSAELAELRLALMHGRLSADDKDAAMAAFRAGEVDVLVCTTVIEVGVDVPNATVMLVMDADRFGISQLHQLRGRIGRGEHPSVCLLASWVPPDTPAGQRLRAVAGTMDGFALADLDLKERKEGDVLGRNQSGKAITLRLLSLAEHEEYIVAARDFCIEAYKNPTDPALALMAARFTSTDRIEYLDKS