wanglab/gogpt-training-data huggingface dataset:
Protein: Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Livin) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30 kDa subunit (Truncated livin) (p30-Livin) (tLivin)] (A2AWP0)
Organism: Mus musculus (Mouse)
Function: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and MAP3K7/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96CA5}. Cytoplasm {ECO:0000250|UniProtKB:Q96CA5}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CA5}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis. {ECO:0000250|UniProtKB:Q96CA5}.
Interaction partners:
- Caspase-9
- Caspase-7
- Caspase-3
- Diablo IAP-binding mitochondrial protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-conjugating enzyme E2 D2
- Serine protease HTRA2, mitochondrial
- E3 ubiquitin-protein ligase RNF4
- Polyubiquitin-B
Sequence:
MFSPADLFRAAVFSMGPESRARDSVRGPELSHREDGSGRTQEQDKPHCPCNHVLGQDCLDGQILGQLRPLSEEEESSGAAFLGEPAFPEMDSEDLRLASFYDWPSTAGIQPEPLAAAGFFHTGQQDKVRCFFCYGGLQSWERGDDPWTEHARWFPRCQFLLRSKGRDFVERIQTYTPLLGSWDQREEPEDAVSATPSAPAHGSPELLRSRRETQPEDVSEPGAKDVQEQLRQLQEERRCKVCLDRAVSIVFVPCGHFVCTECAPNLQLCPICRVPICSCVRTFLS
Protein: Protein S40-6 (AtS40-6) (O80698)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20238146}.
Interaction partners:
Sequence:
MAKGRKPTTMNRSDRYLGSYTYGDSHGNSVTDELELGEEDIWSPAVIHDDTTENEESYGTWNLRATLGKNGRVGGLSLAFEGSLVAPPSSSPMIVQKIHGGGGEGEEDRRKLASSAPVNVPDWSKIYRVDSVESIHELDDEDDEDEESGMMPPHEYLAKSQARRSRKIGGGGASVFDGVGRTLKGRELRRVRDAIWSQTGFYG
Protein: At3g23140 (C2H2 and C2HC zinc fingers superfamily protein) (Q9LTD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein 3
Sequence:
MNHRDKQIDSGSGSGENRRTYDCDICKRGFTNPQALGGHNNIHRRERERYPSSSSSSHSFPFSLPLPSQSPSSSTNFTNPPPYFPTIESYLHQGSQPPINPSHNTQYFGSSSSSRGGGRFAQGASHDLNLSLGLGSMNEDDDTHRSPPETGGSQPQDGDLDLDLRLGGHRHH
Protein: Vacuolar lysine transporter YPQ1 (PQ-loop repeat-containing protein 1) (Q12010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function as an amino acid transporter mediating the export of cationic amino acids from the vacuole.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23169667, ECO:0000269|PubMed:25229858}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23169667}.
Interaction partners:
- Protein SSH4
- Vacuolar membrane protein YPL162C
- Cystine transporter
- E3 ubiquitin-protein ligase RSP5
- Vacuolar basic amino acid transporter 4
Sequence:
MQLVPLELNRSTLSGISGSISISCWIIVFVPQIYENFYRKSSDGLSLLFVVLWLAGDVFNLMGAVMQHLLSTMIILAAYYTVADIILLGQCLWYDNEEKPAVDPIHLSPANPINENVLHDVFNEQQPLLNSQGQPNRIDEEMAAPSSDGNAGDDNLREVNSRNLIKDIFIVSGVVFVGFISWYVTYCVNYTQPPPVEDPSLPVPELQINWMAQIFGYLSALLYLGSRIPQILLNFKRKSCEGISFLFFLFACLGNTTFIFSVIVISLDWKYLIMNASWLVGSIGTLFMDFVIFSQFFIYKRNKKFILN
Protein: Cyclin 9 (Q8IEW6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MAGFTETPSWPSLSCEQSSAAAVSVSYSPFVVEMSYYTIAVQAYSMTRYVVENLRLDSAVVGTAMTYWHIFVSVHGLKKVDEIVLSAACTFLASKVEHHKVRLSDIVALVFEVXPVGGVMESWRDVVGQAELLLCYTLKFNFQVIHPVNRINELVFDGNKAVLECAQRLFLLSFVTPLCTRASAEEIVEALVYLAADGAERLEVYANGFNITSSERRDGIISVMLDALVAMRKTTKLPKIDNVISARRKRLREQESTRPSVACSSVGTASTDNTPCAPSVE
Protein: TGF-beta receptor type-1 (EC 2.7.11.30) (Transforming growth factor-beta receptor type I) (F8VRH6)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTGPFSVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRCKLLESSLVFPASITVPNTW
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 (EC 2.8.2.30) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1) (3-OST-3B) (Heparan sulfate 3-O-sulfotransferase 3B1) (m3-OST-3B) (Q9QZS6)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:10520990}; Single-pass type II membrane protein {ECO:0000305|PubMed:10520990}.
Interaction partners:
- Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MGQRLSGGRSCLDVPGRFLPQPPPPPPPVRRKLALLFAMLCIWLYMFLYSCAGSCTAAPGLLLLGSGSRATHAQPALVTAPNETSPKMPFRAPPANSLAAGKDKTVGAGSQEEQSPEAPDSPSPISSFFSGAGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYHKGLAWYRDLMPRTLKGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPSFESLTFRNRSAGLIDTSWSAIQIGLYAKHLEPWLRHFPLGQMLFVSGERLVSDPAGELRRVQDFLGLKRIITDKHFYFNQTKGFPCLKKAEGSGKPHCLGKTKGRAHPTIAREVLRQLRDFYRPFNRKFYQMTGRDFGWD
Protein: ARO3 (A0A178UVG5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGDLAKQILSRPIQLADQVVKAGDEATINKQECADIKSKTEKLAALLRQAARASSDLYERPTRRILDDTENVLEKALTMVQRCRDDGYIMRLFNIIPAAAFRKMISQLENSVGDVSWLLRVSTPAGNDDDEGFGYLGLPPIAANEPILCLIWEQIAVLMTGSPEDKSDAAASLASLARDNDRYVKLIVEEGGVNPLLKLVKEGKIDGQENAARTIGLLGRDPESVEHMIQLGVCSVLSSILKEGSMKVQAVVAWAVSELVSGNHAKCQELFAQNNVIRLLVSHLAFETVQEHSKYAVVAGRATSMHHAVVMASKISSSKENLPALNEEEDDDNHIGVSSPMTNQMHSIVATTMAMKAVGSGSKSNLSSRFVTGDDDKPPEKIPEKSYSMSSQIKAYGSIAHQSRNASVTRGRELEDPVTKTYMKAMAARALWKLAVGNSSICRVITESRALLCFAVLLDKGDEETKYNTAMAIMEITAVAEENADLRRSAFRRTSPACKAVVDQLFRIVENADAGSDLLIPCVRSIGNLARTFKSAETHMIVPLVKLLDDGEPDLAAEVAIALAKFATEDNFLGKEHSRTIIEAGGSKLLVQLAYFGENGAQIPAMVLLSYVAMNVPDSEQLAKDEVLTVLEWSSKQANVLEDEDMEALLYEAKSRLELYQSRGSRGFHL
Protein: Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) (P30520)
Organism: Homo sapiens (Human)
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}. Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}. Note=Partially associated with particulate fractions.
Interaction partners:
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- AMP deaminase 3
- Argininosuccinate synthase
- AMP deaminase 1
- AMP deaminase 2
- Inosine-5'-monophosphate dehydrogenase 2
- Trifunctional purine biosynthetic protein adenosine-3
- Inosine-5'-monophosphate dehydrogenase 1
- GMP reductase 1
Sequence:
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLEGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLRMCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALALTKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKELPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Protein: Cell polarity protein alp21 (Altered polarity protein 21) (Suppressor of tsm one protein 1) (Q10303)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for microtubule and spindle assembly. Involved in the proper folding of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10341216}.
Interaction partners:
- Tubulin-folding cofactor D
- Cell polarity protein alp11
- Tubulin-specific chaperone C
- Tubulin-specific chaperone A
- ADP-ribosylation factor-like protein alp41
- Tubulin beta chain
Sequence:
MHISTGMVRASISNTLVTLTIEGNNDRYQVILDKNVNAKQFVKTCWRNKKPLIVKEGKIFVDKGFPFDPCRTFLEALYEKYSYSSPLPSSVEFKSGKQVEFCGFEKIQSKQRDLKSLRVIILDNYRIEDIEIEYEYSKILPEVIDLDLSRNLFHEFFPILKLCSQLPSLRNLTLDSNLFSNFISSNTVLLIPHLTQLSVNGCGLNSKDVQWITETFPSLEVLYLEANEIILSKATSFKNLQFLQTLSLANNLNLYSADGYAVDVFQGINNLNLSSTSLADVAELPVHTLHKLTFLDISENNIRDIRSLDHLRTLENLKHLRITLSYFNKPTDIAKLLVIARIPSLVKLNDVNISPNERLDAELYYTSCIRKLVIDNEIKDVEELTKIEPFWEEIWKSHELPSIQFHLEASINDWTSGILKNRITKGIKISSINSGATMLLKLHYNWKLLDIKALISYHFAIPVHTSTFVFASSERDVSFSPKTVRDDQKRLFELPFTCTFIDVYAKESGNV
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (P36587)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Calcium-transporting ATPase 2
- Sulfite reductase subunit beta
- Probable cytochrome b5 1
- Probable cytochrome b5 2
- Uncharacterized hydrolase C9G1.08c
- Acyl-protein thioesterase 1
- Heat shock protein 90 homolog
- N-acetyltransferase 9-like protein
- Lanosterol 14-alpha demethylase erg11
Sequence:
MKTYEYVLLVIILILSLCYFIYNNFLNKPKAPERRVVATDSIVELMEAEKLTAAVFFGSQTGTAEDFAYRFSTEAKANFNLTNMVFDLENYDLTDLDNFDRSKLLVFFLATYGEGEPTDNAEAFLQLLEGDDTVFSSGKGIEDTPFEGIRYAIFGLGNHTYEYYNAMAKKVDAAMTRLGATRVGNLGLGDDAAGMLEEDYLQWKDDTLPEIGKLFHLQEVHKEYNPMFEVIEKPEISNTSSTVFLGEPSRQQLKGNVASKAPRSQANPFFSSPVRSLELFKSGSRNCLHLELDIADSGMRYQTGDYASICPMNPSQAVDDLLEVLGLKEKRDTVIIVKPIDTLDKAPVLSPTTYDTVFRYYYEICGIVSRQLLSFIAPFAPTPESKQELEKLGNDYDYFKKNVVDLHLNLAQVLRRVSPDAPFTKLPFSMLLENMAHMKPRYYSISSSSVVHPDKVHVTAVVDKKEWTDKNHIFYGLTTNYLLAHCRHMHGEKIPHPNGLEYTLEGPRKNWTGKIPMFVKKSTFRLAPPDVPIIMVGPGTGVAPFRGFVMERANLASKGVKVAKTLLFYGCQYSDKDFLYKEEWQQYKDVLKDSFELITAFSREQDHKIYVQHRLLEHSDTIAKLVEEGAAFYICGDADHMAKDVVNALASILTTVDVDGMKAVKALRDDNRFFEDTW
Protein: Histamine H1 receptor (Q195J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MCFLTTLTSCDTLERPMESTTTLTTANSQFKRIDNTTLLIPSAPLHHHINNAVLGIFLGMLSLLTVIMNLLVLFAVRKERTLHTVGNLYIVSLSIADLIVGATVMPLNLVYLLEDQWKLGHVVCQFWLVMDYVASTASIFSLFILCLDRYRSVRHPLQYLKYRTRGRATLLICSAWLLSMTWTIPILGWRMFASVDKKTELENQCDTDFRFVTWFKVLTAILNFYIPSFLMLVFYSQIFIAVRDHYREWENFAGPALKTDATDTLTNGLQLQITKASEKESLALNAYSQNEGLLDQYSLEQPYNSRENTEEMTSEPKRKMCYKKKAIFNLSKRMRKSVPDSEISFQSDDGETVAEGRPSLSLAFLQSENTAQPQTFINVSDCNVLVPNSVGNICESAPTVDIHNYTAVLCTPPSPPSPWAENSPPLDASIALPAKQSWQKLCEQSKQSIHSMRIRKERKAARQLGFIIGVFMVCWIPYFITFMVMALCETCVHHDLHMFTIWLGYINSTLNPFIYPLCNENFKRVFKKIFHMSR
Protein: Thymidylate kinase (PfTMK) (PfTMPK) (EC 2.7.4.8) (EC 2.7.4.9) (Thymidine monophosphate kinase) (Thymidylate/guanylate kinase) (Q8I4S1)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP. Can also phosphorylate dGMP and to a lesser extent GMP, dUMP and dIMP. Can use either ATP or dATP as phosphate donors in presence of Mg(2+).
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase
- nucleoside-diphosphate kinase
- Ribonucleoside-diphosphate reductase small chain, putative
- Ribonucleoside-diphosphate reductase small chain, putative
- Uncharacterized protein
- orotate phosphoribosyltransferase
- Thioredoxin-like protein
Sequence:
MTDDKKKGKFIVFEGLDRSGKSTQSKLLVEYLKNNNVEVKHLYFPNRETGIGQIISKYLKMENSMSNETIHLLFSANRWEHMNEIKSLLLKGIWVVCDRYAYSGVAYSSGALNLNKTWCMNPDQGLIKPDVVFYLNVPPNYAQNRSDYGEEIYEKVETQKKIYETYKHFAHEDYWINIDATRKIEDIHNDIVKEVTKIKVEPEEFNFLWS
Protein: Ethylene-responsive transcription factor 2 (AtERF2) (Ethylene-responsive element-binding factor 2) (EREBP-2) (O80338)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. Involved in disease resistance pathways.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein ETHYLENE INSENSITIVE 3
- ETHYLENE INSENSITIVE 3-like 1 protein
- Ethylene-responsive transcription factor 1B
- ETHYLENE INSENSITIVE 3-like 2 protein
- ETHYLENE INSENSITIVE 3-like 3 protein
- ETHYLENE INSENSITIVE 3-like 5 protein
- Putative ETHYLENE INSENSITIVE 3-like 4 protein
- Floral homeotic protein APETALA 2
- Defensin-like protein 16
- 1-aminocyclopropane-1-carboxylate synthase 6
Sequence:
MYGQCNIESDYALLESITRHLLGGGGENELRLNESTPSSCFTESWGGLPLKENDSEDMLVYGLLKDAFHFDTSSSDLSCLFDFPAVKVEPTENFTAMEEKPKKAIPVTETAVKAKHYRGVRQRPWGKFAAEIRDPAKNGARVWLGTFETAEDAALAYDIAAFRMRGSRALLNFPLRVNSGEPDPVRITSKRSSSSSSSSSSSTSSSENGKLKRRRKAENLTSEVVQVKCEVGDETRVDELLVS
Protein: Glutathione hydrolase proenzyme 1 (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain] (Q9US04)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Cys-Gly metallodipeptidase dug1
- Glutathione synthetase large chain
- Putative aminopeptidase C13A11.05
- Glutamate--cysteine ligase
- Putative glutamate--cysteine ligase regulatory subunit
- Glutathione reductase
- Glutathione S-transferase 3
- Glutathione S-transferase 2
- Glutathione S-transferase 1
- Glutathione hydrolase proenzyme 2
Sequence:
MGINTSSAQSSGAASIARSSVNVKSGNRHLSSNKKSATSALEERASRPSILVTFLVLAGTILSLYIWPILSPDLFFANQRCSFKYKNKGSQRVVVEGKNGVVATEEETCSQIGVGILKAGGNAVDAAIASGICIGAVNSFSSGIGGGGFMLIRHPNGTAHSLNFRETAPAGASKNMFHGNSTLSQVGGLSVAVPGEIAGYERAWKMYGSLPWHKLFEPTIRLMRDGMPMPKELASRIRRPEFSYFKTHPDWSKIFAPEGVFLHVGEKFYRPALASTLEEIAKFGPEVFYTGKIAERLVKFVQQQGGILTMEDMANFSVVVEEPIYGNFYDREVITCGSPCSGEALILGLNVLSKVDLSEGTSILGCEMTDIGVHHLIETMKWMSAGRTVLADPTFYNNTDHVEQLLSLEYADEIRNNISNERTFDFTHYKAEYDFPNDHGTTHLSVIDKDNMAVGLTASINLMFGSQLLEPETGIILNDHMDDFASPGIVNAFGLSPSPYNFIAPGKRPQSSAVPTILVYNGEVEMVLGGSGGSRIVTAVLDTIIKKYKWGKSLLESVESPRFHHQLMPNIVYIDETVEIEVLRALEKFGHIVDLIPVQYPFSEIQAVFRTNGTLYGLSDSRKQAVAAAY
Protein: Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Q9XZ68)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- LD45906p
- Rab proteins geranylgeranyltransferase component A
- PRL-1 phosphatase
- FI01544p
- LD34211p
- Rab11
- Uncharacterized protein, isoform B
- CG2885
Sequence:
MDFTTFVKPSNGGGDSGGGGDADGGGQKLQFWKHVEYIENHGKQEDDYEYCMTEFLRMSGIYWGTTALDIMGQLERLERKSIIEFVKRCQCPNTGGFAPCEGHDPHLLYTLSAIQILCTYDALEEIDREAVVRFVVGLQQPDGSFFGDKWGEVDTRFSFCAVASLTLLGRMEQTIDVEKAVKFVLSCCNQTDGGFGSKPGAESHAGLIYCCVGFFSLTHRLHLLDVDKLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLTIMGRLHWISSEKLQQFILSCQDTETGGFSDRTGNMPDIFHTLFGIGGLSLLGHSGLKAINPTLCMPQYIIDRLGIKPQLLPRP
Protein: Mid-1-related chloride channel domain-containing protein (Q9FN31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- SUMO-conjugating enzyme SCE1
Sequence:
MAASTSQLEDTTREIIEGTSILNIDDTSILNIDDVMTSQLEDTIEKLKKVVRSLEEINRNSTMASLTYKLYRFILEKEDEAAAELNAVDTDSIETKLVKLENKQRYIREVEDNPIDIRSLYRPKLVKLLKERGFTPFPSEDKPFSHYDYLDVALHMELPIQKYEELCDQKNVLQDIVSILKRIIDAYQH
Protein: DNA cross-link repair 1A protein (Beta-lactamase DCLRE1A) (EC 3.5.2.6) (SNM1 homolog A) (hSNM1) (hSNM1A) (Q6PJP8)
Organism: Homo sapiens (Human)
Function: May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin. Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem).
Subcellular location: Nucleus {ECO:0000269|PubMed:10848582, ECO:0000269|PubMed:12446782, ECO:0000269|PubMed:15572677}. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- Fanconi anemia group D2 protein
- Fanconi anemia group M protein
- Structure-specific endonuclease subunit MUS81
- Fanconi anemia group I protein
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit SLX1
- Fanconi-associated nuclease 1
- Zinc phosphodiesterase ELAC protein 2
Sequence:
MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGKLCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPRSETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSPSPASGGSFSETKSGVLCSLEERWSSYQNQTDNSVSNDPLLMTQYFKKSPSLTEASEKISTHIQTSQQALQFTDFVENDKLVGVALRLANNSEHINLPLPENDFSDCEISYSPLQSDEDTHDIDEKPDDSQEQLFFTESSKDGSLEEDDDSCGFFKKRHGPLLKDQDESCPKVNSFLTRDKYDEGLYRFNSLNDLSQPISQNNESTLPYDLACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEESSVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNTNSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPSTKVMKQMDIGVYFGLPPKRKEEKLLGESALEGINLNPVPSPNQKRSSQCKRKAEKSLSDLEFDASTLHESQLSVELSSERSQRQKKRCRKSNSLQEGACQKRSDHLINTESEAVNLSKVKVFTKSAHGGLQRGNKKIPESSNVGGSRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPLDTECIVNGVKVVLLDANHCPGAVMILFYLPNGTVILHTGDFRADPSMERSLLADQKVHMLYLDTTYCSPEYTFPSQQEVIRFAINTAFEAVTLNPHALVVCGTYSIGKEKVFLAIADVLGSKVGMSQEKYKTLQCLNIPEINSLITTDMCSSLVHLLPMMQINFKGLQSHLKKCGGKYNQILAFRPTGWTHSNKFTRIADVIPQTKGNISIYGIPYSEHSSYLEMKRFVQWLKPQKIIPTVNVGTWKSRSTMEKYFREWKLEAGY
Protein: Outer membrane protein, MSP2 family (Q2GIG8)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MVCCVSRVVLYIASVILLMLIMGEDASAAIYKDDLPPNSKKFYVALDYAPALSRVSTFDIVGDGKTHIALPYLKNDQEDRFNAEAIDWDAPNLSVQFKNSVLMSWVGSIGYKMMGGRLELEVGHEKFGARVSSGENREENSDVAYVFFSRLLPYYLVSAQYEKLISGLANLTEDEILAFANGVADQRPDLDKKICKKARLGGDDRGTDAQAACRDSIKGADVGGFGAFMRKAIGTYLMWRYNGGSDRYGLERGGRSVNSKDIVSDIKELPKEERKILAGILAAATGYGVVVEIPSVAATSVMVNACYDHNVSLTRKRASAYSCVGLGSTFVEIVDEHRAAKLAYRLKAGLSYNFASGVTAFVGGFYHHIIGDSWYDRVPMRTVFLDEKTGERPVKTGKVDLSLDYIGAECGIRLIL
Protein: Integrin beta-7 (Integrin beta-P) (M290 IEL antigen) (P26011)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is involved in adhesive interactions of leukocytes. It is a receptor for fibronectin and recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Integrin alpha-4/beta-7 is also a receptor for MADCAM1 and VCAM1. It recognizes the sequence L-D-T in MADCAM1. Integrin alpha-E/beta-7 is a receptor for E-cadherin.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Integrin alpha-E
- Integrin alpha-4
- Fibronectin
- Vascular cell adhesion protein 1
- Integrin alpha-5
- Mucosal addressin cell adhesion molecule 1
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
Sequence:
MVDSSTVLIFLLVLGGGQSELDTKITSSGEAAEWEDPDLSLQGSCQPVPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPAQELEEPRGRQEVLQDKPLSQGDRGEGATQLAPQRIRVTLRPGEPQKFRVRFLRAAGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLHHPCPSRLERCQPPFSFHHVLSLTGDAQAFEREVGRQNVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGRCHLDSNGVYTNSAEFDYPSVGQVAQALTAANIQPIFAVTGATLPVYQELRQLIPKSAVGELSEDSSNVVQLIMDAYDSLSSTVTLEHSPLPPGVSISFESHCKGPEKTEGEAGDRGQCNDVRVNQTVDFWVTLQATHCLPEAHVLRLWALGFSEELTVELHTVCDCNCGDAQPHAPYCSDGQGDLQCGICSCAPGRLGQLCECSEADLSSPDLESGCRAPNGTGPLCSGKGRCQCGRCSCSGQSSGRLCECDDASCERHEGILCGGFGHCQCGVCHCHANHTGRACECSKSVDSCVSPEGGLCSGHGYCKCNRCQCLDGYYGALCDQCLGCKSPCEQYRDCAECGAFGTGPLAANCSVVCADVNVTLTLAPNLDDGWCKERTIDNQLFFFLVEHAASGIVLRVRPQEKGVDHTRAIILGCTGGIVAVGLGLVLAYRLSVEIYDRREYRRFEKEQQQLNWKQDNNPLYKSAITTTVNPRFQGTNGRSPSLSLTREAD
Protein: Selenide, water dikinase 2 (EC 2.7.9.3) (Selenium donor protein 2) (Selenophosphate synthase 2) (Q99611)
Organism: Homo sapiens (Human)
Function: Synthesizes selenophosphate from selenide and ATP.
Interaction partners:
- O-phosphoseryl-tRNA
- Selenocysteine lyase
- Thioredoxin reductase 3
- Thioredoxin reductase 1, cytoplasmic
- Thioredoxin reductase 2, mitochondrial
- Selenide, water dikinase 1
- L-seryl-tRNA
- Thioredoxin reductase-like selenoprotein T
- Type I iodothyronine deiodinase
- Protein adenylyltransferase SelO, mitochondrial
Sequence:
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGUGCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMDSCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVSQSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPDSAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNRTAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRFGLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKPRVIEVLPRGATAAVLAPDSSNASSEPSS