wanglab/gogpt-training-data huggingface dataset:
Protein: Glutathione transferase (Q54B85)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Glutathione reductase
- Putative glutathione S-transferase alpha-5
- Putative glutathione S-transferase alpha-3
- Putative glutathione S-transferase alpha-2
- Putative glutathione S-transferase alpha-4
- Putative glutathione S-transferase alpha-1
- Glutathione synthetase
- Uncharacterized protein
- Probable microsomal glutathione S-transferase
- glutathione-specific gamma-glutamylcyclotransferase
Sequence:
MNCINNYNNNNNNNNNNNKIMIPDLKNNDTGSSADDGRSEGVADYQVYGFYTSCSFKVYFMFEELNIPYQTCLVNIRSGEHFKGEFAEMSPNNKIPMLIDNTYSVDSGDDDEPLKIFESGAILLYLAEKYQKFLPPLSKPKERCQVQQWLSWQISEMQPALTSYVYYFMMAPEPVAFGMEKADQDLHKILKVLDKRLDDGRKYICNEFSIADIACFGFGSYFNLNVFKGWNKYENVVRWVNTMSSRPSISKLLPIVEQTLRVRKLKRLDNQELVL
Protein: Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) (Q00576)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99LH2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99LH2}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q99LH2}.
Interaction partners:
Sequence:
MASCVGSRTLSKDDVNYRMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADIMEYAVNCHVITWERIVSHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWCRILFIGCITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVFWLLCVAFTTFLCLYGMVWYAEHYGHREKTYSECEDGTPEISWHHGKGSKGSEDSPPKHSSNNESHSSRRRNRHSKSKVTNGVGKK
Protein: Olfactory receptor 8B3 (Olfactory receptor OR11-311) (Q8NGG8)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 8B2
- Olfactory receptor 8B8
- Olfactory receptor 8B4
Sequence:
MLARNNSLVTEFILAGLTDHPEFQQPLFFLFLVVYIVTMVGNLGLIILFGLNSHLHTPMYYFLFNLSFIDLCYSSVFTPKMLMNFVSKKNIISYVGCMTQLFFFLFFVISECYMLTSMAYDRYVAICNPLLYKVTMSHQVCSMLTFAAYIMGLAGATAHTGCMLRLTFCSANIINHYLCDILPLLQLSCTSTYVNEVVVLIVVGINIMVPSCTILISYVFIVTSILHIKSTQGRSKAFSTCSSHVIALSLFFGSAAFMYIKYSSGSMEQGKVSSVFYTNVVPMLNPLIYSLRNKDVKVALRKALIKIQRRNIF
Protein: Chemokine XC receptor 1 (Lymphotactin receptor) (SCM1 receptor) (XC chemokine receptor 1) (mXCR1) (Q9R0M1)
Organism: Mus musculus (Mouse)
Function: Receptor for chemokines SCYC1 and SCYC2. Subsequently transduces a signal by increasing the intracellular calcium ions level. Receptor for XCL1/Lymphotactin (Probable).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Lymphotactin
- Guanine nucleotide-binding protein G
- Fractalkine
- C-C motif chemokine 5
- C-X-C motif chemokine 9
- Stromal cell-derived factor 1
- C-C motif chemokine 2
- C-C motif chemokine 1
- C-type lectin domain family 9 member A
- C-C motif chemokine 19
Sequence:
MESSTAFYDYHDKLSLLCENNVIFFSTISTIVLYSLVFLLSLVGNSLVLWVLVKYENLESLTNIFILNLCLSDLMFSCLLPVLISAQWSWFLGDFFCKFFNMIFGISLYSSIFFLTIMTIHRYLSVVSPISTLGIHTLRCRVLVTSCVWAASILFSIPDAVFHKVISLNCKYSEHHGFLASVYQHNIFFLLSMGIILFCYVQILRTLFRTRSRQRHRTVRLIFTVVVAYFLSWAPYNLTLFLKTGIIQQSCESLQQLDIAMIICRHLAFSHCCFNPVLYVFVGIKFRRHLKHLFQQVWLCRKTSSTVPCSPGTFTYEGPSFY
Protein: Probable galacturonosyltransferase-like 5 (EC 2.4.1.-) (Q9FWY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pectin and/or xylans biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Galacturonosyltransferase
- Pectinesterase inhibitor 6
- UDP-rhamnose/UDP-galactose transporter 2
- UDP-URONIC ACID TRANSPORTER 1
- Subtilisin-like protease SBT1.7
- Transmembrane E3 ubiquitin-protein ligase FLY1
- Beta-galactosidase 6
- Peroxidase 36
- Homeobox-leucine zipper protein GLABRA 2
Sequence:
MHWITRFSAFFSAALAMILLSPSLQSFSPAAAIRSSHPYADEFKPQQNSDYSSFRESPMFRNAEQCRSSGEDSGVCNPNLVHVAITLDIDYLRGSIAAVNSILQHSMCPQSVFFHFLVSSESQNLESLIRSTFPKLTNLKIYYFAPETVQSLISSSVRQALEQPLNYARNYLADLLEPCVKRVIYLDSDLVVVDDIVKLWKTGLGQRTIGAPEYCHANFTKYFTGGFWSDKRFNGTFKGRNPCYFNTGVMVIDLKKWRQFRFTKRIEKWMEIQKIERIYELGSLPPFLLVFAGHVAPISHRWNQHGLGGDNVRGSCRDLHSGPVSLLHWSGSGKPWLRLDSKLPCPLDTLWAPYDLYKHSH
Protein: Deubiquitinase MYSM1 (2A-DUB) (EC 3.4.19.-) (Myb-like, SWIRM and MPN domain-containing protein 1) (Q69Z66)
Organism: Mus musculus (Mouse)
Function: Metalloprotease with deubiquitinase activity that plays important regulator roles in hematopoietic stem cell function, blood cell production and immune response. Participates in the normal programming of B-cell responses to antigen after the maturation process. Within the cytoplasm, plays critical roles in the repression of innate immunity and autoimmunity. Removes 'Lys-63'-linked polyubiquitins from TRAF3 and TRAF6 complexes. Attenuates NOD2-mediated inflammation and tissue injury by promoting 'Lys-63'-linked deubiquitination of RIPK2 component. Suppresses the CGAS-STING1 signaling pathway by cleaving STING1 'Lys-63'-linked ubiquitin chains. In the nucleus, acts as a hematopoietic transcription regulator derepressing a range of genes essential for normal stem cell differentiation including EBF1 and PAX5 in B-cells, ID2 in NK-cell progenitor or FLT3 in dendritic cell precursors. Deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, leading to dissociation of histone H1 from the nucleosome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:30405132}. Cytoplasm {ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:30405132}. Note=Localizes to the cytoplasm in response to bacterial infection. {ECO:0000269|PubMed:26474655}.
Interaction partners:
- Histone acetyltransferase KAT2B
- Protein polybromo-1
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 8
- Ubiquitin-like protein FUBI
- Histone acetyltransferase p300
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- 26S proteasome regulatory subunit 6A
Sequence:
MEAEEADVDVEGDVAAAAQPGNDESTASVFQDHYLDSTWRRENGCLPWTLDSTISDENRAIIEKMLLEEEYYLSNKSLPGKFWVNQKEDNKKYTNSLQKSSKAMVDSPAKPASHSVKWTVEEKELFEQGLAKFGRRWTKIATLLKSRTVLQVKSYARQYFKNKVKWDVEKETPTQKSSSDLQVKNKDDRTKAWAAACLRGSADPCLNAVKIEKLSDDEDVDITDELDELTSQTSQNSGSHLTLDVPNSKMYTTNQGELCQEGPLAKSSGESLQNVKQGEGEACSSSEIASWAEKQKSTDKNSAELNEKYNKVVEEHTLHRGEVREEAKHSPSPEPCERQDSSGNEMLLPPCQIEEENHEGEELKPPEQEVEIDRNVIQEEEKQAIPEFFEGRQTKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLKNCGDVNCIGRIHTYLELIGAINFGCEQAVYNRPQPLDKVRAADRKDAEAAYQLAWRLQSMRTRRRRVRDPWGNWCDAKDLEGQTFEHLSVEEMARRKEEEKCKPIKFSKASKLPKSSLDPFQLIPCNFFSEEKQEPFQVKVAAEALLIMNLHAHVSMAEVIGLLGGRYSEADKVLEVCAAEPCNSLSTGLQCEMDPVSQTQASETLALRGYSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRSNPLPYSQITCLVISEEVSPDGTYRLPYKFEVQQMLEEPQWELVFEKTRWIIEKYRLSNSSVPMDRIFRRDSDLTCLQKLLECLRKTLSKVANCFIAEEFLTQIENLFLSNYKSKEENGLAEEDSTKELFM
Protein: Sidestep, isoform C (A0A0B4K7N1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Beaten path Ia, isoform B
Sequence:
MQLLLPTSGMPTNTLETETPAMQTTYWPRQTGNSKSKSNTNCKCNINTHRKSRTRCPDNGKTIWAVGFTLVLLTCLQQLKSVSADEESQDFQKNIPARLVWAALGKTVELPCDLTPPTSQDSVKLLLWFKDTTGIPLYSLDSRGGNVKLAPHAAIASDLGQRLFFSIGDNPKDSRLQINDVKPEDGGVYRCRVDFFNSPTRNFRHNLTLVVPPEEPRIFDAQGKEISQMAGPFREGYELFLCCQVRGGRPPPKVTWWRDDTELIGTSHTSVEEGATVMVNQLLIGTTTRDFYGIRIECRAQGTRLVDPVRKDVTVQVYLKPVRVKIATPNELLTAGQPMPIRCESWGSYPAAKITWLLDGEPIRNAEVTVHSDKEDGNITTSILTLKVTSENDNAELTCRATNPWFSGGAIEDKRIIRVAYPPTVSVHLANEDPSRLVTRAEGQNVTFKCRADARPPVTSYSWFKNGMRMSGESTEIMHLTQLERESAGAYACGATNTEGETRSSSLTLKVQFSPRCKSGTEQTSIGAVSLHSILVKCEVDADPPDSVRFSWTYNNTRNVSPVLNSRIQSNGLASTVTYLPQTDSELITLACWASNAVGRQTTPCLVHILPANTPEAPKACELRNDTVLEVVCVAGSDGGLSQYFMLEVVGGDPLYSGDPGGSAGQGRGQFSEAIGLGDNEISTLNDQATSAPIFRMQENSPQFRLNNLEPGREYQFLVYAVNAKGRSEPPVVIENVRVAAQLGPYDESILSEDPTPAETTHHGGGGVGGSGSSSGLGTGASTGSGPEKQSTLLILAAVVVIGAVVVTSIIVAGIVVVCRHRPRPPEPQEVRKSMRPARNDVPSMYIEEDELNELEEGGGRAADIRARVAPPNSHLCGGGGMPMPGGVGSSGGAIVGVAGPHHYISESFIQYAQPSLNGDVLLPLLVTSSQPCSTNSTISSVVLAMPQAKLCPDPASRNTAWPPEYPDLILPRGELEFTTLDPTLK
Protein: Fc receptor-like protein 2 (FcR-like protein 2) (FcRL2) (Fc receptor homolog 2) (FcRH2) (IFGP family protein 4) (Immunoglobulin receptor translocation-associated protein 4) (SH2 domain-containing phosphatase anchor protein 1) (CD antigen CD307b) (Q96LA5)
Organism: Homo sapiens (Human)
Function: May have an regulatory role in normal and neoplastic B cell development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16849395}; Single-pass type I membrane protein {ECO:0000269|PubMed:16849395}.
Interaction partners:
- Polymeric immunoglobulin receptor
- B-lymphocyte antigen CD19
Sequence:
MLLWSLLVIFDAVTEQADSLTLVAPSSVFEGDSIVLKCQGEQNWKIQKMAYHKDNKELSVFKKFSDFLIQSAVLSDSGNYFCSTKGQLFLWDKTSNIVKIKVQELFQRPVLTASSFQPIEGGPVSLKCETRLSPQRLDVQLQFCFFRENQVLGSGWSSSPELQISAVWSEDTGSYWCKAETVTHRIRKQSLQSQIHVQRIPISNVSLEIRAPGGQVTEGQKLILLCSVAGGTGNVTFSWYREATGTSMGKKTQRSLSAELEIPAVKESDAGKYYCRADNGHVPIQSKVVNIPVRIPVSRPVLTLRSPGAQAAVGDLLELHCEALRGSPPILYQFYHEDVTLGNSSAPSGGGASFNLSLTAEHSGNYSCEANNGLGAQCSEAVPVSISGPDGYRRDLMTAGVLWGLFGVLGFTGVALLLYALFHKISGESSATNEPRGASRPNPQEFTYSSPTPDMEELQPVYVNVGSVDVDVVYSQVWSMQQPESSANIRTLLENKDSQVIYSSVKKS
Protein: G-protein coupled receptor 3 (ACCA orphan receptor) (P46089)
Organism: Homo sapiens (Human)
Function: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Has a potential role in modulating a number of brain functions, including behavioral responses to stress (By similarity), amyloid-beta peptide generation in neurons and neurite outgrowth (By similarity). Maintains also meiotic arrest in oocytes (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Beta-arrestin-2
- Beta-arrestin-1
- N-arachidonyl glycine receptor
Sequence:
MMWGAGSPLAWLSAGSGNVNVSSVGPAEGPTGPAAPLPSPKAWDVVLCISGTLVSCENALVVAIIVGTPAFRAPMFLLVGSLAVADLLAGLGLVLHFAAVFCIGSAEMSLVLVGVLAMAFTASIGSLLAITVDRYLSLYNALTYYSETTVTRTYVMLALVWGGALGLGLLPVLAWNCLDGLTTCGVVYPLSKNHLVVLAIAFFMVFGIMLQLYAQICRIVCRHAQQIALQRHLLPASHYVATRKGIATLAVVLGAFAACWLPFTVYCLLGDAHSPPLYTYLTLLPATYNSMINPIIYAFRNQDVQKVLWAVCCCCSSSKIPFRSRSPSDV
Protein: ADP ribosylation factor like GTPase 1 (cDNA FLJ50309, highly similar to ADP-ribosylation factor-like protein 1) (B4DZG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTSSEMANSLGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETLKSRQ
Protein: Protocadherin gamma B2 (Q8K4A8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
IASQSAKTEFNFLNVTPEVAPQDLLCGDDSWVPGTLGDTDVPFVSDSISKQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNG
Protein: Protein C' (P69738)
Organism: Sendai virus (strain Nagoya) (SeV)
Function: The different products prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN-alpha/beta pathway requires binding to STAT1 in the cytoplasm. They inhibit IFN-gamma induced serine phosphorylation of STAT1. Block the IFN-gamma pathway by binding to and stabilizing the parallel form of the STAT1 dimer, further inducing high-molecular-weight complex formation and inhibition of transcription by IFN-gamma (By similarity). May also have a role in preventing the cell to enter apoptosis. Modulate regulation of viral transcription and replication. Overexpression inhibits the viral RNA polymerase. The absence of all C', C, Y1 and Y2 proteins leads to viral delayed growth. Plays an important role in virion particles release. Modulates virion shape.
Subcellular location: Host cytoplasm {ECO:0000250|UniProtKB:P04862}. Note=Protein C' seems to localize around the Golgi. {ECO:0000250|UniProtKB:P04862}.
Interaction partners:
Sequence:
MASATLTAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSMLSCRVNQLTSEGTEAGSTTPSTLPKDQALLIEPKVRAKEKSQHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWTMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQVIMEEAWSLAAHIVQE
Protein: Nicotinic receptor-associated protein 1 (Q9XUB9)
Organism: Caenorhabditis elegans
Function: Exhibits calcium-dependent phospholipid binding properties (By similarity). May function in membrane trafficking. Regulates synaptic levels of nicotinic acetylcholine receptor subunit lev-1 and unc-38 in the nerve cord. Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and levamisole. Affects directional sperm motility.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15990870}; Peripheral membrane protein {ECO:0000269|PubMed:15990870}.
Interaction partners:
- Nicalin
Sequence:
MNQPIGIADSSRPKTNVRLTISANNLMDLDVFSKSDPICLIYEKTSGRKATTTEEITVPTWKDKQWTERGRTEVVMNNLNPQFTKTFLLPYFFEETQLLRFEIYDADSPTVGQDLSSHDFLGRFECVLAQIVSYSTLKAHLGKTGQIGAQWRNKDKNTKTGSITIYAEEDEKAEKIQFDVCGEGLDKKDFFGKSDPYLNFKRKFDDGSTHLIHRTEVKPKTLDPRWATVQINTQTLCAKDGDRPIIIECYDHDKWKKGEEPRGDAKFSRDDLIGTAQTTLNELLRGSSDAVEILLTNEKKKAKKGDKYKCSGTLKIWNSRIVIEPTFLDFISGGTQLDFAVAVDFTASNGPPKSSSSLHFMSADRPNQYELALRSVLSICQHYNSSKTFEAFGFGAKLPNQSSVSAIFPLDLQRGTSEVVGITGVMTAYRHALSNVQLYGPTNFAPIIENVARKAQNMIHDSARYQILLIITDGIISDMHATIRSIISASGLPLSIIIIGVGNEDFEKMHELDSDDALLQQDSRIAQRDIVQFVTMREFLNNGQGLYLDPDVIQENLAREVLYEVPAQLTGYMKQRGFQPRPVDDPWRRDSPPPEFDPILDGTGRRAPMLQAPPAGFQYPVYADTSIASAPPMY
Protein: Palmitoyltransferase PFA5 (EC 2.3.1.225) (Protein fatty acyltransferase 5) (Q03289)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Palmitoyltransferase SWF1
- Probable palmitoyltransferase AKR2
- Palmitoyltransferase AKR1
- Ras modification protein ERF4
Sequence:
MALSWNIRIRRRSWFRFILPIIVLGLLCYGTWAYCHKLCYEQVDKRLRQKSVSVGLICAVCFLDVVVIFIWLQIVILVGPGTQPHVAPFLILPIASEEKTSNTSQNTSVEYDAVVPPKCYQSDPHGYPIWCSECQSLKMERTHHSSELGHCIPRFDHYCMWIGTVIGRDNYRLFVQFAAYFSTLLLIMWVSICVYIRIITQHNHNYSPNLNANIISTLVFAILGWLLTASLLASSIFYMSQNKTSLEAIIDSKRKKFGTRKIFCYYSEANKLRFVVEFDRSEFHSFWDKKSILANIKDFMGSNILMWIIPLGKPYTSRCKSDGKSGSKTTLVEILGPYEETLSDYTIQAIEDKISRGEYLATLRASGDDSDPAY
Protein: Cullin-associated NEDD8-dissociated protein 2 (Cullin-associated and neddylation-dissociated protein 2) (TBP-interacting protein b) (TBP-interacting protein of 120 kDa B) (TBP-interacting protein 120B) (p120 CAND2) (Q9R0L4)
Organism: Rattus norvegicus (Rat)
Function: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes.
Subcellular location: Nucleus.
Interaction partners:
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cullin-3
Sequence:
MSTGAFYISSLLEKMTSSDKDFSPKSLGGSRVLDPLPWLQILAAITDWISGDRTQDLALPRFMATSDLMSELQKDSIQLDEDSERKVVRTLLRLLEDRSGEVQNLAVKCLGPLVGKVKEYQVENIVDTLCANMRSDKEQLRDIAGIGLKTVLSELPPAATGSGLAISVCRKITGQLTSAIAQQEDVAVQLEALDILSDMLSRLGAPLGTFHASLLHCLLPQLSSPRLAVRKRTVVALGHLAAACSTDLFVELADHLVDRLPGPRAPASPAAIRTLIQCLGSVGRQAGHRLGAHLDRLMPLVEEFCNLDDDELRESCLQAFEAFLRKCPKEMDPHVPNVTSLCLQYMKHDPNYNHDSDEEEQMETEDSEFSEQESEDEYSDDDDMSWKVRRAAAKCMAALISSRPDLLPDFHCTLAPALIRCFKEREENVKADIFGAYIMLLRHTRPPKGWLEAVEEPTQTGRNLNMLRAQVPLVMKALQRQLKDRNVRTRQGCFNLFTELAGVLPGCLAEHMTVLVSGIVFSLADYSSSSTIRMDALAFLQGLLGTEPAEAFHPHLPTLLPPVMACVADPFYKVAAEALLVLQELVRTLWPLDRPRLLDPEPYVGEMSTATLARLRATDLDQEVKERAISCVGHLVGHLGDRLGDDLEPTLLLLLDRLRNEITRLPAVKALTLVAVSPLRLDLQPILAEALPILASFLRKNQRALRLATLAALDALAQSQGLGLPPPAVRSVLAELPALVSENDMHVAQLAVDFLTTVTQTQPASLVEVSGPVLEELLQLLHSPLLPAGVLAATEGFLQALVGTRPPCVEYSELISLLTAPVYNQVGDGGPGLHKQVFHSLARCVAALSAACPQEAAGTASRLVCDARSPHSSTGVKVLAFLSLAEVGQVAGPGPQRELKTVLLEALGSPSEDVRAAAAYALGRVGAGNLPDFLPFLLAQIEAQPRRQYLLLHALREALGAAQPDNLKPYVEDVWALLFQRCESPEEGTRCVVAECIGKLVFVNPPFLLPRFRKQLAAGQPYTRSTVITAVKFLISDQPHSIDPLLKSFIAEFMESLQDPDLNVRRATLTFFNSAVHNKPSLVRDLLDDILPLLYQETKIRRDLIREVEMGPFKHTVDDGLDVRKAAFECMYSLLESCLGQLDICEFLNHVEDGLKDHYDIRMLTFIMLARLAALCPAPVLQRVDRLIEPLRATCTAKVKAGSVKQELEKQDELKRSAMRAVAALMTNPEVRKSPSVADFSTQIRSNPELATLFESIQKDTASGPSMDSMELS
Protein: Antitoxin HigA (Antidote protein) (Host inhibition of growth protein A) (Q7A224)
Organism: Proteus vulgaris
Function: Antitoxin component of a type II toxin-antitoxin (TA) system that counteracts the effect of the HigB toxin. Binds to its own promoter and regulates transcription of the higB/higA operon.
Interaction partners:
Sequence:
MRQFKVSHPGEMIARDLEDMGVSGRRFAHNIGVTPATVSRLLAGKTALTPSLSIRIAAALGSTPEFWLRLQSNYDLRQLENQIDTSGIVLYGESNEQQQNAQEH
Protein: Septin (F8W5J3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}.
Interaction partners:
Sequence:
MVVGESGLGKSTLINSLFLTDLYSGEYPGPSNRIKKTVQVEQSKVLMKEGGVQLLLSIVDTPGFGDAVDNSNCWQPVIDHIDSKFEDYLNAESRVNRRQMPDSRVHCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMREILEHKIKIYEFPETDDEEENKIVKTIKDRLPLAVVGSNTIIEANGKKVRGRQYPWGVAEVENGDHCDFTLLRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTCNGIDNNKAKGQLTKSPLAQMEEERREHVTKMKKMEMEMEQVFEMKVKEKVQKLKDSEGELQRRHEQMKKNLEAQHKELEERRRQFEEERSTWETQQRILEQQKMTLEKNKKKGKIF
Protein: Zinc finger protein 8 (Zinc finger protein 128) (Q8BGV5)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. May modulate BMP and TGF-beta signal transduction, through its interaction with SMAD proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:12370310}.
Interaction partners:
- Zinc finger protein 189
Sequence:
MDHQDKAATVAMASRPQATQLQEPVTFRDVAVDFTQEEWGQLDPTQRTLYRDVMLETFGHLLSVGPDLPKPAVISQLEQGAELWVADRGGTGACHPGWILEPEDHTLLKDQGLPKMEPSPITEKDGFAKAVPCRSMIGIDQESDGQRQALKKDQSNLNDPKEIPLQSQSHKSLGLVEACVLGLNTYLLPDISGREYGCTYDSQVKNSEHNPSLVRQRTDSPATQSFDDNGSQKAFDQIMPITELTKSQVQDKPYKCTDCGKSFNHNAHLTVHKRIHTGERPYMCKECGKAFSQNSSLVQHERIHTGDKPYKCDECGKSFCHSTHLTVHRRIHTGEKPYECQDCGRAFNQNSSLGRHKRTHTGEKPYTCSVCGKSFSRTTCLFLHLRTHTEERPYECNHCGKGFRHSSSLAQHQRKHAGEKPYECRQRLIFEQAPALIKYEWTEPLGCDSPLSQGERTQRSDRPFKCNQCGKCFTQSSHLIRHQLTHSREEEPLRGRSRRQEQPCRRGSRLIQNTNSNSRELPVAQPKAGQASRTLALFDLREIMQEQNPVHVIGVEEPSVGNSMLFDTRESR
Protein: polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Q8IH29)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FTRKSLKLLNYRLKCLSLFCPGGRRGIQSSSNGEAPSVEVNFSNGRNMTFSSGRIPMNFMRRELGPSEKEILSARLIDRSLRPLFHKDYRTETQLVCNMLAMDAVHSPDVLAINAASMALSLSDIPWNGPIGAVRVGLCDGEVLINPTRRELQTSQLDLVVSATKQNLVVMLEGKGNVVLQQDLLKAIKQGTREAQFIIHEIERLQKAYGRQKREVEVAAEVDPELGKAVRSMCEMRLREIFQDSTHDKMSRDNAVNEVRSNVIDKVWSSFPDTEPSLITEQFNQTSRTIFRELIFERGLRCDGRDYDQLRNISCQVDMYKPLHGSALFQRGQTQVFCTVSLDSQESAMKLDSLAALDSGGLKAKNFMLHYEFPPYATGEVGRIGPVGRREMGHGALAERSLLPTLPNDYPFTVRLTSEVLESNGSSSMASVCGGSLALMDAGVPVSAPAAGVAIGLVTKFENDDTKHLQDYRILTDILGIEDYMGDMDMKVAGTRKGFTAIQADLKIPGIPLKVVMESLQKATDAKSKILDIMSEAIREPRKYPKESWPVSETLTVEPQQRAQLIGPSGLHMKRIYLETGTSLTAVDETHFNVFAPSQAAMDEAKELIEGYMVKERVPDLEFGGIYTAKITELRDTGVMVILYPSMPPALLHNSQLDQRKIAHPSALNLEVGQEIQVKYFGRDPVSGFMRLSRKVLQGPALGIPRSLNKSAGESGT
Protein: Protein LZIC (Leucine zipper and CTNNBIP1 domain-containing protein) (Leucine zipper and ICAT homologous domain-containing protein) (Q5PQN7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- dCTP pyrophosphatase 1
Sequence:
MASRGKTETSKLKQNLEEQLDRLMQQLQDLEECREELDGDEYEETKKETLEQLSEFNDSLKKIMSGNMTLVDELSGMQLAIQAAISQAFKTPEVIRLFAKKQPGQLRTRLAEMDRDLMVGKLERDLHTQQKVEILTALRKLGEKLTDDDEAFLSANAGAVLSQFEKVSTELGSGDKVLALAGFEVEKAKK
Protein: COP9 signalosome subunit 7B (A0A087X1P5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGEQKPSSNLLEQFILLAKGTSGSALTALISQVLEAPGVYVFGELLELANVQECIPYSVLLKDLEMRNLRELEDLIIEAVYTDIIQGKLDQRNQLLEVDFCIGRDIRKKDINNIVKTLHEWCDGCEAVLLGIEQQVLRANQYKENHNRTQQQVEAEVTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH
Protein: Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (PKU-alpha) (Tousled-like kinase 2) (O55047)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (By similarity). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (By similarity). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10455159}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q86UE8}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2. {ECO:0000269|PubMed:10455159}.
Interaction partners:
- Serine/threonine-protein kinase tousled-like 1
- Histone chaperone ASF1A
- Histone chaperone ASF1B
- Cullin-3
- E3 ubiquitin-protein ligase ARIH1
- Transmembrane protein 183
Sequence:
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPRGHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN