wanglab/gogpt-training-data huggingface dataset:
Protein: Small conductance calcium-activated potassium channel protein 1 (SK1) (SKCa 1) (SKCa1) (hSK1) (KCa2.1) (Q92952)
Organism: Homo sapiens (Human)
Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization (By similarity). Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9EQR3}.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Potassium channel subfamily U member 1
- Calcium-activated potassium channel subunit beta-1
- Intermediate conductance calcium-activated potassium channel protein 4
- Calcium-activated potassium channel subunit beta-3
- Calcium-activated potassium channel subunit beta-4
- Calcium-activated potassium channel subunit beta-2
- Small conductance calcium-activated potassium channel protein 2
- Protein kinase C gamma type
- Protein kinase C beta type
Sequence:
MNSHSYNGSVGRPLGSGPGALGRDPPDPEAGHPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRASGKPSNVGHRLGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSWGVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVDNGADDWRIAMTCERVFLISLELAVCAIHPVPGHYRFTWTARLAFTYAPSVAEADVDVLLSIPMFLRLYLLGRVMLLHSKIFTDASSRSIGALNKITFNTRFVMKTLMTICPGTVLLVFSISSWIIAAWTVRVCERYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAIRPPPPPLPPRPGPGPQDQAARSSPCRWTPVAPSDCG
Protein: Prefoldin subunit 3 (von Hippel-Lindau-binding protein 1) (VBP-1) (VHL-binding protein 1) (Q2TBX2)
Organism: Bos taurus (Bovine)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In complex with VHL can translocate to the nucleus. {ECO:0000250}.
Interaction partners:
- Prefoldin subunit 1
- Prefoldin subunit 2
- Prefoldin subunit 6
- Prefoldin subunit 5
- Prefoldin subunit 4
- Prefoldin subunit 4
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit beta
- Protein MIX23
- T-complex protein 1 subunit delta
Sequence:
MAASKDGCGVGEVAAGNGRRLHLGIPEAVFVEDVDSFMKQPGNETADIVLKKLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYKQKKKESTSSLETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDEAQALLEKNLLTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNWDVKRRNKDDSTKNKA
Protein: Probable 23S rRNA methyltransferase Erm(37) (Q10838)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS12
Sequence:
MSALGRSRRAWGWHRLHDEWAARVVSAAAVRPGELVFDIGAGEGALTAHLVRAGARVVAVELHPRRVGVLRERFPGITVVHADAASIRLPGRPFRVVANPPYGISSRLLRTLLAPNSGLVAADLVLQRALVCKFASRNARRFTLTVGLMLPRRAFLPPPHVDSAVLVVRRRKCGDWQGR
Protein: Aprataxin (EC 3.6.1.71) (EC 3.6.1.72) (Forkhead-associated domain histidine triad-like protein) (FHA-HIT) (P61798)
Organism: Gallus gallus (Chicken)
Function: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity (By similarity). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q7Z2E3}.
Interaction partners:
- Tyrosyl-DNA phosphodiesterase 1.
- Aprataxin and PNK-like factor
- Uncharacterized protein.
- DNA ligase.
- X-ray repair cross-complementing protein 5
- DNA ligase 4
- XRCC1_N domain-containing protein.
- DNA-dependent protein kinase catalytic subunit
- Ubiquinone biosynthesis protein COQ4 homolog
- Uncharacterized protein.
Sequence:
HASARGEGFLLLKADCNKGYVTVKQIGVNPTSVDLVDVGKDEEVKMRPGQVLHIVNKLYPFVVQFGEESEESVMEAEEKIQTEKRPCEDSCENDDIENVPKKAKKMEVVDTQSSSADLRPSKSSVSPHEGTTSRKEHLGHWSQGLKSSMQDPKVQVYKDEKTVVIKDKYPKARYHWLVLPWDSISSLKSVTREHLGLLEHMHAVGQKMIQQCPAKESLEFRLGYHAIPSMSQLHLHVISQDFDSPALKTKKHWNSFTTEYFLNSEEVIEMVRSKGKVTVNDQASELLKLPLRCHLCKQQLSTIPQLKEHLKKHWTK
Protein: ZO-2 associated speckle protein (E3Q1N2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPASHAPGASANPPCHLPSVIADSFLASHLSPSPERTVMLGSAPDPLPQAGSRRGHRGEANPAPSPRSHCASPTTSWKRRGPREGASPTSLLSSTPCWTGLRGEGGGTGPTPPGTPGAEDAPGLRALREARGEGGLGLGTLGLPAWLPLGSRVWVEGPRVSQVSCQPQ
Protein: GrpE protein homolog 2, mitochondrial (Mt-GrpE#2) (O88396)
Organism: Mus musculus (Mouse)
Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Stress-70 protein, mitochondrial
- Mitochondrial disaggregase
- 10 kDa heat shock protein, mitochondrial
- DnaJ homolog subfamily A member 3, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM44
- 10 kDa heat shock protein, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM50
- Lon protease homolog, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim23
- Heat shock 70 kDa protein 4L
Sequence:
MAARSLWAVQRLQRLLASGAMSESRGWLHPFSTATQRTAGEDCSSEDPPDGLGPSLAEQALRLKAVKLEKEVQDLTLRYQRAVADCENIRRRTQRCVEDAKIFGIQSFCKDLVEVADILEKTAKCCSEGAEPEDHRRTLEKVFQGLSLLEARLKSVFTKHGLEKMTPIGDKYDPHEHELICHMPAGVGVQPGTVALVRQDGYKLHGRTIRLAQVEVAVESQRRL
Protein: Ubiquitin carboxyl-terminal hydrolase 26 (EC 3.4.19.12) (Deubiquitinating enzyme 26) (AtUBP26) (Ubiquitin thioesterase 26) (Ubiquitin-specific-processing protease 26) (Q9SCJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Deubiquitinates H2BK143ub1 of histone H2B.
Subcellular location: Nucleus {ECO:0000269|PubMed:17554311}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin-ribosomal protein eL40z fusion protein
- E3 ubiquitin-protein ligase UPL3
- E3 ubiquitin-protein ligase UPL4
- Ubiquitin-ribosomal protein eS31x fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 6
- Ubiquitin carboxyl-terminal hydrolase 27
Sequence:
MSRPNTRNKNKRQRPDAVDSSSQILRKIHEANDVTDDDINQLFMIWKPVCQGCRVNTRDNPNCFCGLVPPLNGSRKSGLWQKTSEIIQSLGPDPTLDRRDSESTPAGLTNLGATCYANSILQCLYMNTAFREGVFSVEVHVLKQNPVLDQIARLFAQLHASQKSFVDSDAFVKTLELDNGVQQDTHEFLTLLLSLLERCLLHSGVKAKTIVQDLFSGSVSHVTTCSKCGRDSEASSKMEDFYALELNVKGLKSLDASLNDYLSLEQLNGDNQYFCGSCNARVDATRCIKLRTLPPVITFQLKRCIFLPKTTAKKKITSSFSFPQVLDMGSRLAESSQNKLTYDLSAVLIHKGSAVNSGHYVAHIKDEKTGLWWEFDDEHVSELGKRPCNEASSSTPQSESNGTASSGNITDGIQSGSSDCRSAIKSEVFSSSDAYMLMYSLRCDKQENQEGQKENPIDITKGEVKQLKGGYLPKHLSEWINNMNAVFLESCKQYNLRKEKELNALTERRQEVRTILSEAAVQSLEEQYFWISTDWLRLWADTTLPPALDNTPLLCSHGKVHASKVNCMKRISELAWIKLESKFNGGPKLGKGDYCRDCLMDGARMVVSSDSYRDRRTFMKSIANDVLSGKCEDGMYYISRAWLQQWIKRKNLDAPTEADAGPTNAITCNHGELMPEQAPGAKRVVVPENFWSFLFEDALKVMSEDTLDCTCFPVDSSQCCHCTEVLSEVACFEDSLRTLKVKQRQNHEKLATGKGIPLTPQSRYFLLPSPWLVQWRIYINMTGKNSSSAPEPERLDGVINTLKCKKHTRLLERLPELVCRRGSYFQKNPSTDKLTIIPELDWKYFCDEWGGLMENGISAFIEVGNTDQSSSPDVIDLEKDSSPDDNMDVDAQQLILRASPEICEECIGERESCELMQKLSYSEGDVFVCFVRGKEAPKAMLEASDSSFEVDRRTSKRSRRTNYGNLTSLKVSATTTVYQLKMMIWELLGVMKENQELHKGSKVIDQESATLADMNIFPGDRLWVRDTEMHEHRDIADELCEKKPGAQDIEEGFRGTLLTGNISSEAC
Protein: Heterogeneous nuclear ribonucleoprotein 1 (hnRNP1) (Q8W034)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14756317}. Cytoplasm {ECO:0000269|PubMed:14756317}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. Relocalization from the cytoplasm into the nucleus is mediated by TRN1 (By similarity). {ECO:0000250}.
Interaction partners:
- RNA binding
- Cold shock domain-containing protein 3
- Cold shock protein 2
- Uncharacterized protein
- Enolase
- Serine/arginine-rich splicing factor RS31
- Serine/arginine-rich splicing factor SC35
- Transportin-1
- Cleavage stimulating factor 64
Sequence:
MDSDQGKLFVGGISWETDEDKLREHFTNYGEVSQAIVMRDKLTGRPRGFGFVIFSDPSVLDRVLQEKHSIDTREVDVKRAMSREEQQVSGRTGNLNTSRSSGGDAYNKTKKIFVGGLPPTLTDEEFRQYFEVYGPVTDVAIMYDQATNRPRGFGFVSFDSEDAVDSVLHKTFHDLSGKQVEVKRALPKDANPGGGGRSMGGGGSGGYQGYGGNESSYDGRMDSNRFLQHQSVGNGLPSYGSSGYGAGYGNGSNGAGYGAYGGYTGSAGGYGAGATAGYGATNIPGAGYGSSTGVAPRNSWDTPASSGYGNPGYGSGAAHSGYGVPGAAPPTQSPSGYSNQGYGYGGYSGSDSGYGNQAAYGVVGGRPSGGGSNNPGSGGYMGGGYGDGSWRSDPSQGYGGGYNDGQGRQGQ
Protein: Lactase/phlorizin hydrolase (Lactase/glycosylceramidase) [Includes: Lactase (EC 3.2.1.108); Glycosylceramidase (EC 3.2.1.62) (Phlorizin hydrolase)] (P09849)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:1388157}; Single-pass type I membrane protein {ECO:0000269|PubMed:1388157}. Note=Brush border. {ECO:0000269|PubMed:1388157}.
Interaction partners:
- Beta-galactosidase
- Alpha-galactosidase
- Aldose 1-epimerase
- Glucose-6-phosphatase catalytic subunit 1
- hexokinase
- Hexokinase-3
- Alpha-lactalbumin
- hexokinase
- aldose reductase
- Aldo-keto reductase family 1 member B1
Sequence:
MELFWSIVFTVLLSFSCRGSDWESDSNFISAAGPLTTDLLLSLQYPQGNQTSDFAAGGKDLYVCSQPLPAFLPEYFSSLRASEITHYKVFLSWAQLLPAGHSGDPDGNAVRCYRQLLEALRAAQLQPMVVLHHQHLPASSALRSAVFADLFAEYATFAFHAFGDLVGVWLTFSDLEAAIRELPQPESRASRLQLLTEAHRKAYEIYHQKYAAQGGKVSVVLQAEEISELLLESSTSALAKDSIDFLSLDLSYECQSEMSLPEKLSKLQTIEPKVKVFIFTLRLQDCPSSRKSPASLLFSFIEAINKDQVLTLGFDVNAFLNCSSTSKKSISCFLTDSLALQTDHERAARNSAPVSTYQRVWEMFAHQPRAERDAFLQDTFPQGFLWGVSTGAFNVEGGWAEGGRGPSVWDQFGHLKAAQGQATPEVASDSYYKWASDVALLRGLRAQVYKFSISWSRIFPMGRGSSPSPQGVAYYNKLIDSLLDSHIEPMATLFHWDLPQALQDEGGWQNESVVDAFVDYAAFCFSAFGNRVKLWVTFHEPWVMSYAGYGTGQHAPGISDPGIASFQVAHLVLKAHARTWHHYNSHHRPQQQGRVGIVLNSDWAEPLSPERPEDLAASERFLHFMLGWFAHPIFVDGDYPATMKAQIQQRNEQCPSPVAQLPEFTDTEKQLLKGSADFLGLSHYTSRLISKAPEDSCIPSYDTIGGFSQHTDPAWPQTSSPWIRVVPWGIRRLLQFVSLEYTKGKVPIYLAGNGMPIGESENLLSDSLRVDYFNQYINEVLKAIKEDSVDVRSYIARSLMDGFEGPAGYSQRFGLYHVNFNESSKPRTPRKSAFLLTSIIEKNGFLTKAVKQPLPPNSAHLPSKTRASALPSEVPSKAKVVWEKFSNQTKFERDLFYHGTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGNGVTDNSTGDIACDSYNQLDADLNVLRALKVKAYRFSLSWSRIFPTGTNSSINSHGVDYYNRLIDGLLASDIFPMVTLFHWDLPQALQDIGGWENPSLIDLFDSYADYCFQTFGDRVKFWITFNEPTYYSWWSYGSGTFPPNVNDPGWAPYRISHALIKAHARVYHTYDEKYRQSQNGVISLSLVAQWAEPKSPDVLRDVEAADRKMQFTLGWYAHPIFKTGDYPDAMKWKVGNRSELQHLATSRLPSFTEEEKSYIRGTADVFCLNTYSSKIVQHKTPALNPPSYEDDQELAEEEDTSWPTTAMNRAASFGMRRLLNWIKEEYGDIPIYITENGVGLTNPRLEDIDRIFYYKTYINEALKAYRLDGVNLRGYFAWSLMDNFEWLQGYTIKFGLYHVDFENVNRPRTARISASYYTELITNNGMPLPSEDEFVYGQFPEGFVWSTSTAAFQIEGAWRADGKGLGIWDTFTHTRLKIENDDIADVACDSYHKISEDVVALQNLAVTHYRFSISWSRILPDGTTNYINEAGLNYYVRLIDALLAANIKPQVTMYHFDLPQALQDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVVAYHGYGTGLYAPGIYFRPGTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAAKRYVQFMGGWFAHPIFKNGDYNEVMKTQIRERSLAAGLNESRLPEFTESEKRRINGTYDFFGFNHYTTVLAYNFNYPSIMSTVDADRGVASIVDRSWPGSGSYWLKMTPFGFRRILNWIKEEYNNPPIYVTENGVSHRGDSYLNDTTRIYYLRSYINEALKAVQQDKVDLRGYTVWTLMDNFEWYTGFSDKFGLHFVNYSDPSLPRIPRESAKFYASIVRCNGFPDPAEGPHPCLLQPEDTDPTMSPVSQEEVQFLGLSLGSTEAETALYVLFSLMLLGVCGLAFLSYALCKSSKQRKKLSQQELSPVSSF
Protein: IMPACT family member C14C8.09c (O60090)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MNKRQSQLKFGNEGISLAVPKQSLQECSYMSNLITDRESTFLSYFVPSKDPKMLPVYRFMFQESADLKHCNHKMQAWRFPNEIEAFNDDGEEYSGQKLLNVLRKEDVYGMVVCVRWYGGQLLGPVRFQHITNTAKQSIDKYKSVLEEERKKQLLRTETGLLRQSSSRSSSLLDQRIRQITAKDKTVNLLRKTLNRPLLHEVDYHGKSLEILDMLLQSRNSMISSLRSELQEKNQKDKKKEVNKLEEKMTNAKEPNVNVPSMKASSAISVETPETIESEASVDHKEASKIIKDVEKEE
Protein: Transcription factor RBF1 (RPG-box-binding factor 1) (Q5ABZ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcriptional activator that binds to the RPG box and to telomeres. Involved in the regulation of the transition between yeast and filamentous forms and plays a role in virulence. Induces expression of HWP1, a major hyphal cell protein and virulence factor.
Subcellular location: Nucleus {ECO:0000269|PubMed:9043119}. Chromosome, telomere {ECO:0000269|PubMed:9043119}.
Interaction partners:
- Ash2p
- Histone H4
- COMPASS subunit protein
Sequence:
MSSNKNQSDLNIPTNSASLKQKQRQQLGIKSEIGASTSDVYDPQVASYLSAGDSPSQFANTALHHSNSVSYSASAAAAAAELQHRAELQRRQQQLQQQELQHQQEQLQQYRQAQAQAQAQAQAQAQAQREHQQLQHAYQQQQQLHQLGQLSQQLAQPHLSQHEHVRDALTTDEFDTNEDLRSRYIENEIVKTFNSKAELVHFVKNELGPEERCKIVINSSKPKAVYFQCERSGSFRTTVKDATKRQRIAYTKRNKCAYRLVANLYPNEKDQKRKNKPDEPGHNEENSRISEMWVLRMINPQHNHAPDPINKKKRQKTSRTLVEKPINKPHHHHLLQQEQQQQQQQQQQQQQQQQQQQQQQHNANSQAQQQAAQLQQQMQQQLQASGLPTTPNYSELLGQLGQLSQQQSQQQQLHHIPQQRQRTQSQQSQQQPQQTPHGLDQPDAAVIAAIEASAAAAVASQGSPNVTAAAVAALQHTQGNEHDAQQQQDRGGNNGGAIDSNVDPSLDPNVDPNVQAHDHSHGLRNSYGKRSGFL
Protein: Spindlin family member 2B (Spindlin-like protein 2, isoform CRA_b) (Q5JZB7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTPNAQEAEGQQTRAAAGRATGSANMTKKKVSQKKQRGRPSSQPRRNIVGCRISHGWKEGDEPITQWKGTVLDQLLDDYKEGDLRIMPESSESPPTEREPGGVVDGLIGKHVEYTKEDGSKRIGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKKS
Protein: Coilin (Atcoilin) (Q8RWK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs (Probable). Required for CBs formation. Binds snRNAs and non-specific artificial RNA via the N-terminal part of the NOD domain and via the NLS2 region (212-282) of the IDD domain. The two sites are able to function independently and provide effective RNA-binding in a non-cooperative manner.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, Cajal body {ECO:0000305|PubMed:16624863}.
Interaction partners:
- U2 small nuclear ribonucleoprotein B''
- At5g58020
- Small nuclear ribonucleoprotein SmD3a
- Suppressor of mec-8 and unc-52 protein homolog 1
- Probable small nuclear ribonucleoprotein F
- F3F19.7
- At1g25682
- Pentatricopeptide repeat-containing protein At1g13040
- Pentatricopeptide repeat-containing protein At1g12300
- DDB1- and CUL4-associated factor 13
Sequence:
MEEEKVRVRLVFEDRRILSKYQKKQGLTRSWVVLNRKCHRTISEFSDHIFHTFSLCEACPHGLSLSMEGFVLPPFESSCVLKDKDIVCVKKKKESLLEIVGEDSDENVYNAIEVEERPQIRPGEMLLANEEFQKETGGYESESEEDELEEEAEEFVPEKKASKKRKTSSKNQSTKRKKCKLDTTEESPDERENTAVVSNVVKKKKKKKSLDVQSANNDEQNNDSTKPMTKSKRSSQQEESKEHNDLCQLSAETKKTPSRSARRKKAKRQWLREKTKLEKEELLQTQLVVAPSQKPVITIDHQATKEKHCETLENQQAEEVSDGFGDEVVPVEVRPGHIRFKPLAGTDEASLDSEPLVENVLWNGNMTKKKGQKWGTEKSGFSKRYAQDFNEDATTQPAEAETLANCPIDYEQLVAYTGSVKKGDVIAYRLIELTSSWTPEVSSFRVGKISYYDPDSKMVTLMPVQEFPIEKKTEEDDDFCMQPDTSLYKEDGSLEIEFSALLDVRSVKTSSSDSAEVAKSALPEPDQSAKKPKLSANKELQTPAKENGEVSPWEELSEALSAKKAALSQANNGWNKKGSSSGGSWSYKALRGSAMGPVMNYLRSQKEI
Protein: Evasin P1166 (A0A0K8RE99)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVKIFTLLQIALFIALGIHLVVAGPETKEDKKSDVYELFTVEYCGTNCTLLTNGRWTACTGKKGTCRCYHESGEKVGLCLSTEYTDFSEYPNPKSSEIDAAAPLPRETH
Protein: Presequence translocated-associated motor subunit PAM17, mitochondrial (Q5AEM8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 5-phosphatase
- Vacuolar protein 14 C-terminal Fig4-binding domain-containing protein
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM50
- GrpE protein homolog
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM21
Sequence:
MFSLGVQSRLFTRRALFSGFRFNSTTTTTTTASQPRLTWVDYFQLKKQNNRINTIAGVFTGLGGAFITLSYLGNIEIDVEKPIMGFDPLMVMGGAVILGGLVGFLVGPFIGSSIFRLTNRAQLKQFELKNTEFLSRLRIKRPDPSSQSFSNPIPDYYGEKIYSLKDYKQWLRDCNAFRRKSKEFL
Protein: cGMP-dependent protein kinase 2 (cGK 2) (cGK2) (EC 2.7.11.12) (cGMP-dependent protein kinase II) (cGKII) (Q64595)
Organism: Rattus norvegicus (Rat)
Function: Crucial regulator of intestinal secretion and bone growth (By similarity). Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (Probable). Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863. Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q13237}; Lipid-anchor {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:9465038}; Lipid-anchor {ECO:0000305|PubMed:9465038}. Note=Plasma membrane localization is required for its function in the activation of CFTR. {ECO:0000269|PubMed:9465038}.
Interaction partners:
- Guanylate cyclase soluble subunit alpha-1
- Guanylate cyclase soluble subunit alpha-2
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit beta-2
- Vasodilator-stimulated phosphoprotein
- Inositol 1,4,5-triphosphate receptor associated 1
- Calcium-activated potassium channel subunit alpha-1
- Cyclic AMP-responsive element-binding protein 1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Protein phosphatase 1, regulatory subunit 17.
Sequence:
MGNGSVKPKHSKHPDGQSGNLSNEALRSKVAELEREVKRKDAELQEREYHLKELREQLAKQTVAIAELTEELQSKCIQLNKLQDVIHVQGGSPLQASPDKVPLDVHRKTSGLVSLHSRRGAKAGVSAEPTSRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGRNYQQGSYIVKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEEYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFDELQKYLEGYVATLNRDDEKRHAKRSMSSWKLSKALSLEMIQLKEKVARFSSTSPFQNLEIIATLGVGGFGRVELVKVKNENIAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDADGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGIDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLRRELSGPIDHSYFDKYPPEKGVPPDEMSGWDKDF
Protein: Bromodomain-containing protein 7 (75 kDa bromodomain protein) (O88665)
Organism: Mus musculus (Mouse)
Function: Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase (By similarity). Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR.
Subcellular location: Nucleus {ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:19909775}. Chromosome {ECO:0000250|UniProtKB:Q9NPI1}.
Interaction partners:
- AT-rich interactive domain-containing protein 2
- PHD finger protein 10
- Protein polybromo-1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF complex subunit SMARCC2
- Actin-like protein 6A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF complex subunit SMARCC1
Sequence:
MGKKHKKHKSDRHFYEEYVEKPLKLVLKVGGSEVTELSTGSSGHDSSLFEDRSDHDKHKDRKRKKRKKGEKQAPGEEKGRKRRRVKEDKKKRDRDRAENEVDRDLQCHVPIRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMSDLQKTRKQKERTDACQSGEDSGCWQREREDSGDAETQAFRSPAKDNKRKDKDVLEDKWRSSNSEREHEQIERVVQESGGKLTRRLANSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNRVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPNNFSISEFLATCQDYPYVMADSLLDVLTKGGHSRSLQDLDMSSPEDEGQTRALDTAKEAEITQIEPTGRLESSSQDRLTALQAVTTFGAPAEVFDSEEAEVFQRKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMYLAEQVTNNLKELTQQVTPGDVVSIHGVRKAMGISVPSPIVGNSFVDLTGECEEPKETSTAECGPDAS
Protein: Insulin-like growth factor-binding protein 4 (IBP-4) (IGF-binding protein 4) (IGFBP-4) (P21744)
Organism: Rattus norvegicus (Rat)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Pappalysin-1
- Insulin-like growth factor-binding protein 1
- Pappalysin 2.
- Insulin-like growth factor-binding protein 2
Sequence:
MLPFGLVAALLLAAGPRPSLGDEAIHCPPCSEEKLARCRPPVGCEELVREPGCGCCATCALGLGMPCGVYTPRCGSGMRCYPPRGVEKPLRTLMHGQGVCTELSEIEAIQESLQTSDKDESEHPNNSFNPCSAHDHRCLQKHMAKVRDRSKMKVVGTPREEPRPVPQGSCQSELHRALERLAASQSRTHEDLFIIPIPNCDRNGNFHPKQCHPALDGQRGKCWCVDRKTGVKLPGGLEPKGELDCHQLADSLQE