wanglab/gogpt-training-data huggingface dataset:
Protein: Ectonucleoside triphosphate diphosphohydrolase 3 (NTPDase 3) (EC 3.6.1.5) (Ecto-ATP diphosphohydrolase 3) (Ecto-ATPDase 3) (Ecto-ATPase 3) (Q8BFW6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates. Has a threefold preference for the hydrolysis of ATP and UTP over ADP and UDP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15130768}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleoside triphosphate diphosphohydrolase 6
- Ectonucleoside triphosphate diphosphohydrolase 5
- Uridine-cytidine kinase 2
- Adenosine kinase
- Adenylate kinase 4, mitochondrial
- Uridine-cytidine kinase 1
- Cancer-related nucleoside-triphosphatase homolog
- Uridine-cytidine kinase-like 1
Sequence:
MFTVMTRQPCEQAGFRALSRTPAIVTLVVLLVSIVVLVTLTLIQIRHPQVLPPGLKYGVVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFRCSVKGSGISSYENNPQDAPKAFEDCILKVKEQVPEHLHGSTRIYLGATAGMRLLRLQNETAAREVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYIMGNFLEKNLWHMWVHPHGVDTTGALDLGGASTQISFVAGEKMEPNASDTVQVSLYGYTYTLYTHSFQCYGQNEAEKKFLAMLLQSPSTEANISNPCYPQGYSTAFTLGHVFGSLCTEKQRPESYNSSKSVTFMGTGDPRLCREKVASVFDFNACQEQDACSFDGIYQPKVQGPFVAFAGFYYTASALNLSGSFSLTSFNDSSWDFCRHTWSELPALLSRFDETYARSYCFSAHYIYHLLVNGYKFTEETWPQIRFEKEVGNSSIAWSLGYMLSLTNQIPAGSPLIHLPIQPPVFMGVLAFFTAIALLCLAFLLYLCSSFRTKERSENAFDQAVDSD
Protein: Transcription factor GATA-4 (GATA-binding factor 4) (P43694)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development and function. In cooperation with TBX5, it binds to cardiac super-enhancers and promotes cardiomyocyte gene expression, while it down-regulates endocardial and endothelial gene expression. Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). Acts as a transcriptional activator of ANF in cooperation with NKX2-5 (By similarity). Promotes cardiac myocyte enlargement. Required during testicular development. May play a role in sphingolipid signaling by regulating the expression of sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate lyase.
Subcellular location: Nucleus {ECO:0000269|PubMed:21220346, ECO:0000269|PubMed:24000169}.
Interaction partners:
- Homeobox protein Nkx-2.5
- Zinc finger protein ZFPM2
- T-box transcription factor TBX5
- T-box transcription factor TBX20
- Serum response factor
- Heart- and neural crest derivatives-expressed protein 2
- Nuclear factor of activated T-cells, cytoplasmic 4
- Transcription factor SOX-9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- Histone acetyltransferase p300
Sequence:
MYQSLAMAANHGPPPGAYEAGGPGAFMHGAGAASSPVYVPTPRVPSSVLGLSYLQGGGAGSASGGASGGSSGGAASGAGPGTQQGSPGWSQAGADGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYSSGGGAAGAGLAGREQYGRAGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPAARHPNLDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTPAAPSGSESLPPASGASSNSSNATTSSSEEMRPIKTEPGLSSHYGHSSSVSQTFSVSAMSGHGPSIHPVLSALKLSPQGYASPVSQSPQTSSKQDSWNSLVLADSHGDIITA
Protein: AT16994p (Pou domain motif 3, isoform A) (Q7JUR9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEITDGHALLSPPPPSHSHSHSPFDSKDHVKELEFYKNLAAKAASLANQHSPPPMPLPLPLPMQIDGEEDENEGEGEGEGEAEEQSAEVMRLRREEQAQAKAFAAHLNGTMQDMINLQKLQNLATLQQQQQQQQQHPHPHHGHQHHHHHPATAAALASLQGLAASVFNSPLNLSVGGEPVATTGPSVAPTSPTHNGGKSKTAKGGSSGNGSGGSSANSGTSSAQQQQQPDNPSSSSSPHHPLSASSLANVLAAATASPPPSLQAPPASAQMPQLILASGQLVQGVQGAQLLIPTAQGIAVQTILTIPVSPQIPTTEQFLPNAFGAFASYQQQQQQQQQQRDLLPPSLAALQHATALPQLAQTPTNLLKPNLFSTGVQQLLTALHPELFAAAAATHQQQQQQQQQQVQQQREREREREREREREREREREQHLGIGHLPHSHLAADLRRSAERSPTAGSPTGGSPGLAAKGPQPPPPGAAFLLQQQLHIKPETQTHLHHHLQTQSTSAVSSTLPQISLRHPDELTAPQMDLKPLELSASTSPPAPPPRHHFGHSLRGSSTVSPKHSPQGRMGGSGGSTTTGMNLSQHHERHDRLERLERQERHERRSHTPTATATRASVSSSSSAGHHGGSLPSGRLSPPSSAPSNSAANSISDRGYTSPLFRTHSPQGHALSLGGSPRLERDYLGNGPSSGTATSTSSCGAPTAAGSSATANVLSSINRLNASNGELTITKSLGAPTATATRASSASPRDDSPGPGPSTSSVSHMQPLKLSPSSRSEPPHLSPNGNDNDNDLLMDSPNEPTINQATTNVVDGIDLDEIKEFAKAFKLRRLSLGLTQTQVGQALSVTEGPAYSQSAICSALAAQMYAAQLSTQQQNMFEKLDITPKSAQKIKPVLERWMKEAEESHWNRYKSGQNHLTDYIGVEPSKKRKRRTSFTPQALELLNAHFERNTHPSGTEITGLAHQLGYEREVIRIWFCNKRQALKNTVRMMSKGMV
Protein: C-X-C motif chemokine 16 (Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein) (SR-PSOX) (Small-inducible cytokine B16) (Transmembrane chemokine CXCL16) (Q8BSU2)
Organism: Mus musculus (Mouse)
Function: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- C-X-C chemokine receptor type 6
- C-C chemokine receptor type 6
- C-X-C chemokine receptor type 3
- CX3C chemokine receptor 1
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 4
- C-X-C motif chemokine 5
- C-X-C motif chemokine 10
- C-X-C chemokine receptor type 1
- C-X-C chemokine receptor type 2
Sequence:
MRRGFGPLSLAFFLFLLALLTLPGDGNQGSVAGSCSCDRTISSGTQIPQGTLDHIRKYLKAFHRCPFFIRFQLQSKSVCGGSQDQWVRELVDCFERKECGTGHGKSFHHQKHLPQASTQTPEAAEGTPSDTSTPAHSQSTQHSTLPSGALSLNKEHTQPWEMTTLPSGYGLEARPEAEANEKQQDDRQQEAPGAGASTPAWVPVLSLLAIVFFLTAAMAYVLCNRRATQQNSAGLQLWYTPVEPRP
Protein: GDP-L-fucose synthase (EC 1.1.1.271) (FX protein) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (GER) (Q55C77)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Interaction partners:
- GDP-mannose 4,6 dehydratase
- Fucose-1-phosphate guanylyltransferase
- Small ribosomal subunit protein eS30
- Fucosyltransferase
- UDP-glucose 4-epimerase
Sequence:
MTETTSKRTVLVTGGSGLVGKGIEKYVKETDKSNDVWVFMRSSDCDLKSRESTRSYFEKIKPTHVIHLAARVGGLFSNMKYKVEFFRENIDINDNVLACCKEFNVVKCVSCLSTCIFPDKTTYPIDETMIHNGPPHPSNEGYAYAKRMIDVLNRAYNEEYGCKFTSVIPTNIYGPHDNYHLTDGHVIPGLIHKTYLAMKNNQDLTIMGTGKPLRQFIYSYDLAKYFVWTLNNYEEMSPLILSVGEEDEISIADVARLITEAMEFKGKLIFDTSKADGQYKKTASNLKLKSLVPDLTFTPIQQAIKESCQWFIDNYETARK
Protein: B-box type zinc finger protein ncl-1 (P34611)
Organism: Caenorhabditis elegans
Function: Translational repressor that inhibits protein synthesis. Represses the translation of mRNAs such as fib-1, probably by being recruited by RNA-binding protein nos-2 and the Pumilio proteins puf-5, puf-8 and puf-9 to the consensus core PUF binding motif in the 3'-UTR of fib-1 mRNA. Negatively regulates ribosomal RNA (rRNA) synthesis, ribosomal protein synthesis and nucleolus size. Its role in the negative regulation of nucleolus size is most likely through its negative regulation of the translation of proteins such as the rRNA 2'-O-methyltransferase fib-1, and dao-5. Might act directly as a transcription factor to inhibit RNA polymerase I (rRNA) and III (5S RNA) transcription. Plays a role in embryonic development, and in particular, is involved in regulating the localization of proteins, such as par-2, that are required for embryonic cell polarity. Plays a role in the regulation of lifespan, and the response to nutrient availability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18652816, ECO:0000269|PubMed:9508766}.
Interaction partners:
- Guanine nucleotide-binding protein-like 3 homolog
- F-box A protein
- Uncharacterized protein
Sequence:
METQLSVQLGLDSLLTDFGLESVMNKQQQLFANMGLSDIGAPTPSTAIPVPNAHLHPSMVAGSDPSNPVVGFGFGSPSSTTSSSPPLSNSPTIEQQQHAQLTAMMQGIMSNNNVAVSNGSGVQVASVPAVHCSGCKSNETATSFCQDCNANLCDNCTMAHKFMHCFADHRVVSLTTPGTGSSSSSTSSSSSASSTSSHQVPSLGGKQSPDSMMLGSGKRSVLCLQHRASELVFFCVSCNLAICRDCTVSDHPSGTHQYELIADVADKQMLKMEQLIADARSKHADMLDMFKQVDNKQQVLTASLHNAHAQLEETVSNLINVIQDQKKTLAKDIDNAFAAKQIQLTMVDKRIQSMADKLSQTIEFSRRLMSFASPAEVMVFKQLLDTRLQLFLGFNPDTSGVLMTPCEIEYLGAAGLFNNSASTVSQLLGSVHGGSPINNAPAANDFLMPQAGLAPIGRAQSRIIPIEQNQLARSPPHHIAGSLPMNAYSDSNLLRPNKDFGGSSQSLGPFNPLGASVPGAAADPFSSQYDKWSLGVEPSVGGLLEGGNVDEEKFQTLFPPSRSQIKRQKMIYHCKFGEFGVMEGQFTEPSGVAVNGQGDIVVADTNNHRIQVFDKEGRFKFQFGECGKRDGQLLYPNRVAVNRTTGDFVVTERSPTHQIQVYNQYGQFLRKFGANILQHPRGVCVDSKGRIIVVECKVMRVIIFDMFGNILQKFSCSRYLEFPNGVCTNDKNEILISDNRAHCIKVFSYEGQYLRQIGGEGVTNYPIGVGINSLGEVVVADNHNNFNLTVFSQDGTMIGALESRVKHAQCFDVALVDDGSVVLASKDYRLYLYRFLPATSGQSTSSASSQI
Protein: Ciliary-associated calcium-binding coiled-coil protein 1 (Q8CDT7)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein. May be involved in the control of sperm flagellar movement.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26990073}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26990073}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:26990073}. Note=Colocalized with pericentrin at centrosome of spermatocytes and round spermatids (PubMed:26990073). {ECO:0000269|PubMed:26990073}.
Interaction partners:
- Cilia-and flagella-associated protein 96
Sequence:
MNFSIEQYSKFMTLLDMLLHNLQTLHMSLEDSIKWLGEVMAEIGPNHSQKSEDFHVFEVKEANAIIDYLKISLFQHYRLYEFLFYSTREEIVIGTEQTIEVVKPADYPFPAPLEEGISLDTYSTFIEPLPTPDMEQKVLDQEQGTQEALLESEMREEDPLGGFTIDDVKSALERVTDEVLISMQKEISEKLQVQEEAFNARIEKLKKA
Protein: Inositol-pentakisphosphate 2-kinase (EC 2.7.1.158) (Inositol-1,3,4,5,6-pentakisphosphate 2-kinase) (Ins(1,3,4,5,6)P5 2-kinase) (InsP5 2-kinase) (Q4JL91)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis and ion channel regulation. InsP6 also acts as a key regulator of left-right asymmetry in embryo, probably by regulating asymmetric Ca(2+) during left-right specification.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Inositol-tetrakisphosphate 1-kinase
- Kinase
- Kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Kinase
- Kinase
- Kinase
- Inositol-tetrakisphosphate 1-kinase
Sequence:
MELDKMDENDWKYHGEGNKSIVVSHLRHCQVLRLLKVPSEDSAHTRQTAEQTLRHILNIMDYSKHVMKPLLGEKYVHSGEVVRLPLDFLRQMSLKVQQERPELRCDKVMDTFSGCGLCLPDLTQLPLHHLRDHRPPICVEIKPKCGFLPFSRHMTKECKWKVCRFCMHQHYKLANGKWKRLSRYCPLDLFSGSKQRMYVALKNLLEEPQNNLKIFKGGELIFSCKDDAKQQPDLNNLIQHLRPYFPHTNGLYNGHQPGKVILNEFIQVICSALLSGGDSNRSGEPRKMHLSESKPHCEASPFPRDLIRNGHHGLPKDSVLAKILQVQMLDNLDIEGIYPLYKRVEQYLEEFPKERIRLQIDGPYDESFMDTVKSCLNEDDGSVEYAIGKVHQYRVAMTAKDCSVMITFAPCEEDEEHKLNLEKPRFTYSVSILDLDTKPYEGIPHQYKLDSKIVNYYLRSTQAPPPSSLYKERQECTLLFHAV
Protein: NosA protein (C8VPR1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAAPRKKATAAAKRAAESQASSGSESTPKPEGTTKSHKRSRSGCFTCRLRRKKCDEKHPSCGACNNLCVKCEYKRPVWWGNAEQRKMHKERIKNKIKQTKMNERNGSLAIDPASRVRSMAANSPTSPEFEYGRPFPEPSYDIFASQFPTPAMAQTIYAPQYPYEVDVKTEHQTFVNDVQLRHDSVSSTFSTFAPPQLNAPLPTFPGDEWFHDEYFRAPVLPGIDPALCEQPFPETYDMLQNIPVSDHDRPLLEHFIHNVLRVSFPVLEAHQRGHMRAQAVLQTLETNKCYLHCCLSVAAIHLKTTEGITGEQIDHDIMRNRFEAISQLCQALGDDTEHQEILDATLAMIFFHSSVGPADDYLPDIPWLDHFQAAANLVQRLGLTADAPNPYVLPPFSMTLTAWIDILGSTMYRRTPEFAHTYRSKHLGGVSLGLRELMGCEDRVMYLISEIACLDALKSDGRVDEMQVCSHVSALGQQLEFTEPPDQIMESPFSATTGLLRPEVLTKNMTAVFRIAARIYLCSLVPGFEATQPSNINLVQALANTLQYIPSGPDGFDRSLVWPLFIAGVHSLPGSQFRTVLMERAAALAEHADLGSFGRMCRVLQEVWRVNDEFAEQHSSLDEGASSSSQTASPVKAEPPSSPRESENSWTTKEAKKPHWRDIMQQNGWNYLLL
Protein: Nicotinamide phosphoribosyltransferase (NAmPRTase) (EC 2.4.2.12) (E7F8T6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR005943}. Cytoplasm {ECO:0000256|PIRNR:PIRNR005943}. Secreted {ECO:0000256|PIRNR:PIRNR005943}.
Interaction partners:
- protein acetyllysine N-acetyltransferase
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide-nucleotide adenylyltransferase
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial 3
- NAD-dependent protein deacetylase sirtuin-2
- NAD-dependent protein deacylase
- Uncharacterized protein LOC393330
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
- Mibp protein
Sequence:
MEKHREAADFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTDSTKPRKVKYDKTVFYGLQYILHKYLKGQVITPEKIQEAKEVYREHFQDDVFNEKGWNYILEKYNGHLPIEIKAVPEGSVIPRGNVLFTVENTDPECYWLTNWVETCLVQIWYPITVATNSREQKKILAKYLMETSGSLEGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIGVIKKYYGTKDPVPGFSVPAAEHSTITAWGKDHEKDAFEHIIKQFPSVPVSIVSDSYDIYNACEKIWGEDLRSLIEMRSADAPLVVRPDSGNPLDTVLKVLEILGKKFPPEENSKGYKVLPPYIRVIQGDGVDINTLQEIVEGMKEHRWSIENIAFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGVNVFKDPVADPNKRSKKGRLSLHRTPSGDFVTLEEGKGDLEEYGEDLLHTVFRNGKIVKTYTFDEVRDNAKLKESEVQDLLL
Protein: Lipid transferase CIDEC (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27) (P56198)
Organism: Mus musculus (Mouse)
Function: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18654663, ECO:0000269|PubMed:20089860, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:30361435, ECO:0000269|PubMed:34508658}. Endoplasmic reticulum {ECO:0000269|PubMed:20089860}. Nucleus {ECO:0000269|PubMed:22245780}. Note=Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites. {ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:34508658}.
Interaction partners:
- Lipid transferase CIDEA
- Perilipin-1
- Perilipin-4
- Hormone-sensitive lipase
- Adiponectin
- Platelet glycoprotein 4
- Peroxisome proliferator-activated receptor gamma
- Fatty acid-binding protein, adipocyte
- Complement factor D
- Scavenger receptor class B member 1
Sequence:
MDYAMKSLSLLYPRSLSRHVAVSTAVVTQQLVSKPSRETPRARPCRVSTADRKVRKGIMAHSLEDLLNKVQDILKLKDKPFSLVLEEDGTIVETEEYFQALAKDTMFMVLLKGQKWKPPSEQRKKRAQLALSQKPTKKIDVARVTFDLYKLNPQDFIGCLNVKATLYDTYSLSYDLHCYKAKRIVKEMLRWTLFSMQATGHMLLGTSSYMQQFLDATEEEQPAKAKPSSLLPACLKMLQ
Protein: 26RFa protein (Pyroglutamylated RFamide peptide) (F5HPR8)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRAPYSLSCLFLLSLGACIPPGERWEPAEPGEGAALGGGWQRAAEGRGPGWRAGARRRRSEELDELLSITRGPGWRAGARRRRSEELEALLSIARELRGYSAAGAGQRPGGSGGPGALPVVGEKRSGTLGNLAEEINGYNRRKGGFTFRFGR
Protein: Arf-GAP with dual PH domain-containing protein 2 isoform X2 (ArfGAP with dual PH domains 2) (E9QE78)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- UTP6 small subunit processome component.
- Cytokine receptor-like factor 3
- Transcription elongation factor
- Zinc finger protein 207, b.
- Rab11 family-interacting protein 4A
Sequence:
MANREKNKKILLELVKLPENNCCADCGAADPDWASCKLGIFVCLTCSGTHRNLPTISRIKSIRLDFWDDELVQFMKANGNCSAKNFYEKCVPVFYYRPHPHDCEVLREQWIRAKYERMEFTEEKTERPYTADVYEGMLWKKGRDNGQFLERKFVLSVHDFTLKYYKEDESKGPKATIYVKNLNATFQPEKIGHAHGLQITYCVEDHTRNLFVYHKNGQEIVNWFNAIRAVRHAYLKTAFPTASDVDIIPWISRNYLKEGYMEKTGPLQREPFKKRWFILDSMDRKLLYFKTQLDAIELGVVFIGSENHGYSVRECVPKGTRGNKWKCGVIVETPDRQFVFMCEQERDQREWVEALKTVISKPMMPQDYTTEANIRRRK
Protein: Protection of telomeres homolog 1 (P42001)
Organism: Caenorhabditis elegans
Function: Telomeric DNA-binding protein, which binds to single-stranded C-rich repeat sequences, with high specificity to the 5'-GCCTAA-3' sequence. Repeat sequence binding can be at the 5' or 3' telomeric end. May have a role in protecting the 5' end of the C-rich strand of the telomere. Acts redundantly with pot-2 to negatively regulate telomerase-mediated telomere extension. Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres). Through sun-1, anchors telomeres to the nuclear envelope in embryos.
Subcellular location: Nucleus {ECO:0000269|PubMed:23390606, ECO:0000269|PubMed:24297748, ECO:0000305|PubMed:18329362}. Nucleus envelope {ECO:0000269|PubMed:24297748}. Chromosome, telomere {ECO:0000269|PubMed:23390606, ECO:0000305|PubMed:18329362}. Note=More highly expressed in meiotic pachytene nuclei than in diakinesis-stage oocyte nuclei (PubMed:23390606). Also expressed in mitotic nuclei (PubMed:23390606). {ECO:0000269|PubMed:23390606}.
Interaction partners:
- Protection of telomeres homolog 2
- Androgen-induced gene 1 protein
- Protection of telomeres protein 1 ssDNA-binding domain-containing protein
- Double-strand telomeric DNA-binding proteins 2
- Double-strand telomeric DNA-binding proteins 1
- Telomerase reverse transcriptase
- 5' exonuclease Apollo
Sequence:
MQYTYQHIQDLVPGPTPQNFYGKIIFIKKKINQIVVLIKDETQSIYLRVIPKEDQELEFQLRQVVRVHRCKIQSILNSKEGIAQIGLFGCHLIAWSQSGKVDNPVIISSRSWTKSDEDSERLQTLRKLGKSRRKSGRKTSVDTMANKLIERREAMFADTFIKSLFNKIALSRKEHLSRNARELFYHRPGDIVETQNLLEIDDSWFNDENSEQFVQYVLNCTTCHVEYNHVEYAQNNIPTNCRFCQEAMESFHAAFRIRISIETYGVFLTIPLELIKTELDICEDWDSESNIVEEEEKVTRFKKNIQEKVRDASIVHIKGISSLLLIIMLNINSISLVNNITENKRILLQKSNVPSSLQLKILITPFVIVVVRFFGITWIYSGSSCIEEVLNLIDNCSRRR
Protein: Egl nine homolog 1 (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 2) (HIF-PH2) (HIF-prolyl hydroxylase 2) (HPH-2) (Prolyl hydroxylase domain-containing protein 2) (PHD2) (SM-20) (Q91YE3)
Organism: Mus musculus (Mouse)
Function: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9GZT9}. Nucleus {ECO:0000250|UniProtKB:Q9GZT9}. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1. {ECO:0000250|UniProtKB:Q9GZT9}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- von Hippel-Lindau disease tumor suppressor
- Prolyl hydroxylase EGLN2
- Prolyl hydroxylase EGLN3
- Hypoxia-inducible factor 3-alpha
- Protein OS-9
- Protein kinase C alpha type
- Protein kinase C gamma type
- Protein kinase C beta type
Sequence:
MASDSGGPGVLSASERDRQYCELCGKMENLLRCGRCRSSFYCCKEHQRQDWKKHKLVCQGGEAPRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGPEDAAQARSGPGPAEPGSEDPPLSRSPGPERASLCPAGGGPGEALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDQITWIEGKEPGCETIGLLMSSMDDLIRHCSGKLGNYRINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELKPNSVSKDV
Protein: MADS-box protein, GAGA1 (Q9ZS30)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENSDVLELDFSCVDRSMSFPDDTGDMSPQRKMGKGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYANNSVKGTIDKYKKACLDPPTSGTVAEANTQYYQQEAAKLRQQIANLQNQNRQFYRNIMGESLGDMPVKDLKNLEGKLEKAISRIRAKKNELLFAEIEYMQKRELELHNSNQFLRAKIVENERAQQHHMSLMPGSSDYELVTPHQPFDGRNYLQTNDLQPNNDYSCQDQTPLQLV
Protein: Thioredoxin reductase (EC 1.8.1.9) (Q5AG89)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Thioredoxin
- Glutathione reductase
- Peroxiredoxin TSA1-A
- Peroxiredoxin TSA1-B
- cystathionine gamma-lyase
- Adrenodoxin
- Peroxisomal catalase
- Vps53p
- Thioredoxin peroxidase
- Trx2p
Sequence:
MVHHKVTIIGSGPAAHTAAIYLARAEIKPTLYEGMLANGIAAGGQLTTTTDIENFPGFPNGIGGSELMEKMKEQSQRFGTEIITETISKVDFSKRPFKLWTEWNEDAEPITTDAVIIATGASAKRMHLPGEDTYWQQGISACAVCDGAVPIFRNNPLAVIGGGDSACEEAIFLTKYASKVFLLVRRDVLRASTIMQKRVTNNEKIEVLWNTEALEAKGDGKLLKSLRIVNNKTKEEKDLQVNGLFYAIGHIPATKIFADQLKTDEAGYIQTTPGTASTSIEGVFAAGDVQDKIYRQAITSAGSGCMAALECEKFISEQEA
Protein: PTS system N,N'-diacetylchitobiose-specific EIIA component (EIIA-Chb) (EIII-Chb) (IIIcel) (N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIA component) (P69791)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2). Also able to use N,N',N''-triacetyl chitotriose (GlcNAc3).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 6-phospho-beta-glucosidase
- PTS system N,N'-diacetylchitobiose-specific EIIC component
- PTS system N,N'-diacetylchitobiose-specific EIIB component
- HTH-type transcriptional regulator ChbR
- Phosphocarrier protein HPr
- 6-phospho-beta-glucosidase AscB
- 6-phospho-beta-glucosidase BglA
- 6-phospho-beta-glucosidase BglB
- Chitooligosaccharide deacetylase ChbG
- Endoglucanase
Sequence:
MMDLDNIPDTQTEAEELEEVVMGLIINSGQARSLAYAALKQAKQGDFAAAKAMMDQSRMALNEAHLVQTKLIEGDAGEGKMKVSLVLVHAQDHLMTSMLARELITELIELHEKLKA