wanglab/gogpt-training-data huggingface dataset:
Protein: Dynein regulatory complex protein 8 (Flagellar associated protein 200) (A8J3A0)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
Interaction partners:
- Dynein regulatory complex protein 10
- Dynein regulatory complex subunit 6
- Caltractin
- DUF4821 domain-containing protein.
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- Flagellar associated protein
- Uncharacterized protein
Sequence:
MSKLNDKHERVRARVREAFILFEHKEGSRLVDFKDVPTAVRACGVNPTAVQMTHILDQLAALNAETDATGYVGLENFELVVCNFLIQQEASLFRDDYHTLLRAFRAFDPDGRGFIDAESFKSLLTGKGEALSEDELAKMMTVAADGEGKIWYEDYAQRLANDGRTI
Protein: 5'-AMP-activated protein kinase subunit beta-2 (AMPK subunit beta-2) (Q9QZH4)
Organism: Rattus norvegicus (Rat)
Function: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3) (By similarity).
Interaction partners:
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit beta-1
- Serine/threonine-protein kinase STK11
- Calcium/calmodulin-dependent protein kinase kinase 2
- Glycogen [starch] synthase, muscle
- Forkhead box protein O1
Sequence:
MGNTTSERVSGERHGAKAARAEGGGHGPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVPWQQDLDDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYVFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSTKDSVMVLSATHRYKKKYVTTLLYKPI
Protein: Uncharacterized protein (Q585S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLGSALAPTHNVLVCHSPELPPQQVRCVAECYGVVLDISSYHLVDNTDLVSIVQYRDPESVVLCYESLKAHMSQKGSPVKKVAWVHAKATSEILHKSYIRCPYKEEDTAPTNHAHGFLVAYLGELEDTVRSQFLCSVKADTNAVDFFVDTEYKGRCFLHYPTVEAAEETRRGFSMCHPSLRRAIHHCDEADYFNARKKQLQVDR
Protein: Vasoactive intestinal polypeptide receptor 2 (VIP-R-2) (Helodermin-preferring VIP receptor) (Pituitary adenylate cyclase-activating polypeptide type III receptor) (PACAP type III receptor) (PACAP-R-3) (PACAP-R3) (VPAC2 receptor) (VPAC2R) (P41587)
Organism: Homo sapiens (Human)
Function: This is a receptor for VIP as well as PACAP-38 and -27, the activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Can be coupled to phospholipase C.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:35477937}.
Interaction partners:
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
- Guanine nucleotide-binding protein G
- Vasoactive intestinal polypeptide receptor 1
- Pro-glucagon
- Guanine nucleotide-binding protein G
- Gastric inhibitory polypeptide
- Pro-opiomelanocortin
- Follitropin subunit beta
- Natriuretic peptides A
Sequence:
MRTLLPPALLTCWLLAPVNSIHPECRFHLEIQEEETKCAELLRSQTEKHKACSGVWDNITCWRPANVGETVTVPCPKVFSNFYSKAGNISKNCTSDGWSETFPDFVDACGYSDPEDESKITFYILVKAIYTLGYSVSLMSLATGSIILCLFRKLHCTRNYIHLNLFLSFILRAISVLVKDDVLYSSSGTLHCPDQPSSWVGCKLSLVFLQYCIMANFFWLLVEGLYLHTLLVAMLPPRRCFLAYLLIGWGLPTVCIGAWTAARLYLEDTGCWDTNDHSVPWWVIRIPILISIIVNFVLFISIIRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAVFPISISSKYQILFELCLGSFQGLVVAVLYCFLNSEVQCELKRKWRSRCPTPSASRDYRVCGSSFSRNGSEGALQFHRGSRAQSFLQTETSVI
Protein: SR-CI (Scavenger receptor class C, type I, isoform A) (Scavenger receptor class C, type I, isoform B) (Scavenger receptor protein CI) (Q9V3H7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eater
- Hemolectin, isoform A
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSIDLDNGSINYRQRNVVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLAIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Probable conserved transmembrane protein rich in alanine and arginine and proline (O06278)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0497
- Protein NrdI
- Probable conserved secreted protein
- Uncharacterized protein Rv0955
- Polyprenol-phosphate-mannose-dependent alpha-
- Anti-sigma-M factor RsmA
- CAAX prenyl protease 2/Lysostaphin resistance protein A-like domain-containing protein
- PPE family protein PPE2
- Pantothenate synthetase
- Type III pantothenate kinase
Sequence:
MTVLSRGARVRRGGRRPGWVLLTALLVLAIGASSALVFTDRVELLKLAVLLALWAAVAGAFVSVLYRRQSDVDQARVRDLKLVYDLQLDREISARREYELTLESQLRRELASELRAPAADEVAALRAELAALRTSLEILFDADLEHRPALGTVEKEARAARALDGESPPADWVSSDRVMAVRGGDGASRTDEASIIDVPEVGVPPVSGGPRHYEAPPPPQPEPLFEPRHRPPPLPPQQERPVWQPVTSHGQWLPAETPGSQWASVEPETTPAAPPPGRRRRARHASPADQAYNPPAYVELAAQYGESGRRSRHSAEHRDHDIGGSGAGTGERPPSPPMAPPPPAEPTRRHRTADTPPDDSGGLHARDPLTGGQSVADLMARLQVESTGGGRRRRRGE
Protein: Penicillin-binding protein 1A (PBP-1A) (Penicillin-binding protein 1*) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P71707)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (By similarity). Has little peptidoglycan hydrolytic activity; however it inhibits the synergistic peptidoglycan hydrolysis of RipA plus RpfB.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to poles and occasionally septa upon expression in M.smegmatis. {ECO:0000269|PubMed:20686708}.
Interaction partners:
- Cell wall synthesis protein Wag31
- Probable conserved transmembrane protein
- D-alanyl-D-alanine carboxypeptidase DacB1
- Possible penicillin-binding lipoprotein
- Peptidoglycan D,D-transpeptidase PbpA
- D-alanyl-D-alanine carboxypeptidase DacB2
- Uncharacterized protein
- PASTA domain-containing protein
- L,D-transpeptidase 2
- Penicillin-binding protein PbpB
Sequence:
MNSDGRHHQSSSGAPRGPANPGQRGQVPPDDRLTAILPPVTDDRSAPHADSIEAVKAALDGAPPMPPPRDPLEEVTAALAAPPGKPPRGDQLGGRRRPPGPPGPPGSSGQPAGRLPQPRVDLPRVGQINWKWIRRSLYLTAAVVILLPMVTFTMAYLIVDVPKPGDIRTNQVSTILASDGSEIAKIVPPEGNRVDVNLSQVPMHVRQAVIAAEDRNFYSNPGFSFTGFARAVKNNLFGGDLQGGSTITQQYVKNALVGSAQHGWSGLMRKAKELVIATKMSGEWSKDDVLQAYLNIIYFGRGAYGISAASKAYFDKPVEQLTVAEGALLAALIRRPSTLDPAVDPEGAHARWNWVLDGMVETKALSPNDRAAQVFPETVPPDLARAENQTKGPNGLIERQVTRELLELFNIDEQTLNTQGLVVTTTIDPQAQRAAEKAVAKYLDGQDPDMRAAVVSIDPHNGAVRAYYGGDNANGFDFAQAGLQTGSSFKVFALVAALEQGIGLGYQVDSSPLTVDGIKITNVEGEGCGTCNIAEALKMSLNTSYYRLMLKLNGGPQAVADAAHQAGIASSFPGVAHTLSEDGKGGPPNNGIVLGQYQTRVIDMASAYATLAASGIYHPPHFVQKVVSANGQVLFDASTADNTGDQRIPKAVADNVTAAMEPIAGYSRGHNLAGGRDSAAKTGTTQFGDTTANKDAWMVGYTPSLSTAVWVGTVKGDEPLVTASGAAIYGSGLPSDIWKATMDGALKGTSNETFPKPTEVGGYAGVPPPPPPPEVPPSETVIQPTVEIAPGITIPIGPPTTITLAPPPPAPPAATPTPPP
Protein: F-box/LRR-repeat protein 8 (F-box and leucine-rich repeat protein 8) (F-box protein FBL8) (Q96CD0)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MAEPGEGLPEEVLALIFRHLSLRDRAAAARVCRAWAAAATCSAVWHDTKISCECELEGMLPPYLSACLDHIHNLRLEFEPSRKPSRRAAIELLMVLAGRAPGLRGLRLECRGEKPLFDAGRDVLEAVHAVCGAASQLRHLDLRRLSFTLDDALVLQAARSCPELHSLFLDNSTLVGSVGPGSVLELLEACPRLRALGLHLASLSHAILEALAAPDRAPFALLALRCACPEDARASPLPNEAWVALRRRHPGLAVELELEPALPAESVTRVLQPAVPVAALRLNLSGDTVGPVRFAAHHYAATLCALEVRAAASAELNAALEELAARCAALREVHCFCVVSHSVLDAFRAHCPRLRTYTLKLTREPHPWRPTLVA
Protein: Syncrip, isoform R (A0A0B4KGK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYGSWSWAWNHSTAWQSRWPTWQHQSSGGPNSATGGGSGSGGGTGGGGGSSAGGHRSGGAGSNRGVPWGVANASQRSWHPARQAATKFTSWSCIQNIHGG
Protein: Muscarinic acetylcholine receptor M4 (P08485)
Organism: Rattus norvegicus (Rat)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase.
Subcellular location: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Kininogen-1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
Sequence:
MXNFTPVNGSSANQSVRLVTAAHNHLETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLGCADLIIGAFSMNLYTLYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKPSIKKPPPGGASREELRNGKLEEAPPPALPPPPRPVPDKDTSNESSSGSATQNTKERPPTELSTAEATTPALPAPTLQPRTLNPASKWSKIQIVTKQTGNECVTAIEIVPATPAGMRPAANVARKFASIARNQVRKKRQMAARERKVTRTIFAILLAFILTWTPYNVMVLVNTFCQSCIPERVWSIGYWLCYVNSTINPACYALCNATFKKTFRHLLLCQYRNIGTAR
Protein: Zona pellucida A (A3KEZ4)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Zona pellucida {ECO:0000256|ARBA:ARBA00024183}.
Interaction partners:
Sequence:
MRLLLLLLVGFLLFLAPGASGQWDLSESTTCLQDRLELELPMELGNYTWHVLAVDVSGEEMASCELTVDYEKLLLSALLVNCTSLEHGQHQLRLLLLLNGTAGEERNVTFSARCSAARGDEIIAPVFVGATNCTKDSMAVTFPGPSLGNERPVQVAALPRTLVIDDGTRVHQLSPGEASQHGYSFQADGHSLVLQAAFTATGVVSYQHNHKVLYTAAVKLTYGPPEHRLTMESRMLCAPGPVLCNTTHMTVAVPAFPGTLVSVAVEDETIPMDRLQDNGITLSTARGGWSCTSAGGSWKSALHGESCPGARSYLPSLELTFHFHGDTVAMVMHPACPCDQHTPIAAVCTQDGYMDFEVLAGSTTPPLALDTLRLRDPTCKPASRSPSNDRAWFHVPLSGCGTRYWLEGEKIMYENEVRALQSDRVLHRISRDSEFRLTVLCSFSNGDASVSVRVDSPPPLAASMNQGPLSLILLSYPEDSYRQPYRDDQYPIVRFLQQPIFMEVQVLNRNDPNLYLQLDDCWATASEDPSSLPQWNIVVDGCEYDQDSHRTVFHPIGHGVSYPNYRRRLEVKAFAFMSGDKALPSLVYFHCSVLICNRFQPDSPLCTARCPRLPRSKRGSGMPGASSVVSLQGPVLLVPHGWAAAQGDVLLSEAAWAAVTVAAVGALSLVTAMLLFMALLKCLKRRALMVNVVH
Protein: Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein (Q9BSE4)
Organism: Homo sapiens (Human)
Function: Could be involved in the unfolded protein response (UPR) pathway.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDQSGMEIPVTLIIKAPNQKYSDQTISCFLNWTVGKLKTHLSNVYPSKPLTKDQRLVYSGRLLPDHLQLKDILRKQDEYHMVHLVCTSRTPPSSPKSSTNRESHEALASSSNSSSDHSGSTTPSSGQETLSLAVGSSSEGLRQRTLPQAQTDQAQSHQFPYVMQGNVDNQFPGQAAPPGFPVYPAFSPLQMLWWQQMYAHQYYMQYQAAVSAQATSNVNPTQPTTSQPLNLAHVPGEEPPPAPNLVAQENRPMNENVQMNAQGGPVLNEEDFNRDWLDWMYTFSRAAILLSIVYFYSSFSRFIMVMGAMLLVYLHQAGWFPFRQEGGHQQAPNNNAEVNNDGQNANNLELEEMERLMDDGLEDESGEDGGEDASAIQRPGLMASAWSFITTFFTSLIPEGPPQVAN
Protein: Centrosomal protein of 19 kDa (A8MX07)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}.
Interaction partners:
Sequence:
MSFLYSSKDCTRAAEQLKNNPRHKSYLEQVSLRQLEKLFSFLRGYLSGQSLAETMEQIQRETTIDPEEDLNKLDDKELAKRKSIMDELFEKNQKKKDDPNFVYDIEVEFPQDDQLQSCGWDTESADEF
Protein: F5I14.10 (Pectin lyase-like superfamily protein) (Polygalacturonase/pectinase) (O04474)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Pectate lyase
- Protein FANTASTIC FOUR 4
- At5g15780
- Putative pectinesterase 11
- Probable pectate lyase 13
- Probable pectate lyase 12
- Pectate lyase
- Pectate lyase
- Pectate lyase
Sequence:
MALFLSFVQVFSIVITIIMSHFGQFDARTSLNVLSFGANPNGIVESAKAFSDAWDAACGVEDSVVIYVPKGRYLVSGEVRFEGESCKSREITLRIDGTLIGPQDYSLLGKKENWFSFSGVHNVTVLGGSFDAKGSTLWSCKANGYNCPEGATTLRFMDSNNVKIKGVLSLNSQLFHIAINRCRNIKIEDVRIIAPDESPNTDGIHIQLSTDIEVRNASIKTGDDCISIGPGTKNLMVDGITCGPGHGISIGSLAKSIEEQGVENVTVKNAVFVRTDNGLRIKSWPRHSNGFVERVRFLGAIMVNVSYPILIDQNYCPGDSSCPSQESGIKINDVIYSGIMGTSATEIAIKMDCSEKVPCTGIRMQAINLTSYGEAAKTSCTNVSGKQLGLVTPSGCL
Protein: D-aminoacyl-tRNA deacylase 1 (DTD) (EC 3.1.1.96) (DNA-unwinding element-binding protein B) (DUE-B) (Gly-tRNA(Ala) deacylase) (Histidyl-tRNA synthase-related) (Q8TEA8)
Organism: Homo sapiens (Human)
Function: Possible ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes.
Subcellular location: Nucleus {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}. Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at some replication origins containing functional DNA-unwinding elements (PubMed:20065034).
Interaction partners:
- D-aminoacyl-tRNA deacylase 2
Sequence:
MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISLEDTQKELEHMVRKILNLRVFEDESGKHWSKSVMDKQYEILCVSQFTLQCVLKGNKPDFHLAMPTEQAEGFYNSFLEQLRKTYRPELIKDGKFGAYMQVHIQNDGPVTIELESPAPGTATSDPKQLSKLEKQQQRKEKTRAKGPSESSKERNTPRKEDRSASSGAEGDVSSEREP
Protein: Synaptonemal complex protein 2-like (SCP-2-like) (A0A0M3U1B0)
Organism: Mus musculus (Mouse)
Function: Oocyte-specific protein that localizes to centromeres at the dictyate stage and regulates the survival of primordial oocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:26362258}. Chromosome, centromere {ECO:0000269|PubMed:26362258}. Note=Localized to the synaptonemal complex lateral elements in late diplotene oocytes, while it is absent on the synaptonemal complex of leptotene, zygotene, pachytene and early diplotene oocytes (PubMed:26362258). Localizes to centromeres in dictyate oocytes (PubMed:26362258). Detected in nuclear granules and sizable aggregates (By similarity). {ECO:0000250|UniProtKB:Q5T4T6, ECO:0000269|PubMed:26362258}.
Interaction partners:
Sequence:
MSTLQSLIIDGFHGNGFHMIEEYLQQKESHVPQKYNHLLLHHLDRLIKEELDKNEFQNCSLLLKCIQRFFRDDPDHEEPLLIQQGLIPKMVSWFEIITGLLITKVLASEALLTNALEDFLDTALIISRHSRKATVQMLDSFILRLGFLVAEDSVKPSIQQETLATLNCILNAAPQEERRKLSSAEGACCLMKELARTILTVGDYSQQVALSEALCRMSVGRQRNDLAMQWFENTALAEAFKKIKNREFETDCRQFLNFLNNRLGNQRRVYSFPCLAAFADGQEMRKPADEKLEEFWIDFNLGSQSVTFYIDNAESALWEPVKLLKEAMVKFIIIENDRIKMFIVYLKQPIVISKREAKKIEIHFDRQLGILQASIQALGEDKQAPSFQTSVLVKLFSGLEKEDGEIPGRCEREAEDAEESTLLPELVDAEADRCLITRCFNVQTVPGVSKGSLEITNTEERSLENSKQDEPEQVTSEYDYPLDMQEPSIQNQASDLNNIKEDSAFARDREQDRRMPFNDRNHDLLESNEDSSLSTNERSWTQNHKRKSLRTYSQRKKQRVSSLRILPLSPIRSGHAPEKDEAELVPLWKGISRRNDSTLLKISETKLRGSSVLLTSGASTQKIGLEKPERRGSEPSSSTKKTRVTDGLHWREPRSPHPSSGPSSLEYLEVEENIPEIVNRESFMGNSSFKHKLENLGHREIPDGSVAALKQSRLEDAPGSPVVTDTSTPSQEDMPGSVNGSAFKTAFENFTRDLKRKFELELKQREIPFSLEKAKEAPACLIRLWNQIHTCRLDTLERFHSSVLRELSGLEKNLQTLKCLEKDALASLLFVLSLGRERTFSR
Protein: Single-strand-selective monofunctional uracil-DNA glycosylase 1 (D6RA25)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWL
Protein: Very long chain fatty acid elongase 1 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL1) (ELOVL fatty acid elongase 1) (ELOVL FA elongase 1) (Elongation of very long chain fatty acids protein 1) (Very long chain 3-ketoacyl-CoA synthase 1) (Very long chain 3-oxoacyl-CoA synthase 1) (Q9BW60)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate in the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03201, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:30487246}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03201}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 4
- Very long chain fatty acid elongase 3
- Very long chain fatty acid elongase 7
- Ceramide synthase 2
- Acyl-CoA wax alcohol acyltransferase 1
Sequence:
MEAVVNLYQEVMKHADPRIQGYPLMGSPLLMTSILLTYVYFVLSLGPRIMANRKPFQLRGFMIVYNFSLVALSLYIVYEFLMSGWLSTYTWRCDPVDYSNSPEALRMVRVAWLFLFSKFIELMDTVIFILRKKDGQVTFLHVFHHSVLPWSWWWGVKIAPGGMGSFHAMINSSVHVIMYLYYGLSAFGPVAQPYLWWKKHMTAIQLIQFVLVSLHISQYYFMSSCNYQYPVIIHLIWMYGTIFFMLFSNFWYHSYTKGKRLPRALQQNGAPGIAKVKAN
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta) (P48453)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (By similarity). Dephosphorylates and activates transcription factor NFATC1 (By similarity). Dephosphorylates and inactivates transcription factor ELK1 (By similarity). Dephosphorylates DARPP32 (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB. May play a role in skeletal muscle fiber type specification.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P16298}.
Interaction partners:
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Calmodulin-1
- Nuclear factor of activated T-cells, cytoplasmic 1
- Calmodulin-like protein 3
- Nuclear factor of activated T-cells, cytoplasmic 3
- Calmodulin 5
- Calmodulin-4
Sequence:
MAAPEPARAAPPPPPPPPPPLGADRVVKAVPFPPTHRLTSEEVFDMDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDVGSAAARKEIIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEAIEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHTTENHGTGNHSAQ
Protein: Transcription regulator protein BACH2 (BTB and CNC homolog 2) (Q9BYV9)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that acts as repressor or activator (By similarity). Binds to Maf recognition elements (MARE) (By similarity). Plays an important role in coordinating transcription activation and repression by MAFK (By similarity). Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1. Positively regulates the nuclear import of actin (By similarity). Is a key regulator of adaptive immunity, crucial for the maintenance of regulatory T-cell function and B-cell maturation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17018862, ECO:0000269|PubMed:28530713}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:17018862, ECO:0000269|PubMed:28530713}. Note=Nucleocytoplasmic shuttling is controlled by phosphorylation. {ECO:0000269|PubMed:17018862}.
Interaction partners:
- Transcription factor Maf
- Transcription factor MafG
- Transcription factor MafK
- Transcription factor MafF
- Nuclear receptor corepressor 1
- Interferon regulatory factor 4
- Nuclear receptor corepressor 2
- PR domain zinc finger protein 1
- Paired box protein Pax-5
- Single-stranded DNA cytosine deaminase
Sequence:
MSVDEKPDSPMYVYESTVHCTNILLGLNDQRKKDILCDVTLIVERKEFRAHRAVLAACSEYFWQALVGQTKNDLVVSLPEEVTARGFGPLLQFAYTAKLLLSRENIREVIRCAEFLRMHNLEDSCFSFLQTQLLNSEDGLFVCRKDAACQRPHEDCENSAGEEEDEEEETMDSETAKMACPRDQMLPEPISFEAAAIPVAEKEEALLPEPDVPTDTKESSEKDALTQYPRYKKYQLACTKNVYNASSHSTSGFASTFREDNSSNSLKPGLARGQIKSEPPSEENEEESITLCLSGDEPDAKDRAGDVEMDRKQPSPAPTPTAPAGAACLERSRSVASPSCLRSLFSITKSVELSGLPSTSQQHFARSPACPFDKGITQGDLKTDYTPFTGNYGQPHVGQKEVSNFTMGSPLRGPGLEALCKQEGELDRRSVIFSSSACDQVSTSVHSYSGVSSLDKDLSEPVPKGLWVGAGQSLPSSQAYSHGGLMADHLPGRMRPNTSCPVPIKVCPRSPPLETRTRTSSSCSSYSYAEDGSGGSPCSLPLCEFSSSPCSQGARFLATEHQEPGLMGDGMYNQVRPQIKCEQSYGTNSSDESGSFSEADSESCPVQDRGQEVKLPFPVDQITDLPRNDFQMMIKMHKLTSEQLEFIHDVRRRSKNRIAAQRCRKRKLDCIQNLECEIRKLVCEKEKLLSERNQLKACMGELLDNFSCLSQEVCRDIQSPEQIQALHRYCPVLRPMDLPTASSINPAPLGAEQNIAASQCAVGENVPCCLEPGAAPPGPPWAPSNTSENCTSGRRLEGTDPGTFSERGPPLEPRSQTVTVDFCQEMTDKCTTDEQPRKDYT
Protein: 45 kDa calcium-binding protein (Cab45) (Stromal cell-derived factor 4) (SDF-4) (Q61112)
Organism: Mus musculus (Mouse)
Function: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.
Subcellular location: Golgi apparatus lumen {ECO:0000269|PubMed:16608874}.
Interaction partners:
- Calbindin
- Parvalbumin alpha
- Calmodulin-like protein 4
- Calretinin
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-4
- Calmodulin 5
- Protein S100-B
- Protein S100-G
Sequence:
MVWLVAMTPRQSSLCGLAAHGLWFLGLVLLMDATARPANHSSTRERAANREENEIMPPDHLNGVKLEMDGHLNKDFHQEVFLGKDMDGFDEDSEPRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENKLHFRAVDPDGDGHVSWDEYKVKFLASKGHNEREIAEAIKNHEELKVDEETQEVLGNLRDRWYQADNPPADLLLTEDEFLSFLHPEHSRGMLKFMVKEIFRDLDQDGDKQLSLPEFISLPVGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTGSKLMDYARNVHEEF