wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-glucuronidase (EC 3.2.1.31) (P06760)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the degradation of dermatan and keratan sulfates.
Subcellular location: Lysosome.
Interaction partners:
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B37
- UDP-glucuronosyltransferase 1A1
- N-acetylglucosamine-6-sulfatase
- Klotho
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 2B1
- Hyaluronidase
- Hyaluronidase
Sequence:
MSPRRSVCWFVLGQLLCSCAVALQGGMLFPKETPSRELKVLDGLWSFRADYSNNRLQGFEKQWYRQPLRESGPTLDMPVPSSFNDITQEAELRNFIGWVWYEREAVLPQRWTQDTDRRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADITKLVQSGPLTTFRVTIAINNTLTPYTLPPGTIVYKTDPSMYPKGYFVQDISFDFFNYAGLHRSVVLYTTPTTYIDDITVTTDVDRDVGLVNYWISVQGSDHFQLEVRLLDEDGKIVARGTGNEGQLKVPRAHLWWPYLMHEHPAYLYSLEVTMTTPESVSDFYTLPVGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGRGFDWPLLIKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNVSLRHHLEVMDELVRRDKNHPAVVMWSVANEPVSSLKPAGYYFKTLIAHTKALDPTRPVTFVSNTRYDADMGAPYVDVICVNSYLSWYHDYGHLEVIQLQLTSQFENWYKMYQKPIIQSEYGADAVSGLHEDPPRMFSEEYQTALLENYHLILDEKRKEYVIGELIWNFADFMTNQSPLRVTGNKKGIFTRQRNPKMAAFILRERYWRIANETRGYGSVPRTQCMGSRPFTF
Protein: U1 small nuclear ribonucleoprotein 70 kDa (D3Z8H0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSTTQLACS
Protein: E3 ubiquitin-protein ligase DIS1 (EC 2.3.2.27) (Drought-induced SINA protein 1) (OsDIS1) (RING-type E3 ubiquitin transferase DIS1) (Q10L91)
Organism: Oryza sativa subsp. japonica (Rice)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (Probable). Plays a negative role in drought stress tolerance through transcriptional and post-translational regulation of diverse stress-related genes. Interacts with the serine/threonine-protein kinase NEK6 and promotes its degradation via the 26S proteasome-dependent pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:21719639}. Cytoplasm {ECO:0000269|PubMed:21719639}. Note=Predominantly nuclear. Partially cytoplasmic. {ECO:0000269|PubMed:21719639}.
Interaction partners:
- Calcyclin-binding protein
Sequence:
MASVTYIDDSGSEVIDPPKTEVLDVTELAGDPVPHSPKPNVVVSSSVRELLECPVCLSAMYPPIHQCSNGHTLCSGCKPRVHNRCPTCRHELGNIRCLALEKVAASLELPCKYQNFGCVGIYPYYCKLKHESQCQYRPYSCPYAGSECTVAGDIPYLVNHLKDDHKVDMHNGCTFNHRYVKSNPHEVENATWMLTVFSCFGQYFCLHFEAFQLGMAPVYIAFLRFMGDDLEAKNYSYSLEVGGTGRKMIWQGVPRSIRDSHRKVRDSYDGLIIQRNMALFFSGGERKELKLRVTGRIWKEQ
Protein: RuBisCO chaperone RbcX (Q44212)
Organism: Anabaena sp. (strain CA / ATCC 33047)
Function: An RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00855}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00855}. Note=Most protein is cytoplasmic, but some is in the carboxysome. {ECO:0000255|HAMAP-Rule:MF_00855}.
Interaction partners:
Sequence:
MNLKQIAKDTAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSAGKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEMVVTGIQQANMEKRRQHLERMTQVSLSHPSPESEQQQFSDPDWDNLAS
Protein: Multifunctional methyltransferase subunit TRM112 homolog A (Multifunctional methyltransferase subunit TRM112-like protein At1g22270) (Protein SMALL ORGAN 2) (tRNA methyltransferase 112 homolog A) (AtTRM112a) (Q8LFJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases (By similarity). Required for TRM9 tRNA methyltransferase activity. Involved in the regulation of cell division progression during organ growth. Required for the expression of cell cycle-related genes, and the G2-M phase progression during organogenesis.
Interaction partners:
- tRNA
- tRNA
- AT3g13440/MRP15_7
- 18S rRNA
- At5g64156
- tRNA wybutosine-synthesizing protein 2/3/4
- Alkylated DNA repair protein ALKBH8 homolog
- Methyltransferase-like protein 5
- Bystin
- Methylsterol monooxygenase 2-1
Sequence:
MRLITHNMLSCNIKGVTSGFPLRIEAGNVIEKEVDFNPDFIRHMFAKIEWKALVEGARSMGYAELPEESPDAAVLKSDEPFLKKLHHALLELHLEEGALVCPETGRKFPVNKGIPNMLLHEDEV
Protein: Ribonuclease J2 (RNase J2) (EC 3.1.-.-) (O31760)
Organism: Bacillus subtilis (strain 168)
Function: Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:15831787}.
Interaction partners:
- Ribonuclease Y
- Ribonuclease J1
- Polyribonucleotide nucleotidyltransferase
- DEAD-box ATP-dependent RNA helicase CshA
- ATP-dependent 6-phosphofructokinase
- Ribonuclease Z
- Ribonuclease 3
- Ribonuclease P protein component
- Ribonuclease R
- 3'-5' exoribonuclease YhaM
Sequence:
MKKKNTENVRIIALGGVGEIGKNLYVIEIDSDIFVVDAGLMHPENEMLGIDVVIPDISYLIERADRVKAIFLTHGHDENIGGVFYLLNKLSVPVYGTKLTLALLREKLKQYGHNRKTDLREIHSKSVITFESTKVSFFRTIHSIPDSVGVSFKTSLGSIVCTGDFKFDQTPALNQTCDIGEIAKIGNSGVLALLSDSANAERPGYTPSEAAVSGEISDALYNSQNRVIIAVFASNINRIQQVIHAAAQNGRKIAVAGKNLQSVLQLARKLGYIEADDELFISVQDVKKYPKREVAIITAGSQGEPLAALTRMANKAHKQLNIEEGDTVVIASTPIPGQELIYSKTVDLLARAGAQVIFAQKRVHVSGHGSQEELKLMINLLKPKYLIPVNGEYRMQKAHSKIAEETGMKRSDIFLIEKGDVVEFRGQNVKIGDKVPYGNILIDGLGVGDIGNIVLRDRRLLSQDGILIVVITLDKQKKHLVSGPEIITRGFVYVRESEGLIVQATELVRSIVTEATETSNVEWSTLKQAMRDALNQFLYEKTKRKPMIIPIIMEV
Protein: Cyclin-dependent kinase 1-B (CDK1-B) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 2) (Cell division control protein 2-B) (Cell division protein kinase 1) (p34 protein kinase 2) (P24033)
Organism: Xenopus laevis (African clawed frog)
Function: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. May play a role in regulating the amplitude of the cyclic expression of circadian clock genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06493}.
Interaction partners:
Sequence:
MDEYTKIEKIGEGTYGVVYKGRHKATGQVVAMKKIRLENEEEGVPSTAIREISLLKELQHPNIVCLLDVLMQDSRLYLIFEFLSMDLKKYLDSIPSGQYIDTMLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTHEVVTLWYRASEVLLGSVRYSTPVDVWSVGTIFAEIATKKPLFHGDSEIDQLFRIFRSLGTPNNEVWPEVESLQDYKNTFPKWKGGSLSSNVKNIDEDGLDLLSKMLVYDPAKRISARKAMLHPYFDDLDKSSLPANQIRN
Protein: Extensin-like (B1Q247)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLNMSKLITLNQAHSHPTSIAPSSFQVPVIPPPPTLVTGPLKVAPASLAPVPMEIQSQEQPIKKSPAPTPSLDASNKPVAALASTPQQKESTKKTEKEQKEKAAPSVTAQPRIPHVPNTIPSKQFAQSAEVMMNDLQDKQRKLLSYISSAHNGSVTDEVLHDYLRHPFVLLKEKGVIRQQPNPFFHLMSTPQVLAGTPSVIPTPAMMSPNPAMVQKSSKPSTPIPAPPVLVPQVELPAKTSSVSQKTTVSPPVEKVTPPPQHPPQLSLQVPLNGPQMDPTKQFLVPMTRACNQWSVVSMALPLRLVCRCGQMPCRCQ
Protein: General transcription factor II-I (GTFII-I) (TFII-I) (Q5U2Y1)
Organism: Rattus norvegicus (Rat)
Function: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box (By similarity). Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation (By similarity).
Subcellular location: Cytoplasm. Nucleus. Note=Colocalizes with BTK in the cytoplasm. {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase
- Upstream transcription factor 1, isoform CRA_a.
- Zinc finger MYM-type containing 2
Sequence:
MAQVAMSALPAEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKCTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVAVQGLPEGVAFKHPEHYDLATLKWILENKAGISFIIKRPFLEPKKHLGGRVMAADADRPMLSPGGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQGSHHSSEGNEGAEVEVPAEDSTQHVPSETSEDPEVEVTIEDDDYSPPTKRPKSSEPPPPPPVPEPTNAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAYPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVVSYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNNSPQTSTVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKTNSSPSVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQNESEGPVIQESAEASQLEVPATEEIKETDGSSQIKQEPDPTW
Protein: Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A (EC 3.2.1.151) (Glycosyl hydrolase family protein 9A) (BoGH9A) (A7LXT3)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. May be superfluous in xyloglucan degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan-specific endo-beta-1,4-glucanase.
Subcellular location: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MKIVRYIALFGILSGLAVACTPSTSVIPNDAIRLNQLGYYPNQEKIAVVDSGKVEEFVIWDAVSGEQVFVGKSLYTAKSAWSDKTRTTLDFSAVTTPGKYILKVNGASVTFLIKDSVLSPLADAALKSFYYQRTAMPIEEQYAGQWHRMAGHPDNHVLIHPSAASPDRPAGTIVSSSKGWYDAGDYNKYIVNSGYSIGLMQSIYQLFLDYFSRQKINIPESNNHTPDLLDEMQFNLDWMLTMQDPEDGGVYHKLTTPFFEGFVKPVDCKQQRYVVQKSVTAALDFAAVMAQSSRLFASYEEDYPGFSKRALLAAEKAYAWAEKHPEAYYNQNLLNQKYQPAIATGEYGDTHADDEFFWAASELYFSTGKEIYREEAIKKAPQIYTAPGWGNTFALGIFAWLQPGRELNEADRRFADSLKTELLKYADKVIEGAEQTPFHAPYGNDAKDFFWGCLAEKCMNQGVSLMYAYLQTGKDVYLTNAYRNMDYILGRNATGFCYVTGLGTKSPKHPHHRLSASDDIEDPIPGFLVGGPNPGQQDGAFYPTASPDESYVDTEDSYASNEVAINWNAALVALASSLDALAVYSVK
Protein: TSC complex subunit 1 (A0A2R8Y5S3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQQANVGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATRLSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVSHQISARFPHRSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPQATLWSPSMVCGMTTPPTSPGNVPPDLSHPYSKVFGTTGGKGTPLGTPATSPPPAPLCHSDDYVHISLPQATVTPPRKEERMDSARPCLHRQHHLLNDRGSEEPPGSKGSVTLSDLPGFLGDLASEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYRDSLPGSQRKTHSAASSSQGASVNPEPLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEERLDCCNDGCSDSMVGHNEEASGHNGETKTPRPSSARGSSGSRGGGGSSSSSSELSTPEKPPHQRAGPFSSRWETTMGEASASIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDGMTSSLSESLKTELGKDLGVEAKIPLNLDGPHPSPPTPDSVGQLHIMDYNETHHEHS
Protein: Dynein intermediate chain 1 (Meiotically up-regulated gene 44 protein) (O94518)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiotic nuclear divsion where it promotes the movement of 'horsetails'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dynein heavy chain, cytoplasmic
- Dynein light chain Tctex-type
- Dynein light chain 1
- Dynein intermediate light chain dil1
- Tubulin alpha-1 chain
- Tubulin alpha-2 chain
- Tubulin beta chain
- Actin-like protein arp10
- Microtubule-associated protein ssm4
- Meiotic coiled-coil protein 5
Sequence:
MDKNIKREIEIKRAKLLLLKNKENCTDAVSSSNKEGPKQISEDQLSNFLCKILKPTNLTPQTYSLESKSSNLVSDCELKISSVYQSYSSTFNVSNHVPSISKTVNIRETSKHLKHSTKAPKCSLPTSALEIDHLNNFLHSSAKILDRALCDQSNQLFTDYTVKKKSKKNKSQLEENGLNHLFTFQDEKITLNSVVNSISYSSFFEELLITSYAKPKEALRTRGLAIVWNQRWKNSPESVLKARSEITVCKPSPFHPQLIAGGAYNGQVFLWDLRQGQYPVSFTTIISGGHLEPVTDITYINNPPSNNIVTCSTDGLVHIWEPDMFSRPSETICLSSQVDSSSQCIPATCLSFIPENNMEFLVGAEDGKLQRGYRSDYSETKAVQPSNVSYEGHNVFISGIDVMTSNSQNVFLEKNKDFALTSSFDWTVRLWQCSPSRNQHELVPSNDLDEQVIINSCKTFTHKAMVFDVKWCVSEPCCFASVDALGNLNLWDLQKDVEAPVTSDIPDGKPLNKIAWQPEKRNLACGGLNGNVHIYKHLSPNLAN
Protein: Thyrotropin receptor (Q71MM8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Cell membrane {ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361222}.
Interaction partners:
Sequence:
MMKMKKIMKMLLCMLGCVCVSQAEVAMVNSGTTFTYLCMGNTITHMPTHIPKNTTDLEFKQTHIRVFPREAFTNLQQLTAIVLTENGMLESIGAFAFANLPRLTEITITKSKHLVIIHHQAFIGLPKLSHLTICNTGLRVLPNFSRIHSAALTFLLDLQDNVHIVIIPSNAFLGLTTNTIDELRLTKNGISEVESHAFNGTKIHKLFLMGNLQLSHMHNNSFKGAEGPGFLDISRTALSSLPESVLGEVEHLSAVSVFSLRALPPLSLFTKLRQANLTYPSHCCAFHKHQRNRTFRMTSACFKPGAQNNLHFFMDFCLNWTSVACSPAPDAFNPCEDIMGSAPLRVLIWITSVLALLGNTIVLLVLLGSRAKMTVPRFLMCHLSFADLCMGVYLVVIATVDVRTRGLYYNHAISWQTGAGCDIAGFFTVFASELSVFTLTAITLERCHTITHALRLDRKLRLRHACAVMATGWAFSCLAALLPTVGVSSYSKVSICLPMDVESLPSQVFVMFLLLLNVVAFLCVCVCYLSIYLSVRNSSSPPASAETSRMAQRMAILIFTDFLCMAPISFFALSAALKLPLITVSDSKLLLVLLYPINSCANPFLYGLCTRTFRRDFFLLAARYGLFTTKAQVYRTESFPVQQAAWIQMSPKVSHGTLC
Protein: Calcium-binding protein 1 (CaBP1) (Calbrain) (Caldendrin) (Q9NZU7)
Organism: Homo sapiens (Human)
Function: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14685260}. Cell membrane {ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side. Golgi apparatus {ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}. Postsynaptic density {ECO:0000305}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane. {ECO:0000269|PubMed:10625670}.; SUBCELLULAR LOCATION: [Isoform L-CaBP1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures. {ECO:0000269|PubMed:10625670}.; SUBCELLULAR LOCATION: [Isoform S-CaBP1]: Cytoplasm, cell cortex. Cell membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor {ECO:0000305}. Note=S-CaBP1 is localized at or near the plasma membrane.
Interaction partners:
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Guanylyl cyclase-activating protein 1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- G protein-coupled receptor kinase 5
Sequence:
MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
Protein: Retinoic acid receptor alpha protein (Q50HQ0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
TTLTIADQITLLKSACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLLCGDRQDLEQADKVDVLQEPLLEALKIYVRKRRPHKPHMFPKI
Protein: Uncharacterized protein (Q580D2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEQDSHPRIGLMLTEGQFEALVTRLHDKSVEHKAETLRQLDARFYPTAPPKRLPKEAIESSVVRQVDHEMNRRRAARENLEIQEERKTLSKKISSADVESSVERLYTETLARKKANMEESRKRYLYAGPDMVKKNAKEIQEYVGRLAVPKKKEFTIEEVNKVYDLV
Protein: Protein giant-lens (Protein argos) (Protein strawberry) (Q00805)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates cell determination; development of ommatidia and optic lobe. Is a signaling molecule involved in the process of axon pathfinding in the eye. Part of the Ras pathway regulating programmed cell death in pupal eyes; activated by lozenge (lz). Antagonist for the Egfr receptor (gurken). Inhibits Egfr signaling without interacting directly with the receptor, but instead by sequestering the Egfr-activating ligand spitz (spi).
Subcellular location: Secreted {ECO:0000269|PubMed:1606617}.
Interaction partners:
- Epidermal growth factor receptor
- Protein spitz
- Protein rhomboid
- Ras-like protein 1
- ETS-like protein pointed
- Protein sprouty
Sequence:
MPTTLMLLPCMLLLLLTAAAVAVGGTRLPLEVFEITPTTSTADKHKSLQYTVVYDAKDISGAAAATGVASSTVKPATEQLTVVSISSTAAAEKDLAESRRHARQMLQKQQQHRSIIGGKHGDRDVRILYQVGDSEEDLPVCAPNAVCSKIDLYETPWIERQCRCPESNRMPNNVIIHHHSHSSGSVDSLKYRNYYEREKMMQHKRMLLGEFQDKKFESLHMKKLMQKLGAVYEDDLDHLDQSPDYNDALPYAEVQDNEFPRGSAHMRHSGHRGSKEPATTFIGGCPSSLGVEDGHTIADKTRHYKMCQPVHKLPVCTHFRDYTWTLTTAAELNVTEQIVHCRCPRNSVTYLTKREPIGNGSPGYRYLFACSPLTRLRCQRKQPCKLFTVRKRQEFLDEVNINSLCQCPKGHRCPSHHTQSGVIAGESFLEDNIQTYSGYCMAND
Protein: IKAROS family zinc finger 1 isoform 14 (R9R4D9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVVTYGADDFRDFHAIIPKSFSRERPFQCNQCGASFTQKGNLLRHIKLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
Protein: Protein XNDC1N (XRCC1 N-terminal domain-containing 1 N-terminal like) (Q6ZNB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPVKISHVVSFSSQDPKYPVENLLNPDSPRRPWLGCPQDKSGQLKVELQLERAVPTGYIDVGNCGCAFLQIDVGHSSWPLDRPFITLLPATTLMSLTDSKQGKNRSGVRMFKDVDFLAPASGELWDRLRLTCSRPFTRHQSFGLAFLRVCSSLDSLDDSVVGPSALLSSVLNKIREFKTCFFSWSLKKMELEFSPLLLSINLNDLQFAADAEVSTVSNCMFISIALQSAMIIF
Protein: Proline racemase (Q9L4Q3)
Organism: Acetoanaerobium sticklandii (Clostridium sticklandii)
Interaction partners:
Sequence:
MADKKKYLEDNLDYVRTALMHEPRGHNDMFGSIITSSNNKEADFGIIFMDGGGYLNMCGHGSIGAATVAVETGMVEMVEPVTNINMEAPAGLIKAKVMVENEKVKEVSITNVPSFLYMEDAKLEVPSLNKTITFDISFGGSFFAIIHAKELGVKVETSQVDVLKKLGIEIRDLINEKIKVQHPELEHIKTVDLVEIYDEPSNPEATYKNVVIFGQGQVDRSPCGTGTSAKLATLYKKGHLKIDEKFVYESITGTMFKGRVLEETKVGEFDAIIPEITGGAYITGFNHFVIDPLKYGFTV
Protein: Transmembrane transport protein (Q38FQ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSQLNANAKEWVPTGDFSAFSLPDSAVAEGEGLEQKSGVGTNGSMNTVPGSPPQEQYDTLQWNDMVSDPPPYFPSFMLAGQSISAPNATEVGEFTLEGIDWKKEFDNVMALTRELLERQLNGEQDTPGRQEAAEHEAENAVSNPKGLRATPKTTPGAASILDPAAYPDLPGCDVVRPLQSGKWLKAASAMKGKAQTVLTNLEGREHNGDRVHGTSRIVGGHGMASSVGDDDVDEFGRPLPPLTANGNRRWKKPTKGQQKREAAQKNAFEAFANALLHSVSPFMAPLRERCKTSLPHIKVDQRFGKVGQPHTAVAQFVVAPLVTNYRPRHFHDLTPGDLMEFHYDFAQVLKQLKSADEVLFGYGPVWKRYAVPFCYVNCKEYRDEVLSLCPDEVPNMRVEAIYEDDVVKDITDVVLSVEELEPLQNMSFLQAMGRRVNLAPLFDAFDAVFQPIENYRIIIKELHSAPSTYLIQTSQHEVNQKPQPLVLYNDPKLWYDLPVVSRIKVESTVGRGASERGGAAASGQPGVMSASSLGGPASEKEGQGRNAASGGTTGRKAKDISTDYQNWGGYRFNRAQIYGVLIPLVGSAAFLTVTGFILWRRRKTK
Protein: Protein phosphatase inhibitor 2 (C0H480)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Serine/threonine-protein phosphatase
Sequence:
MKKKVDKSVTKKTISWDEVTINEQDKERGSRMKILEPNTPFNFILMDSASEDEASKYGDVKGSDEGQNNIADDLINKLNQLVEKQENKGVSNIDFKEKRKKHYNEYKMLQKLRKSGTLDDIDEEYKPDNKDSNCDNSNMNESEE
Protein: DAZ protein 1 (Q20870)
Organism: Caenorhabditis elegans
Function: RNA-binding protein that plays a central role in oogenesis, but not for spermatogenesis. Required for meiotic entry and germline differentiation, at the pachytene stage of meiosis I of female germline regardless of the sex of the soma. May act by regulating translation of specific mRNAs, possibly by binding to their 3'-UTR.
Interaction partners:
- Cytoplasmic polyadenylation element-binding protein 3
- Female germline-specific tumor suppressor gld-1
- Ubiquitin-like domain-containing protein
Sequence:
MMSPPLRYQKDQQNQQHQQNQSQQAAHQMVSFMPQTPTSLPSTPIQLYPTGAAALIPAPPTYELIPNRIFVGGFPTSTTETELREHFEKFFAVKDVKMVKSLDGQSKGYGFITFETEDQAEEIRKLTPKQLEFRSRKLNLGPAIRKINSNSFQPSYAIATPSQLVAASPGPFSYAIPASPSPYSGYSYPASPQMFVYPPLRSQDQSRQQSEQQTTPQNSPTNLQHQQSPQVFFGGDQDPIRSYASAVAGVEKSEVSPEKHESVSPQPLLPNQNVLNTQYSQGQQQWNSNVQQQQQQQMDSNNGGPYYNENYSQGYTRPHPYQQFAQSGVYMNSQGMYHSSYSYMTPPLAPGQYPQMMSAPYWQQQQQHHQSHAYAGYNPAYNNWVGPSGDMNQFKQNPSNYFYQNYPGNFSQQHTMGNNENTFSLPLQAPRQGKKSRKPSECQDKKTKSPIKGARTERPSSSASTPDAKYQKNHRYPVHLSPLSASLQSLAISSPTKNN
Protein: Serine/threonine-protein phosphatase 3 (EC 3.1.3.16) (PP2C-like Ser/Thr phosphatase) (Protein phosphatase C) (P76395)
Organism: Escherichia coli (strain K12)
Function: PP2C-like phosphatase that can dephosphorylate YegI. In vitro, can hydrolyze p-nitrophenyl phosphate (pNPP) to p-nitrophenol.
Interaction partners:
- Uncharacterized protein YegL
- Protein kinase YegI
- Uncharacterized protein YegJ
- Ribosomal RNA small subunit methyltransferase B
- Aminomethyltransferase
- Probable transcriptional regulatory protein YeeN
- Uncharacterized protein YrbL
- Uncharacterized protein YhaL
- Bifunctional polymyxin resistance protein ArnA
- Methionyl-tRNA formyltransferase
Sequence:
MSWRLVYASTVGTSHISADLPCQDACQMQIAWLNDQQPLLSVFVADGAGSVSQGGEGAMLAVNEAMAYMSQKVQGGELGLNDVLATNMVLTIRQRLFAEAEAKELAVRDFACTFLGLISSPDGTLIMQIGDGGVVVDLGHGLQLPLTPMAGEYANMTHFITDEDAVSRLETFTSTGRAHKVAAFTDGIQRLALNMLDNSPHVPFFTPFFNGLAAATQEQLDLLPELLKQFLSSPAVNERTDDDKTLALALWAE