wanglab/gogpt-training-data huggingface dataset:
Protein: Small COPII coat GTPase SAR1B (EC 3.6.5.2) (Q9CQC9)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex (By similarity). Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11422940}; Peripheral membrane protein {ECO:0000269|PubMed:11422940}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11422940}; Peripheral membrane protein {ECO:0000269|PubMed:11422940}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y6B6}. Lysosome membrane {ECO:0000250|UniProtKB:Q9Y6B6}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII. Upon leucine deprivation, associates with lysosomal membranes to repress TORC1 signaling. {ECO:0000250|UniProtKB:Q9Y6B6}.
Interaction partners:
- Protein SEC13 homolog
- Guanine nucleotide-exchange factor SEC12
- Protein transport protein Sec31A
- Protein transport protein Sec23A
- Protein transport protein Sec31B
- SEC24 homolog B, COPII coat complex component)
- Protein transport protein Sec24A
- Protein transport protein Sec23B
- Small COPII coat GTPase SAR1A
- SEC24 homolog C, COPII coat complex component
Sequence:
MSFIFDWIYSGFSSVLQFLGLYKKSGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHVQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSVSLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID
Protein: Retinoic acid early transcript 1L (F1LUU5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- NKG2-D type II integral membrane protein
Sequence:
MLGVTGTCVLWLYVHSLSCNLIIRSPTKAEPLWYEGQCSMDGIDFLSFNNVNKTMPLGNQEKMANATEVWTCVTQWIDLLGQDLRDKVSEIKGDTTKTSGHPTLWVTMLSNHSHRHIIGASCVFNISENYSFILDLKTMKWKLINPVPEDIMKEWKDDATLMKHLNLSIAECSQKFNEFLNQHEERTRSRTRAPDIAQPPPTRQFPYKEVLIPVVLIIFIIFICICVKRMCCTQGGRELQLLKDYYINLHKPQRNEGLEETKGEVPNQSTKMLSQEEDPKTLGGPRRASESVELELQMFSSTGS
Protein: E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting-zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (Q6AZ28)
Organism: Rattus norvegicus (Rat)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:9920921}. Nucleus, PML body {ECO:0000250|UniProtKB:O75928}. Nucleus {ECO:0000269|PubMed:9920921}. Note=Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). {ECO:0000250|UniProtKB:O75928, ECO:0000269|PubMed:12077349}.
Interaction partners:
- Small ubiquitin-related modifier 1
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 3
- Signal transducer and activator of transcription 3
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 2
- Androgen receptor
- Signal transducer and activator of transcription 1
- Signal transducer and activator of transcription 5A
Sequence:
MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCTPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGSSSPVEPDLAVAGIHSLPSTSIAPHSPSSPVASVLLQDTKPTFEMQQPSPPIPPVHPDVQLKTLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVTSQPCTKVESSSVFSKPCSVTVASDASKKKIDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPVSSMSSDLPGEQRRNDINNEVQLGTSSDTVQQ
Protein: Hepatocyte growth factor (Hepatopoietin-A) (Scatter factor) (SF) [Cleaved into: Hepatocyte growth factor alpha chain; Hepatocyte growth factor beta chain] (Q08048)
Organism: Mus musculus (Mouse)
Function: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
Interaction partners:
- Hepatocyte growth factor receptor
- Vascular endothelial growth factor receptor 2
- Epidermal growth factor receptor
- Receptor tyrosine-protein kinase erbB-3
- Fibroblast growth factor 2
- Fibronectin
- Mast/stem cell growth factor receptor Kit
- Insulin-like growth factor 1 receptor
- Receptor tyrosine-protein kinase erbB-2
- Kunitz-type protease inhibitor 1
Sequence:
MMWGTKLLPVLLLQHVLLHLLLLHVAIPYAEGQKKRRNTLHEFKKSAKTTLTKEDPLLKIKTKKVNSADECANRCIRNRGFTFTCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDLYENKDYIRNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKTCAHSAVNETDVPMETTECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSQIPKCDVSSGQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTQTTVGWMVSLKYRNKHICGGSLIKESWVLTARQCFPARNKDLKDYEAWLGIHDVHERGEEKRKQILNISQLVYGPEGSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADGLLRVAHLYIMGNEKCSQHHQGKVTLNESELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKVILTYKL
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSW7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Sulfiredoxin
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Thioredoxin
Sequence:
MVAQVQKPAPTFKKTAVIDGVFDEVSLDKYKGKYVVLAFVPLAFTFVCPTEIVAFSEAAKRFEALDAQVLFASTDSEYSLLAWTNVPRQDGGLGPVDIPLLADTNHTLSRDYGVLIEEEGIALRGLFIIDPKGIVRHITINDLPVGRNVEEALRLVEGFQWTDKNGTVLPCNWTPGAATIKPTVEDSKEYFKNVK
Protein: Inactive C-alpha-formylglycine-generating enzyme 2 (Paralog of formylglycine-generating enzyme) (pFGE) (Sulfatase-modifying factor 2) (Q8NBJ7)
Organism: Homo sapiens (Human)
Function: Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010, ECO:0000269|PubMed:18266766}.
Interaction partners:
- Formylglycine-generating enzyme
- Arylsulfatase A
Sequence:
MARHGLPLLPLLSLLVGAWLKLGNGQATSMVQLQGGRFLMGTNSPDSRDGDGPVREATVKPFAIDIFPVTNKDFRDFVREKKYRTEAEMFGWSFVFEDFVSDELRNKATQPMKSVLWWLPVEKAFWRQPAGPGSGIRERLEHPVLHVSWNDARAYCAWRGKRLPTEEEWEFAARGGLKGQVYPWGNWFQPNRTNLWQGKFPKGDKAEDGFHGVSPVNAFPAQNNYGLYDLLGNVWEWTASPYQAAEQDMRVLRGASWIDTADGSANHRARVTTRMGNTPDSASDNLGFRCAADAGRPPGEL
Protein: F17F16.6 protein (Q9FWQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Stress-response A/B barrel domain-containing protein UP3
- Hydrolase-like protein family
- Peroxisomal membrane protein 11B
- Peroxisomal membrane protein 11D
- Peroxisomal membrane protein 11C
- 15.7 kDa heat shock protein, peroxisomal
- Plasminogen activator inhibitor
Sequence:
MENHHRISATKYNGEAVSDDVGQGKLYSPNHAIKISPESDENVGQGNLYSPDHAIKIATNPDSVDSSSEEEEGEKQRKTIMLGLKNLAAVKDKVLEKLSAASVPSESLENAKQFLEGAIKDFAGAAQGMTKDALHRIKTQLAVIVPSVSPAVTEKIVDDAEKEAIDGEEEDESKSKESSGKLPFVSPTSSFFSSLAKPFSKL
Protein: Non-histone chromosomal protein HMG-17 (High mobility group nucleosome-binding domain-containing protein 2) (P05204)
Organism: Homo sapiens (Human)
Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10739259}. Cytoplasm {ECO:0000269|PubMed:10739259}. Note=Cytoplasmic enrichment upon phosphorylation.
Interaction partners:
- Non-histone chromosomal protein HMG-14
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL14
Sequence:
MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK
Protein: I[[h]] channel, isoform E (A1Z9N7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHVKHTQRRVSGPGAFGTFTNDQRASRDNLCPDNQQQQQQRHSHSHQHLVRQSLVSLSNGQPAASAAPDSVSLLRAGDDQQQHPQQPHLQQQQQQQQHLQQQQQRHRSSSSRLSTSGISKQNSSDSRSGLRILDSSHSPVSCGTQSVSSTGGQSALYDACHEYSRSLSAAAAEGAASLLKSHYSDQQLAQTEPDPEPDPERDRDRDRDRDRDRERERRHLTNLNLNLSSEYDYSGSDKQQLVNETYIFKCIANSPSFLRTNKIKEQSKKLRNLSLKTRTAKKKGQIISKSNAVSDNSLHPGDKYLNLYLVEKKHSLQPQVASTSSSINTTHPQASSAPASSSSTCTKAPQLPALSAVAARQQQLLLNGSLKGKGQSQSQGQSRQTLPGHRASVRSESGSGSSHTIPATGKSPPVPHSLAAKISSSASGSKNCNLLSASSNSCHKLNAHAQGSGAGSGSGSGSGSGPPGHSHYAAASPKSSVSSNGHLNKYCLTDLTRRKAEFNRQLSAPTDYTHHSSSNGSQQEGSSEANEGHEPVGESTITVASAGVSYPHPYSYPYHYAHHASSATAPANLKASLQLHSFGSHHPCPYPARPTSTSCTNSFNRRHIRRHKGKLGDRLLSGDSEESVRCSYCSVLNVNDNDLRISFENTCTDSLVTAFDDEALLICDQGTEMVHFDDVSLYGTPKEEPMPNIPIVSEKVSANFLKSQLQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMQQDNAEQVILDPKLIAKHYLRTWFFLDLISSIPLDYIFLIFNQIMKLQDFSDSFQILHAGRALRILRLAKLLSLVRLLRLSRLVRYVSQWEEVYILQNLQKKSADRRGRMNRKDKDGLTKSNLILKFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVSINELQESYWLEQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIQSLDSSRRQYREKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGEVATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERLNKIGKNPNIMHQKDEQLSNPESNTITAVVNALAAEADDCKDDDMDLKENLLHGSESSIAEPVQTIREGLPRPRSGEFRALFEGNTP
Protein: Calmodulin (CaM) (P06787)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8247006}.
Interaction partners:
- Spindle pole body component 110
- Serine/threonine-protein phosphatase 2B catalytic subunit A1
- Tubulin beta chain
- Myosin-2
- Myosin-5
- Calcium-channel protein CCH1
- Calcium/calmodulin-dependent protein kinase I
- Actin
- Calcium/calmodulin-dependent protein kinase II
- Myosin-3
Sequence:
MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAEVDDMLREVSDGSGEINIQQFAALLSK
Protein: Methylxanthine N1-demethylase NdmA (EC 1.14.13.178) (1-methylxanthine demethylase) (H9N289)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline, paraxanthine, and 1-methylxanthine to 3-methylxanthine, 7-methylxanthine, and xanthine, respectively. NADH is the preferred substrate.
Interaction partners:
Sequence:
MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERYGLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKDAPADEVSVVADKVSIQYRKWLRELKEAHKEGSQAFRSALLDPVIESDRSYI
Protein: Ras-related protein Rab-38 (EC 3.6.5.2) (Melanoma antigen NY-MEL-1) (P57729)
Organism: Homo sapiens (Human)
Function: May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (By similarity). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays an important role in the control of melanin production and melanosome biogenesis. In concert with RAB32, regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000269|PubMed:12643545}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane {ECO:0000269|PubMed:23084991}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). The BLOC-3 complex, a heterodimer of HPS1 and HPS4 promotes its membrane localization (PubMed:23084991). {ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
Interaction partners:
- Condensin complex subunit 3
- Ankyrin repeat domain-containing protein 27
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Ras-related protein Rab-32
- Tyrosinase
- BLOC-3 complex member HPS4
- Leucine-rich repeat serine/threonine-protein kinase 2
- Unconventional myosin-VIIa
- BLOC-3 complex member HPS1
Sequence:
MQAPHKEHLYKLLVIGDLGVGKTSIIKRYVHQNFSSHYRATIGVDFALKVLHWDPETVVRLQLWDIAGQERFGNMTRVYYREAMGAFIVFDVTRPATFEAVAKWKNDLDSKLSLPNGKPVSVVLLANKCDQGKDVLMNNGLKMDQFCKEHGFVGWFETSAKENINIDEASRCLVKHILANECDLMESIEPDVVKPHLTSTKVASCSGCAKS
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (A0A140NCK4)
Organism: Escherichia coli (strain B / BL21-DE3)
Interaction partners:
Sequence:
MSKVGINGFGRIGRLVLRRLLEVKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDFTEDSLIVDGKSIAVYAEKEAKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGSVTELVSILGKKVTAEEVNNALKQATTNNESFGYTDEEIVSSDIIGSHFGSVFDATQTEITAVGDLQLVKTVAWYDNEYGFVTQLIRTLEKFAKL
Protein: Protein spindle-F (Q9V9Y9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in oocyte axis determination and microtubule organization during oogenesis. Also required for polarized organization of the bristle. Required, with jvl, for activation of the kinase IKKepsilon in the germ line. Also required for localization of IKKepsilon to the distal tip of elongating bristles by acting as an adapter linking IKKepsilon and cytoplasmic dynein. Involved in dendrite pruning in larval sensory neurons during metamorphosis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16540510}. Cytoplasm {ECO:0000269|PubMed:18796167}. Cell projection, axon {ECO:0000269|PubMed:26540204}. Cell projection, dendrite {ECO:0000269|PubMed:26540204}. Perikaryon {ECO:0000269|PubMed:26540204}. Note=Localizes to the minus ends of microtubules in oocytes (PubMed:16540510). Found in a punctate pattern colocalized with IKKepsilon in nurse cells (PubMed:16540510, PubMed:18796167). Displays a punctate pattern in the soma, dendrites and axons of larval C4da neurons but becomes dispersed in pupal neurons which is necessary for dendrite pruning (PubMed:26540204). {ECO:0000269|PubMed:16540510, ECO:0000269|PubMed:18796167, ECO:0000269|PubMed:26540204}.
Interaction partners:
- Javelin-like, isoform D
- FI05319p
- Dynein light chain 1, cytoplasmic
- Dynein heavy chain, cytoplasmic
Sequence:
MEASAAKITPMASSMSASGSTNSPSSEKMNYALQVALQTIKERCIQLQRRVASMEEENQQLREASSRSEGAPRANEIGVTGDVLSLKAQVSELQRQKEQLEEHIGMVSNENRRLWSRLSQISKDQQLNALPSSTDSRAQQNQNLVRSKTFTQHSPNPHLRQKMLSDGIKDLSLEEIALDDFGASSEELGYPYNLQKVEETTSEPDANVDAKRCLDGLQELRREAMKQQQELRSVMTLLENRIALKPCPECAQKTIKKPEMADKSLETDDSLTSELKNYESQHNGHNGTPPSQRINIIQEKIKADAADAMEKTCPMCGKQYSSQVSFNAFREHVEMHFIDDALELESENSIERQFEFVSHAVGDF
Protein: Integrator complex assembly factor WDR73 (WD repeat-containing protein 73) (Q567G2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May play a role in the regulation of microtubule organization and dynamics.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6P4I2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6P4I2}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q6P4I2}. Cleavage furrow {ECO:0000250|UniProtKB:Q6P4I2}. Note=During interphase, located in the cytosol. During mitosis, accumulates at the spindle poles and microtubule asters and later in the cleavage furrow. {ECO:0000250|UniProtKB:Q6P4I2}.
Interaction partners:
- Mortality factor 4-like protein 1
- AT-rich interactive domain-containing protein 4B
- AT-rich interactive domain-containing protein 4A
- Si:ch211-262i1.5
- Si:ch211-9d9.1.
- Histone acetyltransferase type B catalytic subunit
- Polycomb protein eed
- Nuclear autoantigenic sperm protein
- Chromatin assembly factor 1 subunit B
- Protein lin-9 homolog
Sequence:
MDISSDESDDWFMESLNAYRDLHLFQLEHPTKVIEWMGDKSICVAGYTGARSEILELLLPLKLYAGDNQGLCAERDFKVKHGGFSEEPVECLIHIPGTRCLVTSGNSNTLQIWDIGGDDSDVIKMTRVINLKSPSAKGSKITPGFTDSPTVLHGSCISDIQLTEIATGRVLHTVGKESSDSVSGLQFVNAFVFLICSTNGALLLGDTRDPSTCHYPLEESNSGLRWSFGLRSDSSQSEPSCCKVARLSSSGHMLLSDLRDLKSPFCQTQIKVPQSASKNHFMNISWAPVLDKCLSVSGFDGTVHIYNTNNWSTESSSPQPIFSHRGHEMSQEAKSSTSPAVVTAHSWHPSRPKTLLSAATDGSLHVWDWVDKITDR
Protein: Chemokine (C-C motif) receptor 4 (cDNA FLJ75821, highly similar to Homo sapiens chemokine (C-C motif) receptor 4 (CCR4), mRNA) (A0N0Q1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNPTDIADTTLDESIYSNYYLYESIPKPCTKEGIKAFGELFLPPLYSLVFVFGLLGNSVVVLVLFKYKRLRSMTDVYLLNLAISDLLFVFSLPFWGYYAADQWVFGLGLCKMISWMYLVGFYSGIFFVMLMSIDRYLAIVHAVFSLRARTLTYGVITSLATWSVAVFASLPGFLFSTCYTERNHTYCKTKYSLNSTTWKVLSSLEINILGLVIPLGIMLFCYSMIIRTLQHCKNEKKNKAVKMIFAVVVLFLGFWTPYNIVLFLETLVELEVLQDCTFERYLDYAIQATETLAFVHCCLNPIIYFFLGEKFRKYILQLFKTCRGLFVLCQYCGLLQIYSADTPSSSYTQSTMDHDLHDAL
Protein: F-box/LRR-repeat protein At3g59250 (Q9LX46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Defensin-like protein 200
- Cystatin/monellin superfamily protein
- RING-type E3 ubiquitin transferase
- Cysteine/Histidine-rich C1 domain family protein
- Nucleolin 2
- Protein FANTASTIC FOUR 3
- Sulfite exporter TauE/SafE family protein 1
- NAC domain containing protein 50
- At1g48720
- Probable serine/threonine-protein kinase PBL25
Sequence:
MDIGPKDKISNLPEALICHILSFLPIEDSALTSVLSKRWRYLFAFRPNLVFDDSVCLRPPCGHGVIPDYVTSWILNVLERGVLDLDLQVNVNGVRLPSKVFVSKSLVRLRIESGNVRGIDVDDVFLPKLKSLYLHTIMLGKGEDCFEKLTSGCHVLEELVLNNVYSNVWNRSVSSKTLKRLTLWCTESYDKNPHSVLFDTPNLVYLKYSDYVAAKYPKVNFSSLVDATIGLAMTSDQDANASYDALVGNATDFLMGICNVQILCLSANSLAVLTFCCESIPVFNNLIQLTIKTNQSVGWESLPALLKNCPILETLVFEGLLHMYTIKCGDVDGCLCKYSGEVPSCLSSSPVKVLKILRFGEYGIVNQIEMIKIFLETMPHLEQLTVYYNTPIGGDLIEEVSSQLKNFAREASPNCEIQVIPDVLS
Protein: Histidine-containing phosphotransfer protein 1 (Q9ZNV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction through the multistep His-to-Asp phosphorelay.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18642946}. Nucleus {ECO:0000269|PubMed:18642946}.
Interaction partners:
- Histidine kinase 5
- Histidine kinase 4
- Ethylene receptor 1
- Two-component response regulator ARR1
- Two-component response regulator ARR2
- Two-component response regulator ARR4
- Histidine kinase 2
- Two-component response regulator ARR9
- Histidine kinase 3
- Putative two-component response regulator-like APRR6
Sequence:
MDLVQKQKSLQDYTKSLFLEGILDSQFLQLQQLQDESNPDFVSQVVTLFFQDSDRILNDLSLSLDQQVVDFKKVDPHVHQLKGSSSSIGAQRVKNACVVFRSFCEQQNVEACHRCLQQVKQEYYLVKNRLETLFKLEQQIVASGGMIPAVELGF
Protein: Filamin (Q90WF1)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSAAGRAREPEAEMPATEKDLADDAPWKRIQQNTFTRWCNEHLKCVQKRVGNLQTDLGDGLRLIALLEVLSQKKLGRRYNARPTFRQMQLENVSVALDFLERENIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDEDEEEARRQTPKQRLLGWIQNRLPQLPVTNFSRDWSSGRALGALVDSCAPGLCPDWESWDPERAVENAREAMQQADEWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNVVKQRAEFTVETISAGQGDVTVYVEDPEGHREEAKVVPNNDKNRTFSVSYVPKVTGVHKVTVLFAGQHIAKSPFEVAVGRAAGDAGRVTAQGPGIEPTGNVANRTTHFDILTAGAGPGSPDVVVTDPGGRRVEALLEGRGDGAFRCSYRPTAEGTHSVAVTFGGTPIPRSPFAVGVGQACNPSQCRAEGRGLQPKGLRVKEAADFKVYTKGAGSGELKVAVKGPKGAKALKQKDLGEGVFGCEYTPTVPGAHSVTFTYGGQPIPRSPFEVQVAPAGGAPKVRAWGRGLQGGMVGCSADFVVEALGDDVGTLGFSVEGPSQARIECSDGGDGCCAVGYRPLEAGLYAVHVLCDGDDIAGSPFMATVRGPERGCCPDKVKAQGPGLEPTGVAVNQPAEFTVDAKQAGKGPLTVQIQDSEGTPVEVAVKDRGDGTYSCSYTPRKALKHTAVLAWGGVNIPHSPYRVSVGPGSHPNKVKVYGPGVGKTGLKAHEPTYFTVDCSEQGQGDVSIGIKSAPGVVGPAEADLDFDILRNADDTFTVRYTPRGAGMHTVMVLFADQPTPSSPIRVRVDPSHDASKVKAEGPGLSRTGLELGKPTQFTVLSKGAGRAALDVEVSGPGKGDAVRDLEVRDNRDGTHTVTYTPVQQGNLEVSVKYGGDPIPKSPFGVTVSPAVELGRIKISGLDDKLEVGKEQEFTVKAKGAGGQGKVGARIVGPTHKAVPCRVEAGPGAESSVVRWTAPHEGPYEVEVTYDGHPVPGSPFPVEAVPPTDPSKVRAFGPGLQGGQAGVPAPFTIDTKGAGTGGLGLTVEGPCEAPIECQDHGDGTCSVSYLPAVPGDYTINILFAGAHVPGSPFRAPVAAPFDPTKVTCEGPGLEKGVVGQRSHFRVDCSRAGSAELSIGIASDGGAQAEVCVEDNGDGTYNIGYTALSPGPHSITVLYGGQPVPHFPAKVCVEPAGDAAAVKVYGPGVEGKGVFRGALTHFEVDARALGAAGGAAVTARIRKPSGGGVEAAVEDRGDGTYGVQYTPYEEGVHTVEVSYGGSPLPAGPFRVAVTEGCDPSRVRVHGPGIAGGTARQPNCFTVETRGAGTGGLGLAMEGPSEAQLSCTDNKDGSCSVQYIPSAPGTYSLNVTYGGRRVPGSPFRVPVVETGGGGGAADAGMVKCAGPGLTKGEVRVNPVQRFDVDCSKAGEAALDVKVVGPKGVVEPVEVTDNGDGTRSVSYVPSREGPYSISVRYGDQEVPRSPFKVKALPSHDASKVRASGPGLNTSGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKASIRDNGDGTYTVSYVPDTTGRYTILIKYGGDEIPYSPYRIRAVPAGDASKCTVTGPGLGPTIQLGEQTLLTVDAKAAGPGKVTCAVRAPDGAEADVDVVENADGTFDIFYTAPQPGKYIICVRFGGEHVPNSPFQVMATERPLLGVNGLDVGLRPFDLVIPLTIAKGEITGEVRMPSGKVSRPAITDNKDGTVTVRFEPSEAGLHQMDIRYDSVHIPGSPLQFYVDYVNSGHVTAYGPGLTHGTVNKAAQFTVNTKDAGEGGLSLAVEGPSKAEISCTDHQDGTCTVSYLPVLPGDYSIVVKYNDKHIAGSPFTARITGDDSLRQSHLKVGASADIPLDIAESDLSQLAASVTAPSGRKEPCQLKRLRDGHVGISFVPQEVGEHLVHISRGGQPLPRSPITVSISQAELGDAARVRVGGPGLHEGRTLTPTHFTIDTRDAGYGGLSLSIEGPSKVDISTEELPDGTCRVGYCPTEPGNYIIAVQFGEQHVPGSPFSVKVTGEGRVKESITRRRRAPPEAHVGTACDLSLKMPEPTAHDVTAQVTAPSGTSMAAQVLEGERGAYSIRFVPEESGVHSVSVKDRGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAETGVPAEFSIWTREAGAGGLSISVEGPSKAEIAFEDRKDGSCGVSYVVQEPGDYEVAVKFNEEHIPDSPFVVTAAPNSDAARRLTVSSLRESGLKVHQPASFAVSLNGAKGALDAKVHSPSGAVEECHISEVTEDKYAVRFIPRENGVYSIDVKFDGAHIPGSPFKVRVGDPGQAGDPGLVTAYGAGLEGGTTGSPAEFVVNTLHAGPGALSVTIEGPSKVKMECVECPEGFRVVYTPMAPGSYLIAIKFGGPHHIAGSPFKAKVTGPRLVSTHSLRESSSVLVDSGMGGGVSVPPPSATAAAPSSTSAPPGGVPQFSDPSKVVAKGLGLSKAFVGQRNSFTVDCSKAGSNMLLVGIQGPRAPCEELQVKHLGRQLYSVAYVVRERGEHLLVLKWGDHHVPHSPFRITVP