UniProtKB - Q6F5E8 (CARL2_HUMAN)
Capping protein, Arp2/3 and myosin-I linker protein 2
CARMIL2
Functioni
Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization (PubMed:26466680).
Plays a role in cell protrusion formations; involved in cell polarity, lamellipodial assembly, membrane ruffling and macropinosome formations (PubMed:19846667, PubMed:26578515, PubMed:26466680).
Involved as well in cell migration and invadopodia formation during wound healing (PubMed:19846667, PubMed:26578515, PubMed:26466680).
Required for CD28-mediated stimulation of NF-kappa-B signaling, involved in naive T cells activation, maturation into T memory cells, and differentiation into T helper and T regulatory cells (PubMed:27647349, PubMed:27647348, PubMed:28112205).
6 PublicationsGO - Molecular functioni
- phospholipid binding Source: UniProtKB
- protein-containing complex binding Source: UniProtKB
GO - Biological processi
- actin filament network formation Source: UniProtKB
- establishment or maintenance of cell polarity Source: UniProtKB
- establishment or maintenance of monopolar cell polarity Source: UniProtKB
- maintenance of cell polarity Source: InterPro
- negative regulation of barbed-end actin filament capping Source: UniProtKB
- positive regulation of cell migration Source: UniProtKB
- positive regulation of extracellular matrix disassembly Source: UniProtKB
- positive regulation of lamellipodium assembly Source: UniProtKB
- positive regulation of lamellipodium organization Source: UniProtKB
- positive regulation of ruffle assembly Source: UniProtKB
- wound healing, spreading of cells Source: UniProtKB
Enzyme and pathway databases
PathwayCommonsi | Q6F5E8 |
SignaLinki | Q6F5E8 |
Names & Taxonomyi
Protein namesi | Recommended name: Capping protein, Arp2/3 and myosin-I linker protein 21 PublicationAlternative name(s): Capping protein regulator and myosin 1 linker 2Imported F-actin-uncapping protein RLTPRCurated Leucine-rich repeat-containing protein 16C RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:27089, CARMIL2 |
MIMi | 610859, gene |
neXtProti | NX_Q6F5E8 |
VEuPathDBi | HostDB:ENSG00000159753 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 2 Publications
Cytoskeleton
- cytoskeleton 3 Publications
Plasma membrane
- Cell membrane 2 Publications; Peripheral membrane protein Curated; Cytoplasmic side Curated
Other locations
- lamellipodium 1 Publication
- ruffle 2 Publications
Note: Colocalizes to dynamic vimentin filaments both in the central cytoplasm and at leading edges of migrating cells (PubMed:26578515, PubMed:26466680, PubMed:19846667). Colocalizes with F-actin, Arp2/3 complex and cortactin to leading edge lamellipodia, ruffles and macropinosomes of migrating cells (PubMed:26578515).3 Publications
Cytoskeleton
- actin cytoskeleton Source: UniProtKB
- intermediate filament cytoskeleton Source: UniProtKB
Endosome
- macropinosome Source: UniProtKB
Plasma Membrane
- extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- cell leading edge Source: UniProtKB
- cytoplasm Source: UniProtKB
- lamellipodium Source: UniProtKB
- membrane Source: UniProtKB
- ruffle Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, MembranePathology & Biotechi
Involvement in diseasei
Immunodeficiency 58 (IMD58)4 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081149 | 50 | R → T in IMD58; decreased protein expression in patient's cells. 1 PublicationCorresponds to variant dbSNP:rs1567626023EnsemblClinVar. | 1 | |
Natural variantiVAR_081150 | 372 | L → R in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1567628757EnsemblClinVar. | 1 | |
Natural variantiVAR_081151 | 525 | L → Q in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1567629943EnsemblClinVar. | 1 | |
Natural variantiVAR_081152 | 639 | L → H in IMD58. 1 PublicationCorresponds to variant dbSNP:rs775061512EnsemblClinVar. | 1 | |
Natural variantiVAR_081153 | 853 – 1435 | Missing in IMD58; no detectable protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationAdd BLAST | 583 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1021 | R → A: Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1023. 1 Publication | 1 | |
Mutagenesisi | 1023 | R → A: Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1021. 1 Publication | 1 | |
Mutagenesisi | 1096 – 1106 | KKLGTLFAFKK → EEEEEEEEEEE: Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing. 1 PublicationAdd BLAST | 11 | |
Mutagenesisi | 1096 – 1106 | KKLGTLFAFKK → GGGGGGGGGGG: Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing. 1 PublicationAdd BLAST | 11 | |
Mutagenesisi | 1096 – 1106 | Missing : Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing. 1 PublicationAdd BLAST | 11 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 146206 |
MalaCardsi | CARMIL2 |
MIMi | 618131, phenotype |
OpenTargetsi | ENSG00000159753 |
Orphaneti | 542301, Combined immunodeficiency due to CARMIL2 deficiency |
PharmGKBi | PA162401371 |
Miscellaneous databases
Pharosi | Q6F5E8, Tbio |
Genetic variation databases
BioMutai | CARMIL2 |
DMDMi | 172045901 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000325817 | 1 – 1435 | Capping protein, Arp2/3 and myosin-I linker protein 2Add BLAST | 1435 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 991 | PhosphoserineCombined sources | 1 | |
Modified residuei | 993 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1120 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1246 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1303 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 1315 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1420 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Methylation, PhosphoproteinProteomic databases
EPDi | Q6F5E8 |
jPOSTi | Q6F5E8 |
MassIVEi | Q6F5E8 |
MaxQBi | Q6F5E8 |
PaxDbi | Q6F5E8 |
PeptideAtlasi | Q6F5E8 |
PRIDEi | Q6F5E8 |
ProteomicsDBi | 66290 [Q6F5E8-1] 7286 |
PTM databases
GlyGeni | Q6F5E8, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q6F5E8 |
MetOSitei | Q6F5E8 |
PhosphoSitePlusi | Q6F5E8 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSG00000159753, Expressed in cerebellar vermis and 159 other tissues |
ExpressionAtlasi | Q6F5E8, baseline and differential |
Genevisiblei | Q6F5E8, HS |
Organism-specific databases
HPAi | ENSG00000159753, Tissue enhanced (brain, intestine, lymphoid tissue) |
Interactioni
Subunit structurei
Protein-protein interaction databases
BioGRIDi | 126970, 15 interactors |
IntActi | Q6F5E8, 5 interactors |
MINTi | Q6F5E8 |
STRINGi | 9606.ENSP00000334958 |
Miscellaneous databases
RNActi | Q6F5E8, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 64 – 88 | LRR 1Add BLAST | 25 | |
Repeati | 89 – 111 | LRR 2Add BLAST | 23 | |
Repeati | 249 – 272 | LRR 3Add BLAST | 24 | |
Repeati | 274 – 297 | LRR 4Add BLAST | 24 | |
Repeati | 303 – 326 | LRR 5Add BLAST | 24 | |
Repeati | 335 – 362 | LRR 6Add BLAST | 28 | |
Repeati | 393 – 423 | LRR 7Add BLAST | 31 | |
Repeati | 429 – 452 | LRR 8Add BLAST | 24 | |
Repeati | 461 – 481 | LRR 9Add BLAST | 21 | |
Repeati | 492 – 514 | LRR 10Add BLAST | 23 | |
Repeati | 519 – 543 | LRR 11Add BLAST | 25 | |
Repeati | 546 – 572 | LRR 12Add BLAST | 27 | |
Repeati | 581 – 604 | LRR 13Add BLAST | 24 | |
Repeati | 608 – 631 | LRR 14Add BLAST | 24 | |
Repeati | 636 – 660 | LRR 15Add BLAST | 25 | |
Repeati | 664 – 687 | LRR 16Add BLAST | 24 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 573 – 667 | Tropomodulin-likeAdd BLAST | 95 | |
Regioni | 965 – 1435 | DisorderedSequence analysisAdd BLAST | 471 | |
Regioni | 1087 – 1114 | Necessary for localization at the cell membrane1 PublicationAdd BLAST | 28 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 992 – 1006 | Pro residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1020 – 1034 | Basic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1059 – 1079 | Basic and acidic residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 1187 – 1206 | Basic and acidic residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 1230 – 1249 | Basic and acidic residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 1257 – 1271 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1284 – 1302 | Polar residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 1407 – 1421 | Pro residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Leucine-rich repeat, RepeatPhylogenomic databases
eggNOGi | KOG4242, Eukaryota |
GeneTreei | ENSGT00940000161003 |
HOGENOMi | CLU_003119_3_1_1 |
InParanoidi | Q6F5E8 |
OMAi | YIHNWRQ |
OrthoDBi | 208951at2759 |
PhylomeDBi | Q6F5E8 |
TreeFami | TF316381 |
Family and domain databases
Gene3Di | 2.30.29.30, 1 hit 3.80.10.10, 1 hit |
InterProi | View protein in InterPro IPR029763, CARMIL2 IPR031943, CARMIL_C IPR041245, CARMIL_PH IPR001611, Leu-rich_rpt IPR032675, LRR_dom_sf IPR011993, PH-like_dom_sf |
PANTHERi | PTHR24112:SF32, PTHR24112:SF32, 1 hit |
Pfami | View protein in Pfam PF17888, Carm_PH, 1 hit PF16000, CARMIL_C, 1 hit PF13516, LRR_6, 2 hits |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAQTPDGISC ELRGEITRFL WPKEVELLLK TWLPGEGAVQ NHVLALLRWR
60 70 80 90 100
AYLLHTTCLP LRVDCTFSYL EVQAMALQET PPQVTFELES LRELVLEFPG
110 120 130 140 150
VAALEQLAQH VAAAIKKVFP RSTLGKLFRR PTPASMLARL ERSSPSESTD
160 170 180 190 200
PCSPCGGFLE TYEALCDYNG FPFREEIQWD VDTIYHRQGC RHFSLGDFSH
210 220 230 240 250
LGSRDLALSV AALSYNLWFR CLSCVDMKLS LEVSEQILHM MSQSSHLEEL
260 270 280 290 300
VLETCSLRGD FVRRLAQALA GHSSSGLREL SLAGNLLDDR GMTALSRHLE
310 320 330 340 350
RCPGALRRLS LAQTGLTPRG MRALGRALAT NAAFDSTLTH LDLSGNPGAL
360 370 380 390 400
GASEDSGGLY SFLSRPNVLS FLNLAGTDTA LDTVRGCSVG GWMTGRADWR
410 420 430 440 450
AGRGGLGPPA GVANSLPPQL FAAVSRGCCT SLTHLDASRN VFSRTKSRAA
460 470 480 490 500
PAALQLFLSR ARTLRHLGLA GCKLPPDALR ALLDGLALNT HLRDLHLDLS
510 520 530 540 550
ACELRSAGAQ VIQDLVCDAG AVSSLDLADN GFGSDMVTLV LAIGRSRSLR
560 570 580 590 600
HVALGRNFNV RCKETLDDVL HRIVQLMQDD DCPLQSLSVA ESRLKLGASV
610 620 630 640 650
LLRALATNPN LTALDISGNA MGDAGAKLLA KALRVNSRLR SVVWDRNHTS
660 670 680 690 700
ALGLLDVAQA LEQNHSLKAM PLPLNDVAQA QRSRPELTAR AVHQIQACLL
710 720 730 740 750
RNNRADPASS DHTTRLQPLG LVSDPSEQEV NELCQSVQEH VELLGCGAGP
760 770 780 790 800
QGEAAVRQAE DAIQNANFSL SILPILYEAG SSPSHHWQLG QKLEGLLRQV
810 820 830 840 850
GEVCRQDIQD FTQATLDTAR SLCPQMLQGS SWREQLEGVL AGSRGLPELL
860 870 880 890 900
PEQLLQDAFT RLRDMRLSIT GTLAESIVAQ ALAGLSAARD QLVESLAQQA
910 920 930 940 950
TVTMPPALPA PDGGEPSLLE PGELEGLFFP EEKEEEKEKD DSPPQKWPEL
960 970 980 990 1000
SHGLHLVPFI HSAAEEAEPE PELAAPGEDA EPQAGPSARG SPSPAAPGPP
1010 1020 1030 1040 1050
AGPLPRMDLP LAGQPLRHPT RARPRPRRQH HHRPPPGGPQ VPPALPQEGN
1060 1070 1080 1090 1100
GLSARVDEGV EEFFSKRLIQ QDRLWAPEED PATEGGATPV PRTLRKKLGT
1110 1120 1130 1140 1150
LFAFKKPRST RGPRTDLETS PGAAPRTRKT TFGDLLRPPT RPSRGEELGG
1160 1170 1180 1190 1200
AEGDTSSPDP AGRSRPRYTR DSKAYSMILL PAEEEATLGA RPDKRRPLER
1210 1220 1230 1240 1250
GETELAPSFE QRVQVMLQRI GVSRGSGGAE GKRKQSKDGE IKKAGSDGDI
1260 1270 1280 1290 1300
MDSSTEAPPI SIKSRTHSVS ADPSCRPGPG SQGPESATWK TLGQQLNAEL
1310 1320 1330 1340 1350
RSRGWGQQDG PGPPSPGQSP SPCRTSPSPD SLGLPEDPCL GPRNEDGQLR
1360 1370 1380 1390 1400
PRPLSAGRRA VSVHEDQLQA PAERPLRLQR SPVLKRRPKL EAPPSPSLGS
1410 1420 1430
GLGTEPLPPQ PTEPSSPERS PPSPATDQRG GGPNP
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketR4GMZ7 | R4GMZ7_HUMAN | Capping protein, Arp2/3 and myosin-... | CARMIL2 | 124 | Annotation score: | ||
R4GNC4 | R4GNC4_HUMAN | Capping protein, Arp2/3 and myosin-... | CARMIL2 | 55 | Annotation score: |
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081149 | 50 | R → T in IMD58; decreased protein expression in patient's cells. 1 PublicationCorresponds to variant dbSNP:rs1567626023EnsemblClinVar. | 1 | |
Natural variantiVAR_081150 | 372 | L → R in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1567628757EnsemblClinVar. | 1 | |
Natural variantiVAR_081151 | 525 | L → Q in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationCorresponds to variant dbSNP:rs1567629943EnsemblClinVar. | 1 | |
Natural variantiVAR_081152 | 639 | L → H in IMD58. 1 PublicationCorresponds to variant dbSNP:rs775061512EnsemblClinVar. | 1 | |
Natural variantiVAR_081153 | 853 – 1435 | Missing in IMD58; no detectable protein expression in patient's leukocytes; no effect on homodimerization. 1 PublicationAdd BLAST | 583 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_047857 | 384 – 419 | Missing in isoform 2. 1 PublicationAdd BLAST | 36 | |
Alternative sequenceiVSP_047858 | 1346 – 1372 | Missing in isoform 2. 1 PublicationAdd BLAST | 27 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB113647 mRNA Translation: BAD26751.1 Different initiation. FJ026014 mRNA Translation: ACI49710.1 AC009095 Genomic DNA No translation available. AC010530 Genomic DNA No translation available. |
CCDSi | CCDS45513.1 [Q6F5E8-1] CCDS81998.1 [Q6F5E8-2] |
RefSeqi | NP_001013860.1, NM_001013838.1 [Q6F5E8-1] NP_001303955.1, NM_001317026.1 [Q6F5E8-2] |
Genome annotation databases
Ensembli | ENST00000334583.11; ENSP00000334958.5; ENSG00000159753.14 ENST00000545661.5; ENSP00000441481.1; ENSG00000159753.14 [Q6F5E8-2] |
GeneIDi | 146206 |
KEGGi | hsa:146206 |
MANE-Selecti | ENST00000334583.11; ENSP00000334958.5; NM_001013838.3; NP_001013860.1 |
UCSCi | uc002etn.4, human [Q6F5E8-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB113647 mRNA Translation: BAD26751.1 Different initiation. FJ026014 mRNA Translation: ACI49710.1 AC009095 Genomic DNA No translation available. AC010530 Genomic DNA No translation available. |
CCDSi | CCDS45513.1 [Q6F5E8-1] CCDS81998.1 [Q6F5E8-2] |
RefSeqi | NP_001013860.1, NM_001013838.1 [Q6F5E8-1] NP_001303955.1, NM_001317026.1 [Q6F5E8-2] |
3D structure databases
AlphaFoldDBi | Q6F5E8 |
SMRi | Q6F5E8 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 126970, 15 interactors |
IntActi | Q6F5E8, 5 interactors |
MINTi | Q6F5E8 |
STRINGi | 9606.ENSP00000334958 |
PTM databases
GlyGeni | Q6F5E8, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q6F5E8 |
MetOSitei | Q6F5E8 |
PhosphoSitePlusi | Q6F5E8 |
Genetic variation databases
BioMutai | CARMIL2 |
DMDMi | 172045901 |
Proteomic databases
EPDi | Q6F5E8 |
jPOSTi | Q6F5E8 |
MassIVEi | Q6F5E8 |
MaxQBi | Q6F5E8 |
PaxDbi | Q6F5E8 |
PeptideAtlasi | Q6F5E8 |
PRIDEi | Q6F5E8 |
ProteomicsDBi | 66290 [Q6F5E8-1] 7286 |
Protocols and materials databases
Antibodypediai | 49241, 53 antibodies from 12 providers |
DNASUi | 146206 |
Genome annotation databases
Ensembli | ENST00000334583.11; ENSP00000334958.5; ENSG00000159753.14 ENST00000545661.5; ENSP00000441481.1; ENSG00000159753.14 [Q6F5E8-2] |
GeneIDi | 146206 |
KEGGi | hsa:146206 |
MANE-Selecti | ENST00000334583.11; ENSP00000334958.5; NM_001013838.3; NP_001013860.1 |
UCSCi | uc002etn.4, human [Q6F5E8-1] |
Organism-specific databases
CTDi | 146206 |
DisGeNETi | 146206 |
GeneCardsi | CARMIL2 |
HGNCi | HGNC:27089, CARMIL2 |
HPAi | ENSG00000159753, Tissue enhanced (brain, intestine, lymphoid tissue) |
MalaCardsi | CARMIL2 |
MIMi | 610859, gene 618131, phenotype |
neXtProti | NX_Q6F5E8 |
OpenTargetsi | ENSG00000159753 |
Orphaneti | 542301, Combined immunodeficiency due to CARMIL2 deficiency |
PharmGKBi | PA162401371 |
VEuPathDBi | HostDB:ENSG00000159753 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4242, Eukaryota |
GeneTreei | ENSGT00940000161003 |
HOGENOMi | CLU_003119_3_1_1 |
InParanoidi | Q6F5E8 |
OMAi | YIHNWRQ |
OrthoDBi | 208951at2759 |
PhylomeDBi | Q6F5E8 |
TreeFami | TF316381 |
Enzyme and pathway databases
PathwayCommonsi | Q6F5E8 |
SignaLinki | Q6F5E8 |
Miscellaneous databases
BioGRID-ORCSi | 146206, 9 hits in 1012 CRISPR screens |
ChiTaRSi | CARMIL2, human |
GenomeRNAii | 146206 |
Pharosi | Q6F5E8, Tbio |
PROi | PR:Q6F5E8 |
RNActi | Q6F5E8, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000159753, Expressed in cerebellar vermis and 159 other tissues |
ExpressionAtlasi | Q6F5E8, baseline and differential |
Genevisiblei | Q6F5E8, HS |
Family and domain databases
Gene3Di | 2.30.29.30, 1 hit 3.80.10.10, 1 hit |
InterProi | View protein in InterPro IPR029763, CARMIL2 IPR031943, CARMIL_C IPR041245, CARMIL_PH IPR001611, Leu-rich_rpt IPR032675, LRR_dom_sf IPR011993, PH-like_dom_sf |
PANTHERi | PTHR24112:SF32, PTHR24112:SF32, 1 hit |
Pfami | View protein in Pfam PF17888, Carm_PH, 1 hit PF16000, CARMIL_C, 1 hit PF13516, LRR_6, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | CARL2_HUMAN | |
Accessioni | Q6F5E8Primary (citable) accession number: Q6F5E8 Secondary accession number(s): B8X2Z3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 18, 2008 |
Last sequence update: | March 18, 2008 | |
Last modified: | May 25, 2022 | |
This is version 129 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families