Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Macrophage-capping protein

Gene

CAPG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA.

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

  • barbed-end actin filament capping Source: ProtInc
  • protein complex assembly Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage-capping protein
Alternative name(s):
Actin regulatory protein CAP-G
Gene namesi
Name:CAPG
Synonyms:AFCP, MCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1474. CAPG.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • F-actin capping protein complex Source: ProtInc
  • Flemming body Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • mitotic spindle Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26056.

Polymorphism and mutation databases

BioMutaiCAPG.
DMDMi313104088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Macrophage-capping proteinPRO_0000218753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei337 – 3371Phosphoserine; in variant Arg-335Combined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP40121.
MaxQBiP40121.
PaxDbiP40121.
PeptideAtlasiP40121.
PRIDEiP40121.
TopDownProteomicsiP40121-1. [P40121-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00027341.

PTM databases

iPTMnetiP40121.
PhosphoSiteiP40121.

Expressioni

Tissue specificityi

Macrophages and macrophage-like cells.

Gene expression databases

BgeeiP40121.
CleanExiHS_CAPG.
ExpressionAtlasiP40121. baseline and differential.
GenevisibleiP40121. HS.

Organism-specific databases

HPAiHPA018843.
HPA019080.
HPA019092.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SIAH1Q8IUQ43EBI-4291044,EBI-747107

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107272. 28 interactions.
DIPiDIP-61547N.
IntActiP40121. 4 interactions.
MINTiMINT-5232538.
STRINGi9606.ENSP00000263867.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 2610Combined sources
Beta strandi28 – 336Combined sources
Turni36 – 405Combined sources
Beta strandi41 – 433Combined sources
Beta strandi46 – 538Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 657Combined sources
Helixi71 – 8212Combined sources
Beta strandi92 – 987Combined sources
Helixi104 – 1074Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi139 – 1435Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi149 – 1535Combined sources
Helixi157 – 1593Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi173 – 1786Combined sources
Helixi184 – 19815Combined sources
Turni200 – 2045Combined sources
Beta strandi207 – 2126Combined sources
Helixi218 – 2247Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi269 – 2724Combined sources
Helixi274 – 2763Combined sources
Beta strandi281 – 2866Combined sources
Helixi288 – 2903Combined sources
Beta strandi291 – 2977Combined sources
Helixi303 – 32018Combined sources
Beta strandi327 – 3326Combined sources
Turni338 – 3403Combined sources
Beta strandi343 – 3453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J72X-ray2.50A1-348[»]
1JHWX-ray2.80A1-348[»]
ProteinModelPortaliP40121.
SMRiP40121. Positions 11-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40121.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 7549Gelsolin-like 1Add
BLAST
Repeati148 – 18841Gelsolin-like 2Add
BLAST
Repeati261 – 30747Gelsolin-like 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 14610Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 3 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000235030.
HOVERGENiHBG001093.
InParanoidiP40121.
KOiK10368.
OMAiTERALNW.
PhylomeDBiP40121.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029917. CapG.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF13. PTHR11977:SF13. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40121-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYTAIPQSGS PFPGSVQDPG LHVWRVEKLK PVPVAQENQG VFFSGDSYLV
60 70 80 90 100
LHNGPEEVSH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG
110 120 130 140 150
NESDLFMSYF PRGLKYQEGG VESAFHKTST GAPAAIKKLY QVKGKKNIRA
160 170 180 190 200
TERALNWDSF NTGDCFILDL GQNIFAWCGG KSNILERNKA RDLALAIRDS
210 220 230 240 250
ERQGKAQVEI VTDGEEPAEM IQVLGPKPAL KEGNPEEDLT ADKANAQAAA
260 270 280 290 300
LYKVSDATGQ MNLTKVADSS PFALELLISD DCFVLDNGLC GKIYIWKGRK
310 320 330 340
ANEKERQAAL QVAEGFISRM QYAPNTQVEI LPQGHESPIF KQFFKDWK
Length:348
Mass (Da):38,499
Last modified:November 30, 2010 - v2
Checksum:iBE6E5641D15E9C07
GO
Isoform 2 (identifier: P40121-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-221: Missing.

Note: No experimental confirmation available.
Show »
Length:333
Mass (Da):36,857
Checksum:iD0CFFAF6C1F8147F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411V → I.
Corresponds to variant rs2229668 [ dbSNP | Ensembl ].
VAR_047776
Natural varianti198 – 1981R → W.
Corresponds to variant rs11539103 [ dbSNP | Ensembl ].
VAR_047777
Natural varianti335 – 3351H → R.Combined sources5 Publications
Corresponds to variant rs6886 [ dbSNP | Ensembl ].
VAR_047778

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei207 – 22115Missing in isoform 2. 1 PublicationVSP_045538Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94345 mRNA. Translation: AAA59570.1.
AK225374 mRNA. No translation available.
AC062037 Genomic DNA. Translation: AAY24128.1.
CH471053 Genomic DNA. Translation: EAW99517.1.
CH471053 Genomic DNA. Translation: EAW99518.1.
CH471053 Genomic DNA. Translation: EAW99519.1.
CH471053 Genomic DNA. Translation: EAW99520.1.
BC000728 mRNA. Translation: AAH00728.1.
BC014549 mRNA. Translation: AAH14549.1.
U12026 Genomic DNA. Translation: AAA92670.1.
CCDSiCCDS1974.1. [P40121-1]
CCDS58715.1. [P40121-2]
PIRiA43358.
RefSeqiNP_001243068.1. NM_001256139.1. [P40121-1]
NP_001243069.1. NM_001256140.1. [P40121-2]
NP_001307661.1. NM_001320732.1. [P40121-1]
NP_001307662.1. NM_001320733.1. [P40121-1]
NP_001738.2. NM_001747.3. [P40121-1]
XP_011531424.1. XM_011533122.1. [P40121-1]
XP_011531425.1. XM_011533123.1. [P40121-1]
UniGeneiHs.516155.

Genome annotation databases

EnsembliENST00000263867; ENSP00000263867; ENSG00000042493. [P40121-1]
ENST00000409670; ENSP00000386315; ENSG00000042493. [P40121-1]
ENST00000409724; ENSP00000386965; ENSG00000042493. [P40121-1]
ENST00000409921; ENSP00000387063; ENSG00000042493. [P40121-2]
GeneIDi822.
KEGGihsa:822.
UCSCiuc002spm.3. human. [P40121-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94345 mRNA. Translation: AAA59570.1.
AK225374 mRNA. No translation available.
AC062037 Genomic DNA. Translation: AAY24128.1.
CH471053 Genomic DNA. Translation: EAW99517.1.
CH471053 Genomic DNA. Translation: EAW99518.1.
CH471053 Genomic DNA. Translation: EAW99519.1.
CH471053 Genomic DNA. Translation: EAW99520.1.
BC000728 mRNA. Translation: AAH00728.1.
BC014549 mRNA. Translation: AAH14549.1.
U12026 Genomic DNA. Translation: AAA92670.1.
CCDSiCCDS1974.1. [P40121-1]
CCDS58715.1. [P40121-2]
PIRiA43358.
RefSeqiNP_001243068.1. NM_001256139.1. [P40121-1]
NP_001243069.1. NM_001256140.1. [P40121-2]
NP_001307661.1. NM_001320732.1. [P40121-1]
NP_001307662.1. NM_001320733.1. [P40121-1]
NP_001738.2. NM_001747.3. [P40121-1]
XP_011531424.1. XM_011533122.1. [P40121-1]
XP_011531425.1. XM_011533123.1. [P40121-1]
UniGeneiHs.516155.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J72X-ray2.50A1-348[»]
1JHWX-ray2.80A1-348[»]
ProteinModelPortaliP40121.
SMRiP40121. Positions 11-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107272. 28 interactions.
DIPiDIP-61547N.
IntActiP40121. 4 interactions.
MINTiMINT-5232538.
STRINGi9606.ENSP00000263867.

PTM databases

iPTMnetiP40121.
PhosphoSiteiP40121.

Polymorphism and mutation databases

BioMutaiCAPG.
DMDMi313104088.

2D gel databases

REPRODUCTION-2DPAGEIPI00027341.

Proteomic databases

EPDiP40121.
MaxQBiP40121.
PaxDbiP40121.
PeptideAtlasiP40121.
PRIDEiP40121.
TopDownProteomicsiP40121-1. [P40121-1]

Protocols and materials databases

DNASUi822.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263867; ENSP00000263867; ENSG00000042493. [P40121-1]
ENST00000409670; ENSP00000386315; ENSG00000042493. [P40121-1]
ENST00000409724; ENSP00000386965; ENSG00000042493. [P40121-1]
ENST00000409921; ENSP00000387063; ENSG00000042493. [P40121-2]
GeneIDi822.
KEGGihsa:822.
UCSCiuc002spm.3. human. [P40121-1]

Organism-specific databases

CTDi822.
GeneCardsiCAPG.
HGNCiHGNC:1474. CAPG.
HPAiHPA018843.
HPA019080.
HPA019092.
MIMi153615. gene.
neXtProtiNX_P40121.
PharmGKBiPA26056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000235030.
HOVERGENiHBG001093.
InParanoidiP40121.
KOiK10368.
OMAiTERALNW.
PhylomeDBiP40121.
TreeFamiTF313468.

Miscellaneous databases

ChiTaRSiCAPG. human.
EvolutionaryTraceiP40121.
GeneWikiiCAPG.
GenomeRNAii822.
PROiP40121.
SOURCEiSearch...

Gene expression databases

BgeeiP40121.
CleanExiHS_CAPG.
ExpressionAtlasiP40121. baseline and differential.
GenevisibleiP40121. HS.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029917. CapG.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF13. PTHR11977:SF13. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of human macrophage capping protein cDNA. A unique member of the gelsolin/villin family expressed primarily in macrophages."
    Dabiri G.A., Young C.L., Rosenbloom J., Southwick F.S.
    J. Biol. Chem. 267:16545-16552(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 220-260 AND 320-343, VARIANT ARG-335.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ARG-335.
    Tissue: Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Tissue: Bone marrow and Placenta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-335.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-335.
    Tissue: Bone marrow and Placenta.
  6. "The human actin-regulatory protein cap G: gene structure and chromosome location."
    Mishra V.S., Henske E.P., Kwiatkowski D.J., Southwick F.S.
    Genomics 23:560-565(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172.
    Tissue: Placenta.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 307-335, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT ARG-335.
    Tissue: Fetal brain cortex.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Gain-of-function mutations conferring actin-severing activity to human macrophage cap G."
    Southwick F.S.
    J. Biol. Chem. 270:45-48(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-348.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 (VARIANT ARG-335), VARIANT [LARGE SCALE ANALYSIS] ARG-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPG_HUMAN
AccessioniPrimary (citable) accession number: P40121
Secondary accession number(s): B8ZZS7, D6W5K8, Q53SA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 30, 2010
Last modified: July 6, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Caution

This protein was originally thought to be a DNA-binding protein with a helix-loop-helix domain.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.