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Protein

Probable global transcription activator SNF2L1

Gene

SMARCA1

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

Functioni

Energy-transducing component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes. Both complexes facilitate the perturbation of chromatin structure in an ATP-dependent manner. Potentiates neurite outgrowth. May be involved in brain development by regulating En-1 and En-2 expression. May be involved in the development of luteal cells.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi208 – 2158ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • annealing helicase activity Source: UniProtKB
  • ATPase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: InterPro
  • helicase activity Source: ProtInc

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: MGI
  • brain development Source: HGNC
  • chromatin remodeling Source: HGNC
  • DNA strand renaturation Source: GOC
  • neuron differentiation Source: HGNC
  • positive regulation of transcription, DNA-templated Source: HGNC
  • transcription, DNA-templated Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable global transcription activator SNF2L1 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent helicase SMARCA1
Nucleosome-remodeling factor subunit SNF2L
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1
Gene namesi
Name:SMARCA1
Synonyms:SNF2L, SNF2L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11097. SMARCA1.

Subcellular locationi

GO - Cellular componenti

  • CERF complex Source: MGI
  • nucleus Source: HGNC
  • NURF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141K → R: No effect on neurite outgrowth. 1 Publication

Organism-specific databases

PharmGKBiPA35947.

Polymorphism and mutation databases

DMDMi115311627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10541054Probable global transcription activator SNF2L1PRO_0000074351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei119 – 1191PhosphoserineCombined sources
Cross-linki728 – 728Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei954 – 9541Phosphotyrosine1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP28370.
MaxQBiP28370.
PaxDbiP28370.
PRIDEiP28370.

PTM databases

iPTMnetiP28370.
PhosphoSiteiP28370.

Expressioni

Gene expression databases

BgeeiP28370.
CleanExiHS_SMARCA1.
ExpressionAtlasiP28370. baseline and differential.
GenevisibleiP28370. HS.

Organism-specific databases

HPAiHPA003335.

Interactioni

Subunit structurei

Part of the nucleosome-remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Part of the CECR2-containing-remodeling factor (CERF) complex which contains CECR2 and SMARCA1. Interacts with PRLR.3 Publications

Protein-protein interaction databases

BioGridi112478. 32 interactions.
DIPiDIP-57685N.
IntActiP28370. 15 interactions.
MINTiMINT-2802155.
STRINGi9606.ENSP00000360163.

Structurei

3D structure databases

ProteinModelPortaliP28370.
SMRiP28370. Positions 758-1036.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 360166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini490 – 653164Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini855 – 90753SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini958 – 102265SANT 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi311 – 3144DEAH box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0385. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128349.
HOVERGENiHBG056329.
InParanoidiP28370.
OrthoDBiEOG71K625.
PhylomeDBiP28370.
TreeFamiTF300674.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 3 hits.
PfamiPF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P28370-1) [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
MEQDTAAVAA TVAAADATAT IVVIEDEQPG PSTSQEEGAA AAATEATAAT
60 70 80 90 100
EKGEKKKEKN VSSFQLKLAA KAPKSEKEMD PEYEEKMKAD RAKRFEFLLK
110 120 130 140 150
QTELFAHFIQ PSAQKSPTSP LNMKLGRPRI KKDEKQSLIS AGDYRHRRTE
160 170 180 190 200
QEEDEELLSE SRKTSNVCIR FEVSPSYVKG GPLRDYQIRG LNWLISLYEN
210 220 230 240 250
GVNGILADEM GLGKTLQTIA LLGYLKHYRN IPGPHMVLVP KSTLHNWMNE
260 270 280 290 300
FKRWVPSLRV ICFVGDKDAR AAFIRDEMMP GEWDVCVTSY EMVIKEKSVF
310 320 330 340 350
KKFHWRYLVI DEAHRIKNEK SKLSEIVREF KSTNRLLLTG TPLQNNLHEL
360 370 380 390 400
WALLNFLLPD VFNSADDFDS WFDTKNCLGD QKLVERLHAV LKPFLLRRIK
410 420 430 440 450
TDVEKSLPPK KEIKIYLGLS KMQREWYTKI LMKDIDVLNS SGKMDKMRLL
460 470 480 490 500
NILMQLRKCC NHPYLFDGAE PGPPYTTDEH IVSNSGKMVV LDKLLAKLKE
510 520 530 540 550
QGSRVLIFSQ MTRLLDILED YCMWRGYEYC RLDGQTPHEE REDKFLEVEF
560 570 580 590 600
LGQREAIEAF NAPNSSKFIF MLSTRAGGLG INLASADVVI LYDSDWNPQV
610 620 630 640 650
DLQAMDRAHR IGQKKPVRVF RLITDNTVEE RIVERAEIKL RLDSIVIQQG
660 670 680 690 700
RLIDQQSNKL AKEEMLQMIR HGATHVFASK ESELTDEDIT TILERGEKKT
710 720 730 740 750
AEMNERLQKM GESSLRNFRM DIEQSLYKFE GEDYREKQKL GMVEWIEPPK
760 770 780 790 800
RERKANYAVD AYFREALRVS EPKIPKAPRP PKQPNVQDFQ FFPPRLFELL
810 820 830 840 850
EKEILYYRKT IGYKVPRNPD IPNPALAQRE EQKKIDGAEP LTPEETEEKE
860 870 880 890 900
KLLTQGFTNW TKRDFNQFIK ANEKYGRDDI DNIAREVEGK SPEEVMEYSA
910 920 930 940 950
VFWERCNELQ DIEKIMAQIE RGEARIQRRI SIKKALDAKI ARYKAPFHQL
960 970 980 990 1000
RIQYGTSKGK NYTEEEDRFL ICMLHKMGFD RENVYEELRQ CVRNAPQFRF
1010 1020 1030 1040 1050
DWFIKSRTAM EFQRRCNTLI SLIEKENMEI EERERAEKKK RATKTPMVKF

SAFS
Note: Inactive as an ATPase and a chromatin remodeler due to the presence of exon 13, but retains its ability to incorporate into the NURF complex. Predominant in non neuronal tissues.
Length:1,054
Mass (Da):122,605
Last modified:September 19, 2006 - v2
Checksum:iD3FBFCA177F7D3C0
GO
Isoform 2 (identifier: P28370-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     543-554: Missing.

Show »
Length:1,042
Mass (Da):121,142
Checksum:iC6F6F9EF9C9F1C60
GO

Sequence cautioni

The sequence AAA80560.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti656 – 6561Q → R.1 Publication
Corresponds to variant rs1134838 [ dbSNP | Ensembl ].
VAR_001242

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei543 – 55412Missing in isoform 2. 1 PublicationVSP_020406Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88163 mRNA. Translation: AAA80559.1.
M89907 mRNA. Translation: AAA80560.1. Different initiation.
AL138745, AL022577 Genomic DNA. Translation: CAI42612.1.
AL138745, AL022577 Genomic DNA. Translation: CAI42613.1.
AL022577, AL138745 Genomic DNA. Translation: CAI42682.1.
AL022577, AL138745 Genomic DNA. Translation: CAI42683.1.
BC117447 mRNA. Translation: AAI17448.1.
CCDSiCCDS14612.1. [P28370-1]
PIRiS35457.
S35458.
RefSeqiNP_001269804.1. NM_001282875.1.
NP_003060.2. NM_003069.4. [P28370-1]
XP_005262518.1. XM_005262461.1. [P28370-1]
XP_006724845.1. XM_006724782.1. [P28370-2]
UniGeneiHs.152292.

Genome annotation databases

EnsembliENST00000371122; ENSP00000360163; ENSG00000102038. [P28370-1]
GeneIDi6594.
UCSCiuc004eun.6. human. [P28370-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88163 mRNA. Translation: AAA80559.1.
M89907 mRNA. Translation: AAA80560.1. Different initiation.
AL138745, AL022577 Genomic DNA. Translation: CAI42612.1.
AL138745, AL022577 Genomic DNA. Translation: CAI42613.1.
AL022577, AL138745 Genomic DNA. Translation: CAI42682.1.
AL022577, AL138745 Genomic DNA. Translation: CAI42683.1.
BC117447 mRNA. Translation: AAI17448.1.
CCDSiCCDS14612.1. [P28370-1]
PIRiS35457.
S35458.
RefSeqiNP_001269804.1. NM_001282875.1.
NP_003060.2. NM_003069.4. [P28370-1]
XP_005262518.1. XM_005262461.1. [P28370-1]
XP_006724845.1. XM_006724782.1. [P28370-2]
UniGeneiHs.152292.

3D structure databases

ProteinModelPortaliP28370.
SMRiP28370. Positions 758-1036.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112478. 32 interactions.
DIPiDIP-57685N.
IntActiP28370. 15 interactions.
MINTiMINT-2802155.
STRINGi9606.ENSP00000360163.

PTM databases

iPTMnetiP28370.
PhosphoSiteiP28370.

Polymorphism and mutation databases

DMDMi115311627.

Proteomic databases

EPDiP28370.
MaxQBiP28370.
PaxDbiP28370.
PRIDEiP28370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371122; ENSP00000360163; ENSG00000102038. [P28370-1]
GeneIDi6594.
UCSCiuc004eun.6. human. [P28370-1]

Organism-specific databases

CTDi6594.
GeneCardsiSMARCA1.
HGNCiHGNC:11097. SMARCA1.
HPAiHPA003335.
MIMi300012. gene.
neXtProtiNX_P28370.
PharmGKBiPA35947.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0385. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128349.
HOVERGENiHBG056329.
InParanoidiP28370.
OrthoDBiEOG71K625.
PhylomeDBiP28370.
TreeFamiTF300674.

Miscellaneous databases

ChiTaRSiSMARCA1. human.
GeneWikiiSMARCA1.
GenomeRNAii6594.
NextBioi25645.
PROiP28370.
SOURCEiSearch...

Gene expression databases

BgeeiP28370.
CleanExiHS_SMARCA1.
ExpressionAtlasiP28370. baseline and differential.
GenevisibleiP28370. HS.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR029915. ISWI.
IPR015194. ISWI_HAND-dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR015195. SLIDE.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF691. PTHR10799:SF691. 3 hits.
PfamiPF13892. DBINO. 1 hit.
PF09110. HAND. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09111. SLIDE. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF101224. SSF101224. 1 hit.
SSF46689. SSF46689. 2 hits.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human and bovine homologs of SNF2/SWI2: a global activator of transcription in yeast S. cerevisiae."
    Okabe I., Bailey L.C., Attree O.F., Perkel J.M., Nelson D.L., Nussbaum R.L.
    Nucleic Acids Res. 20:4649-4655(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-656.
    Tissue: Kidney.
  2. "A tissue-specific, naturally occurring human SNF2L variant inactivates chromatin remodeling."
    Barak O., Lazzaro M.A., Cooch N.S., Picketts D.J., Shiekhattar R.
    J. Biol. Chem. 279:45130-45138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Lung.
  5. "Identification of the phosphotyrosine proteome from thrombin activated platelets."
    Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
    Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-954.
  6. "Isolation of human NURF: a regulator of Engrailed gene expression."
    Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R.
    EMBO J. 22:6089-6100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NURF COMPLEX, MUTAGENESIS OF LYS-214, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "CECR2, a protein involved in neurulation, forms a novel chromatin remodeling complex with SNF2L."
    Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S., Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.
    Hum. Mol. Genet. 14:513-524(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE CERF COMPLEX.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The imitation switch protein SNF2L regulates steroidogenic acute regulatory protein expression during terminal differentiation of ovarian granulosa cells."
    Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C., Picketts D.J.
    Mol. Endocrinol. 20:2406-2417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRLR.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSMCA1_HUMAN
AccessioniPrimary (citable) accession number: P28370
Secondary accession number(s): Q5JV41, Q5JV42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 19, 2006
Last modified: May 11, 2016
This is version 171 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.