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Q9NVU7

- SDA1_HUMAN

UniProt

Q9NVU7 - SDA1_HUMAN

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Protein

Protein SDA1 homolog

Gene

SDAD1

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

Functioni

Required for 60S pre-ribosomal subunits export to the cytoplasm.By similarity

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. protein transport Source: UniProtKB-KW
  3. ribosomal large subunit biogenesis Source: UniProtKB
  4. ribosomal large subunit export from nucleus Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Ribosome biogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SDA1 homolog
Alternative name(s):
Nucleolar protein 130
SDA1 domain-containing protein 1
Short name:
hSDA
Gene namesi
Name:SDAD1
Synonyms:NUC130
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:25537. SDAD1.

Subcellular locationi

Nucleusnucleolus 2 Publications

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134961441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Protein SDA1 homologPRO_0000287482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei232 – 2321Phosphoserine2 Publications
Modified residuei234 – 2341Phosphoserine2 Publications
Modified residuei236 – 2361Phosphoserine2 Publications
Modified residuei585 – 5851Phosphoserine6 Publications
Modified residuei595 – 5951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NVU7.
PaxDbiQ9NVU7.
PeptideAtlasiQ9NVU7.
PRIDEiQ9NVU7.

PTM databases

PhosphoSiteiQ9NVU7.

Expressioni

Tissue specificityi

Highly expressed in testis, kidney, spleen, brain and fetal tissues. Also expressed at lower level in heart, lung, liver, small intestine, ovary, uterus, mammary gland and placenta.2 Publications

Gene expression databases

BgeeiQ9NVU7.
CleanExiHS_SDAD1.
ExpressionAtlasiQ9NVU7. baseline and differential.
GenevestigatoriQ9NVU7.

Organism-specific databases

HPAiHPA035949.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TGIF1Q155831EBI-1043768,EBI-714215

Protein-protein interaction databases

BioGridi120456. 13 interactions.
IntActiQ9NVU7. 4 interactions.
MINTiMINT-4994740.
STRINGi9606.ENSP00000348596.

Structurei

3D structure databases

ProteinModelPortaliQ9NVU7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili253 – 31563Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SDA1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG292808.
GeneTreeiENSGT00390000010355.
HOGENOMiHOG000204601.
HOVERGENiHBG059552.
InParanoidiQ9NVU7.
KOiK14856.
OMAiQVAQCYP.
OrthoDBiEOG7QG43K.
PhylomeDBiQ9NVU7.
TreeFamiTF105727.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027312. Sda1.
IPR007949. SDA1_dom.
IPR012977. Uncharacterised_NUC130/133_N.
[Graphical view]
PANTHERiPTHR12730:SF0. PTHR12730:SF0. 1 hit.
PfamiPF08158. NUC130_3NT. 1 hit.
PF05285. SDA1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NVU7-1) [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
MSNRNNNKLP SNLPQLQNLI KRDPPAYIEE FLQQYNHYKS NVEIFKLQPN
60 70 80 90 100
KPSKELAELV MFMAQISHCY PEYLSNFPQE VKDLLSCNHT VLDPDLRMTF
110 120 130 140 150
CKALILLRNK NLINPSSLLE LFFELFRCHD KLLRKTLYTH IVTDIKNINA
160 170 180 190 200
KHKNNKVNVV LQNFMYTMLR DSNATAAKMS LDVMIELYRR NIWNDAKTVN
210 220 230 240 250
VITTACFSKV TKILVAALTF FLGKDEDEKQ DSDSESEDDG PTARDLLVQY
260 270 280 290 300
ATGKKSSKNK KKLEKAMKVL KKQKKKKKPE VFNFSAIHLI HDPQDFAEKL
310 320 330 340 350
LKQLECCKER FEVKMMLMNL ISRLVGIHEL FLFNFYPFLQ RFLQPHQREV
360 370 380 390 400
TKILLFAAQA SHHLVPPEII QSLLMTVANN FVTDKNSGEV MTVGINAIKE
410 420 430 440 450
ITARCPLAMT EELLQDLAQY KTHKDKNVMM SARTLIHLFR TLNPQMLQKK
460 470 480 490 500
FRGKPTEASI EARVQEYGEL DAKDYIPGAE VLEVEKEENA ENDEDGWEST
510 520 530 540 550
SLSEEEDADG EWIDVQHSSD EEQQEISKKL NSMPMEERKA KAAAISTSRV
560 570 580 590 600
LTQEDFQKIR MAQMRKELDA APGKSQKRKY IEIDSDEEPR GELLSLRDIE
610 620 630 640 650
RLHKKPKSDK ETRLATAMAG KTDRKEFVRK KTKTNPFSSS TNKEKKKQKN
660 670 680
FMMMRYSQNV RSKNKRSFRE KQLALRDALL KKRKRMK
Length:687
Mass (Da):79,871
Last modified:May 18, 2010 - v3
Checksum:iB01EE09383EA959C
GO
Isoform 2 (identifier: Q9NVU7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Note: No experimental confirmation available.

Show »
Length:590
Mass (Da):68,455
Checksum:i06780B225C43F041
GO

Sequence cautioni

The sequence AAI07896.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA91648.1 differs from that shown. Reason: Frameshift at position 53. Curated
The sequence BAB14177.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861E → G in CAH18368. (PubMed:17974005)Curated
Sequence conflicti288 – 2881H → L in BAA91648. (PubMed:14702039)Curated
Sequence conflicti319 – 3191N → S in CAH18368. (PubMed:17974005)Curated
Sequence conflicti396 – 3961N → S in CAH18368. (PubMed:17974005)Curated
Sequence conflicti617 – 6171A → S in BAB14177. (PubMed:14702039)Curated
Sequence conflicti634 – 6341T → A in CAH18368. (PubMed:17974005)Curated
Sequence conflicti651 – 6511F → L in CAH18368. (PubMed:17974005)Curated

Polymorphismi

Variations in SDAD1 may be a cause of susceptibility to seasonal allergic rhinitis (SAR). SAR is a common allergic disorder characterized by episodes of sneezing, rhinorrhea, and swelling of the nasal mucosa.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti258 – 2581K → Q.
Corresponds to variant rs15481 [ dbSNP | Ensembl ].
VAR_032312
Natural varianti490 – 4901A → D.
Corresponds to variant rs34627298 [ dbSNP | Ensembl ].
VAR_032313
Natural varianti575 – 5751S → C.2 Publications
Corresponds to variant rs2242471 [ dbSNP | Ensembl ].
VAR_032314
Natural varianti660 – 6601V → I.
Corresponds to variant rs17001276 [ dbSNP | Ensembl ].
VAR_032315

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_025505Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR749574 mRNA. Translation: CAH18368.1.
AC110615 Genomic DNA. No translation available.
AC112719 Genomic DNA. No translation available.
AC115628 Genomic DNA. No translation available.
BC054040 mRNA. Translation: AAH54040.1.
BC063797 mRNA. Translation: AAH63797.1.
BC107895 mRNA. Translation: AAI07896.1. Sequence problems.
AK001360 mRNA. Translation: BAA91648.1. Frameshift.
AK022683 mRNA. Translation: BAB14177.1. Different initiation.
AK024031 mRNA. Translation: BAB14790.1. Different initiation.
CCDSiCCDS3573.2. [Q9NVU7-1]
RefSeqiNP_001275912.1. NM_001288983.1.
NP_001275913.1. NM_001288984.1. [Q9NVU7-2]
NP_060585.2. NM_018115.3. [Q9NVU7-1]
XP_005263162.1. XM_005263105.2. [Q9NVU7-2]
UniGeneiHs.632604.

Genome annotation databases

EnsembliENST00000356260; ENSP00000348596; ENSG00000198301. [Q9NVU7-1]
GeneIDi55153.
KEGGihsa:55153.
UCSCiuc003hje.4. human. [Q9NVU7-1]

Polymorphism databases

DMDMi296452964.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR749574 mRNA. Translation: CAH18368.1 .
AC110615 Genomic DNA. No translation available.
AC112719 Genomic DNA. No translation available.
AC115628 Genomic DNA. No translation available.
BC054040 mRNA. Translation: AAH54040.1 .
BC063797 mRNA. Translation: AAH63797.1 .
BC107895 mRNA. Translation: AAI07896.1 . Sequence problems.
AK001360 mRNA. Translation: BAA91648.1 . Frameshift.
AK022683 mRNA. Translation: BAB14177.1 . Different initiation.
AK024031 mRNA. Translation: BAB14790.1 . Different initiation.
CCDSi CCDS3573.2. [Q9NVU7-1 ]
RefSeqi NP_001275912.1. NM_001288983.1.
NP_001275913.1. NM_001288984.1. [Q9NVU7-2 ]
NP_060585.2. NM_018115.3. [Q9NVU7-1 ]
XP_005263162.1. XM_005263105.2. [Q9NVU7-2 ]
UniGenei Hs.632604.

3D structure databases

ProteinModelPortali Q9NVU7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120456. 13 interactions.
IntActi Q9NVU7. 4 interactions.
MINTi MINT-4994740.
STRINGi 9606.ENSP00000348596.

PTM databases

PhosphoSitei Q9NVU7.

Polymorphism databases

DMDMi 296452964.

Proteomic databases

MaxQBi Q9NVU7.
PaxDbi Q9NVU7.
PeptideAtlasi Q9NVU7.
PRIDEi Q9NVU7.

Protocols and materials databases

DNASUi 55153.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356260 ; ENSP00000348596 ; ENSG00000198301 . [Q9NVU7-1 ]
GeneIDi 55153.
KEGGi hsa:55153.
UCSCi uc003hje.4. human. [Q9NVU7-1 ]

Organism-specific databases

CTDi 55153.
GeneCardsi GC04M076871.
H-InvDB HIX0025559.
HGNCi HGNC:25537. SDAD1.
HPAi HPA035949.
neXtProti NX_Q9NVU7.
PharmGKBi PA134961441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292808.
GeneTreei ENSGT00390000010355.
HOGENOMi HOG000204601.
HOVERGENi HBG059552.
InParanoidi Q9NVU7.
KOi K14856.
OMAi QVAQCYP.
OrthoDBi EOG7QG43K.
PhylomeDBi Q9NVU7.
TreeFami TF105727.

Miscellaneous databases

GeneWikii SDAD1.
GenomeRNAii 55153.
NextBioi 58895.
PROi Q9NVU7.

Gene expression databases

Bgeei Q9NVU7.
CleanExi HS_SDAD1.
ExpressionAtlasi Q9NVU7. baseline and differential.
Genevestigatori Q9NVU7.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR027312. Sda1.
IPR007949. SDA1_dom.
IPR012977. Uncharacterised_NUC130/133_N.
[Graphical view ]
PANTHERi PTHR12730:SF0. PTHR12730:SF0. 1 hit.
Pfami PF08158. NUC130_3NT. 1 hit.
PF05285. SDA1. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT CYS-575.
    Tissue: Rectum tumor.
  2. "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].
  3. "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] OF 1-277 (ISOFORM 1).
    Tissue: PNS and Uterus.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-687 (ISOFORM 1), VARIANT CYS-575.
  5. Cited for: SUBCELLULAR LOCATION.
  6. "Expression and localization studies of hSDA, the human ortholog of the yeast SDA1 gene."
    Babbio F., Farinacci M., Saracino F., Carbone M.L., Privitera E.
    Cell Cycle 3:486-490(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Identification and characterization of RNA sequences to which human PUMILIO-2 (PUM2) and deleted in Azoospermia-like (DAZL) bind."
    Fox M., Urano J., Reijo Pera R.A.
    Genomics 85:92-105(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Association of a haplotype block spanning SDAD1 gene and CXC chemokine genes with allergic rhinitis."
    Zhang J., Noguchi E., Migita O., Yokouchi Y., Nakayama J., Shibasaki M., Arinami T.
    J. Allergy Clin. Immunol. 115:548-554(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-234; SER-236 AND SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-232; SER-234; SER-236; SER-585 AND SER-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSDA1_HUMAN
AccessioniPrimary (citable) accession number: Q9NVU7
Secondary accession number(s): Q32Q11
, Q68D52, Q7Z5U4, Q9H831, Q9H9P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 96 of the entry and version 3 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

Miscellaneous

DAZL and PUM2 bind its 3'-UTR mRNA, suggesting that these proteins may regulate its translation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3