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Protein

Heterogeneous nuclear ribonucleoprotein A/B

Gene

HNRNPAB

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

Functioni

Binds single-stranded RNA. Has a high affinity for G-rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site.

GO - Molecular functioni

  1. mRNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: ProtInc

GO - Biological processi

  1. epithelial to mesenchymal transition Source: HGNC
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of transcription, DNA-templated Source: HGNC
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein A/B
Short name:
hnRNP A/B
Alternative name(s):
APOBEC1-binding protein 1
Short name:
ABBP-1
Gene namesi
Name:HNRNPAB
Synonyms:ABBP1, HNRPAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5034. HNRNPAB.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleoplasm Source: HPA
  3. nucleus Source: HGNC
  4. ribonucleoprotein complex Source: UniProtKB
  5. RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Heterogeneous nuclear ribonucleoprotein A/BPRO_0000081492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei215 – 2151N6-acetyllysineBy similarity
Modified residuei242 – 2421Phosphoserine4 Publications
Modified residuei245 – 2451Dimethylated arginine; alternate1 Publication
Modified residuei245 – 2451Omega-N-methylarginine; alternate1 Publication
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei322 – 3221Dimethylated arginine1 Publication

Post-translational modificationi

Dimethylation at Arg-322 is probably asymmetric.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ99729.
PaxDbiQ99729.
PRIDEiQ99729.

2D gel databases

SWISS-2DPAGEQ99729.

PTM databases

PhosphoSiteiQ99729.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ99729.
CleanExiHS_HNRNPAB.
ExpressionAtlasiQ99729. baseline and differential.
GenevestigatoriQ99729.

Organism-specific databases

HPAiHPA046688.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APOBEC1.1 Publication

Protein-protein interaction databases

BioGridi109423. 76 interactions.
DIPiDIP-50394N.
IntActiQ99729. 33 interactions.
MINTiMINT-4537784.
STRINGi9606.ENSP00000351108.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi70 – 745Combined sources
Helixi82 – 898Combined sources
Turni90 – 923Combined sources
Beta strandi95 – 1028Combined sources
Turni104 – 1063Combined sources
Beta strandi109 – 11911Combined sources
Helixi121 – 1288Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1437Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S7RX-ray2.15A/B59-144[»]
ProteinModelPortaliQ99729.
SMRiQ99729. Positions 24-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99729.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 15486RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 23381RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi241 – 32484Gly-richAdd
BLAST

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ99729.
KOiK13044.
OMAiFIMSPLE.
OrthoDBiEOG715Q6V.
PhylomeDBiQ99729.
TreeFamiTF314808.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99729-1) [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
MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN
60 70 80 90 100
QNGAEGDQIN ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI
110 120 130 140 150
KMDPNTGRSR GFGFILFKDA ASVEKVLDQK EHRLDGRVID PKKAMAMKKD
160 170 180 190 200
PVKKIFVGGL NPESPTEEKI REYFGEFGEI EAIELPMDPK LNKRRGFVFI
210 220 230 240 250
TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY GSGGRGNRNR
260 270 280 290 300
GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY
310 320 330
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
Length:332
Mass (Da):36,225
Last modified:September 10, 2007 - v2
Checksum:iF824A7E08D15268A
GO
Isoform 2 (identifier: Q99729-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     164-165: SP → A

Show »
Length:332
Mass (Da):35,968
Checksum:iF710B690D495500D
GO
Isoform 3 (identifier: Q99729-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     164-165: SP → A
     264-310: Missing.

Note: Contains a N6-acetyllysine at position 271. Contains a phosphoserine at position 255.3 Publications

Show »
Length:285
Mass (Da):30,588
Checksum:i3E4F386C2F5B9705
GO
Isoform 4 (identifier: Q99729-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-32: ASRGRGW → GESPAGAG
     264-310: Missing.

Note: Contains a N6-acetyllysine at position 272. Contains a phosphoserine at position 256.Curated3 Publications

Show »
Length:286
Mass (Da):30,701
Checksum:iAA24BA3F6A0BAD62
GO

Sequence cautioni

Isoform 4 : The sequence AAA36575.1 differs from that shown. Reason: Frameshift at several positions. Curated3 Publications
The sequence AAC50956.1 differs from that shown. Reason: Frameshift at positions 296, 307 and 330. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 327ASRGRGW → GESPAGAG in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_007826
Alternative sequencei164 – 1652SP → A in isoform 2 and isoform 3. 2 PublicationsVSP_007828
Alternative sequencei264 – 31047Missing in isoform 3 and isoform 4. 3 PublicationsVSP_007829Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65028 mRNA. Translation: AAA36575.1. Frameshift.
U76713 mRNA. Translation: AAC50956.1. Frameshift.
AK054600 mRNA. Translation: BAG51397.1.
AK097657 mRNA. Translation: BAC05134.1.
CH471165 Genomic DNA. Translation: EAW53843.1.
CH471165 Genomic DNA. Translation: EAW53844.1.
CH471165 Genomic DNA. Translation: EAW53845.1.
BC001616 mRNA. Translation: AAH01616.1.
BC002625 mRNA. Translation: AAH02625.1.
BC004561 mRNA. Translation: AAH04561.1.
BC009359 mRNA. Translation: AAH09359.1.
BC036708 mRNA. Translation: AAH36708.1.
CCDSiCCDS34309.1. [Q99729-2]
CCDS34310.1. [Q99729-3]
PIRiS17563.
RefSeqiNP_004490.2. NM_004499.3. [Q99729-3]
NP_112556.2. NM_031266.2. [Q99729-2]
UniGeneiHs.591731.
Hs.715055.

Genome annotation databases

EnsembliENST00000355836; ENSP00000348093; ENSG00000197451. [Q99729-3]
ENST00000358344; ENSP00000351108; ENSG00000197451. [Q99729-2]
ENST00000504898; ENSP00000425031; ENSG00000197451. [Q99729-2]
ENST00000506259; ENSP00000427465; ENSG00000197451. [Q99729-3]
GeneIDi3182.
KEGGihsa:3182.
UCSCiuc003miu.3. human. [Q99729-2]
uc003miv.3. human. [Q99729-3]

Polymorphism databases

DMDMi158523286.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65028 mRNA. Translation: AAA36575.1. Frameshift.
U76713 mRNA. Translation: AAC50956.1. Frameshift.
AK054600 mRNA. Translation: BAG51397.1.
AK097657 mRNA. Translation: BAC05134.1.
CH471165 Genomic DNA. Translation: EAW53843.1.
CH471165 Genomic DNA. Translation: EAW53844.1.
CH471165 Genomic DNA. Translation: EAW53845.1.
BC001616 mRNA. Translation: AAH01616.1.
BC002625 mRNA. Translation: AAH02625.1.
BC004561 mRNA. Translation: AAH04561.1.
BC009359 mRNA. Translation: AAH09359.1.
BC036708 mRNA. Translation: AAH36708.1.
CCDSiCCDS34309.1. [Q99729-2]
CCDS34310.1. [Q99729-3]
PIRiS17563.
RefSeqiNP_004490.2. NM_004499.3. [Q99729-3]
NP_112556.2. NM_031266.2. [Q99729-2]
UniGeneiHs.591731.
Hs.715055.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S7RX-ray2.15A/B59-144[»]
ProteinModelPortaliQ99729.
SMRiQ99729. Positions 24-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109423. 76 interactions.
DIPiDIP-50394N.
IntActiQ99729. 33 interactions.
MINTiMINT-4537784.
STRINGi9606.ENSP00000351108.

PTM databases

PhosphoSiteiQ99729.

Polymorphism databases

DMDMi158523286.

2D gel databases

SWISS-2DPAGEQ99729.

Proteomic databases

MaxQBiQ99729.
PaxDbiQ99729.
PRIDEiQ99729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355836; ENSP00000348093; ENSG00000197451. [Q99729-3]
ENST00000358344; ENSP00000351108; ENSG00000197451. [Q99729-2]
ENST00000504898; ENSP00000425031; ENSG00000197451. [Q99729-2]
ENST00000506259; ENSP00000427465; ENSG00000197451. [Q99729-3]
GeneIDi3182.
KEGGihsa:3182.
UCSCiuc003miu.3. human. [Q99729-2]
uc003miv.3. human. [Q99729-3]

Organism-specific databases

CTDi3182.
GeneCardsiGC05P177631.
HGNCiHGNC:5034. HNRNPAB.
HPAiHPA046688.
MIMi602688. gene.
neXtProtiNX_Q99729.
PharmGKBiPA162391196.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ99729.
KOiK13044.
OMAiFIMSPLE.
OrthoDBiEOG715Q6V.
PhylomeDBiQ99729.
TreeFamiTF314808.

Miscellaneous databases

ChiTaRSiHNRNPAB. human.
EvolutionaryTraceiQ99729.
GeneWikiiHNRPAB.
GenomeRNAii3182.
NextBioi12628.
PROiQ99729.
SOURCEiSearch...

Gene expression databases

BgeeiQ99729.
CleanExiHS_HNRNPAB.
ExpressionAtlasiQ99729. baseline and differential.
GenevestigatoriQ99729.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a human type A/B hnRNP protein."
    Khan F., Jaiswal A.K., Szer W.
    FEBS Lett. 290:159-161(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  2. "Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing."
    Lau P.P., Zhu H.J., Nakamuta M., Chan L.
    J. Biol. Chem. 272:1452-1455(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Placenta, Skin and Uterus.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248, METHYLATION AT ARG-245, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
    Ong S.E., Mittler G., Mann M.
    Nat. Methods 1:119-126(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  10. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), 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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiROAA_HUMAN
AccessioniPrimary (citable) accession number: Q99729
Secondary accession number(s): B3KNN5
, D3DWP7, Q04150, Q8N7U3, Q9BQ99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 18, 2003
Last sequence update: September 10, 2007
Last modified: March 3, 2015
This is version 141 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

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

Documents

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

External Data

Dasty 3

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 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.