Q99729 (ROAA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein A/B
Short name=hnRNP A/B

Alternative name(s):
APOBEC1-binding protein 1
Short name=ABBP-1

Gene names

Name:	HNRNPAB
Synonyms:	ABBP1, HNRPAB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with APOBEC1. Ref.9
Subcellular location	Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9
Tissue specificity	Ubiquitous.
Post-translational modification	Dimethylation at Arg-322 is probably asymmetric.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.
Sequence caution	The sequence AAC50956.1 differs from that shown. Reason: Frameshift at positions 296, 307 and 330. Isoform 4: The sequence AAA36575.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: HGNC positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: HGNC nucleus Inferred from sequence or structural similarity. Source: HGNC ribonucleoprotein complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	mRNA binding Traceable author statement Ref.2. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99729-1)

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.

Isoform 2 (identifier: Q99729-2)

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

Isoform 3 (identifier: Q99729-3)

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.

Isoform 4 (identifier: Q99729-4)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Heterogeneous nuclear ribonucleoprotein A/B

PRO_0000081492

Regions

Domain

69 – 154

86

RRM 1

Domain

153 – 233

81

RRM 2

Compositional bias

241 – 324

84

Gly-rich

Amino acid modifications

Modified residue

77

1

Phosphoserine By similarity

Modified residue

242

1

Phosphoserine Ref.8 Ref.11 Ref.13 Ref.15

Modified residue

245

1

Dimethylated arginine; alternate Ref.6

Modified residue

245

1

Omega-N-methylarginine; alternate Ref.6

Modified residue

322

1

Dimethylated arginine Ref.7

Natural variations

Alternative sequence

26 – 32

7

ASRGRGW → GESPAGAG in isoform 2, isoform 3 and isoform 4.

VSP_007826

Alternative sequence

164 – 165

2

SP → A in isoform 2 and isoform 3.

VSP_007828

Alternative sequence

264 – 310

47

Missing in isoform 3 and isoform 4.

VSP_007829

Secondary structure

1

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332

Helix Strand Turn

Details...

Beta strand

70 – 74

5

Helix

82 – 89

8

Turn

90 – 92

3

Beta strand

95 – 102

8

Turn

104 – 106

3

Beta strand

109 – 119

11

Helix

121 – 128

8

Beta strand

132 – 134

3

Beta strand

137 – 143

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: F824A7E08D15268A	FASTA	332	36,225
	10 20 30 40 50 60 MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN QNGAEGDQIN 70 80 90 100 110 120 ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI KMDPNTGRSR GFGFILFKDA 130 140 150 160 170 180 ASVEKVLDQK EHRLDGRVID PKKAMAMKKD PVKKIFVGGL NPESPTEEKI REYFGEFGEI 190 200 210 220 230 240 EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY 250 260 270 280 290 300 GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY 310 320 330 YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
	Isoform 2 [UniParc]. Checksum: F710B690D495500D	FASTA	332	35,968
	10 20 30 40 50 60 MSEAGEEQPM ETTGATENGH EAVPEGESPA GAGTGAAAGA GGATAAPPSG NQNGAEGDQI 70 80 90 100 110 120 NASKNEEDAG KMFVGGLSWD TSKKDLKDYF TKFGEVVDCT IKMDPNTGRS RGFGFILFKD 130 140 150 160 170 180 AASVEKVLDQ KEHRLDGRVI DPKKAMAMKK DPVKKIFVGG LNPEATEEKI REYFGEFGEI 190 200 210 220 230 240 EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY 250 260 270 280 290 300 GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY 310 320 330 YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
	Isoform 3 [UniParc]. Checksum: 3E4F386C2F5B9705	FASTA	285	30,588
	10 20 30 40 50 60 MSEAGEEQPM ETTGATENGH EAVPEGESPA GAGTGAAAGA GGATAAPPSG NQNGAEGDQI 70 80 90 100 110 120 NASKNEEDAG KMFVGGLSWD TSKKDLKDYF TKFGEVVDCT IKMDPNTGRS RGFGFILFKD 130 140 150 160 170 180 AASVEKVLDQ KEHRLDGRVI DPKKAMAMKK DPVKKIFVGG LNPEATEEKI REYFGEFGEI 190 200 210 220 230 240 EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY 250 260 270 280 GSGGRGNRNR GNRGSGGGGG GGGQGSTNYG KSQRRGGHQN NYKPY
	Isoform 4 [UniParc]. Checksum: AA24BA3F6A0BAD62	FASTA	286	30,701
	10 20 30 40 50 60 MSEAGEEQPM ETTGATENGH EAVPEGESPA GAGTGAAAGA GGATAAPPSG NQNGAEGDQI 70 80 90 100 110 120 NASKNEEDAG KMFVGGLSWD TSKKDLKDYF TKFGEVVDCT IKMDPNTGRS RGFGFILFKD 130 140 150 160 170 180 AASVEKVLDQ KEHRLDGRVI DPKKAMAMKK DPVKKIFVGG LNPESPTEEK IREYFGEFGE 190 200 210 220 230 240 IEAIELPMDP KLNKRRGFVF ITFKEEEPVK KVLEKKFHTV SGSKCEIKVA QPKEVYQQQQ 250 260 270 280 YGSGGRGNRN RGNRGSGGGG GGGGQGSTNY GKSQRRGGHQ NNYKPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1991) [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(1997) [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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Testis.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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(2004) [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 (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248, METHYLATION AT ARG-245, 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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, MASS SPECTROMETRY. 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(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] 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(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), MASS SPECTROMETRY.
[13]	"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-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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-242, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 (ISOFORM 4), MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00106509.
IPI00329355.
IPI00334587.
IPI00334713.

PIR

S17563.

RefSeq

NP_004490.2. NM_004499.3.
NP_112556.2. NM_031266.2.

UniGene

Hs.591731.
Hs.715055.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3S7R	X-ray	2.15	A/B	59-144	[»]

ProteinModelPortal

Q99729.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99729. 24 interactions.

MINT

MINT-4537784.

STRING

9606.ENSP00000351108.

PTM databases

PhosphoSite

Q99729.

Polymorphism databases

DMDM

158523286.

2D gel databases

SWISS-2DPAGE

Q99729.

Proteomic databases

PaxDb

Q99729.

PRIDE

Q99729.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355836; ENSP00000348093; ENSG00000197451.
ENST00000358344; ENSP00000351108; ENSG00000197451.
ENST00000504898; ENSP00000425031; ENSG00000197451.
ENST00000506259; ENSP00000427465; ENSG00000197451.

GeneID

3182.

KEGG

hsa:3182.

UCSC

uc003miu.3. human.
uc003miv.3. human.

Organism-specific databases

CTD

3182.

GeneCards

GC05P177631.

HGNC

HGNC:5034. HNRNPAB.

HPA

HPA046688.

MIM

602688. gene.

neXtProt

NX_Q99729.

PharmGKB

PA162391196.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000234441.

HOVERGEN

HBG002295.

InParanoid

Q99729.

KO

K13044.

OMA

FILFKDP.

OrthoDB

EOG42BX9K.

Gene expression databases

ArrayExpress

Q99729.

Bgee

Q99729.

CleanEx

HS_HNRNPAB.

Genevestigator

Q99729.

GermOnline

ENSG00000197451. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPAB. human.

EvolutionaryTrace

Q99729.

GenomeRNAi

3182.

NextBio

12628.

SOURCE

Search...

Entry information

Entry name

ROAA_HUMAN

Accession

Primary (citable) accession number: Q99729
Secondary accession number(s): B3KNN5 , D3DWP7, Q04150, Q8N7U3, Q9BQ99

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.