P82979 (SARNP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SAP domain-containing ribonucleoprotein

Alternative name(s):
Cytokine-induced protein of 29 kDa
Nuclear protein Hcc-1
Proliferation-associated cytokine-inducible protein CIP29

Gene names

Name:	SARNP
Synonyms:	HCC1
ORF Names:	HSPC316

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Ref.8 Ref.9
Subunit structure	Interacts with DDX39A. Interacts with FUS. Ref.9
Subcellular location	Nucleus Ref.1.
Tissue specificity	Low expression in spleen, liver, pancreas, testis, thymus, heart, and kidney. Increased levels are seen in hepatocellular carcinoma and pancreatic adenocarcinoma. Ref.1
Induction	By EPO/erythropoietin.
Sequence similarities	Contains 1 SAP domain.
Sequence caution	The sequence AAF28994.1 differs from that shown. Reason: Frameshift at positions 134 and 149.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Translation regulation
Cellular component	Nucleus
Ligand	DNA-binding RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 210

209

SAP domain-containing ribonucleoprotein

PRO_0000083916

Regions

Domain

8 – 42

35

SAP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7 Ref.11

Modified residue

142

1

N6-acetyllysine Ref.12

Modified residue

163

1

Phosphoserine Ref.10

Experimental info

Sequence conflict

127

1

F → V in AAF28994. Ref.3

Sequence conflict

153 – 157

5

RAQRF → ELKDL in AAF28994. Ref.3

Sequence conflict

199 – 210

12

KKRKR…RFGIA → RRGKEQSALGLP in AAF28994. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

210

Helix Strand Turn

Details...

Turn

8 – 10

3

Helix

13 – 23

11

Helix

31 – 44

14

Sequences

	Sequence		Length	Mass (Da)
	P82979 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 96AFDD37EA328126	FASTA	210	23,671
	10 20 30 40 50 60 MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA NEEDVLGDET 70 80 90 100 110 120 EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT ERMQKRAERF NVPVSLESKK 130 140 150 160 170 180 AARAARFGIS SVPTKGLSSD NKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER 190 200 210 FGIVTSSAGT GTTEDTEAKK RKRAERFGIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An integrated approach in the discovery and characterization of a novel nuclear protein over-expressed in liver and pancreatic tumors." Choong M.L., Tan L.K., Lo S.L., Ren E.-C., Ou K.L., Ong S.-E., Liang R.C.M.Y., Seow T.K., Chung M.C.M. FEBS Lett. 496:109-116(2001) [PubMed: 11356193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119; 157-167 AND 181-199, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Liver.
[2]	"Cloning and characterization of a proliferation-associated cytokine-inducible protein, CIP29." Fukuda S., Wu D.W., Stark K., Pelus L.M. Biochem. Biophys. Res. Commun. 292:593-600(2002) [PubMed: 11922608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary cancer.
[3]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal brain.
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[7]	Bienvenut W.V., Potts A., Brablan J., Quadroni M. Submitted (JUL-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10 AND 127-135, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"Hcc-1 is a novel component of the nuclear matrix with growth inhibitory function." Leaw C.L., Ren E.C., Choong M.L. Cell. Mol. Life Sci. 61:2264-2273(2004) [PubMed: 15338056] [Abstract] Cited for: FUNCTION.
[9]	"Intracellular characterization of DDX39, a novel growth-associated RNA helicase." Sugiura T., Sakurai K., Nagano Y. Exp. Cell Res. 313:782-790(2007) [PubMed: 17196963] [Abstract] Cited for: FUNCTION, INTERACTION WITH DDX39A AND FUS.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, MASS SPECTROMETRY.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Solution structure of the SAP domain of human nuclear protein HCC-1." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 6-47.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ409089 Genomic DNA. Translation: CAC37950.1.
AF486281 mRNA. Translation: AAM09686.1.
AF161434 mRNA. Translation: AAF28994.1. Sequence problems.
AK290508 mRNA. Translation: BAF83197.1.
CH471054 Genomic DNA. Translation: EAW96838.1.
BC007099 mRNA. Translation: AAH07099.1.

IPI

IPI00014938.

PIR

JC7830.

RefSeq

NP_149073.1. NM_033082.3.

UniGene

Hs.505676.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DO1	NMR	-	A	6-46	[»]

ProteinModelPortal

P82979.

SMR

P82979. Positions 6-47.

ModBase

Search...

Protein-protein interaction databases

IntAct

P82979. 3 interactions.

STRING

P82979.

PTM databases

PhosphoSite

P82979.

Polymorphism databases

DMDM

18202440.

Proteomic databases

PRIDE

P82979.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336133; ENSP00000337632; ENSG00000205323.
ENST00000444631; ENSP00000392892; ENSG00000205323.

GeneID

84324.

KEGG

hsa:84324.

UCSC

uc001sht.1. human.

Organism-specific databases

CTD

84324.

GeneCards

GC12M056146.

H-InvDB

HIX0010706.

HGNC

HGNC:24432. SARNP.

HPA

HPA030902.
HPA030903.

MIM

610049. gene.

neXtProt

NX_P82979.

PharmGKB

PA165513309.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20287.

HOGENOM

HBG280797.

InParanoid

P82979.

OMA

VNMDKLK.

OrthoDB

EOG41RPWD.

PhylomeDB

P82979.

Gene expression databases

ArrayExpress

P82979.

Bgee

P82979.

Genevestigator

P82979.

GermOnline

ENSG00000205323. Homo sapiens.

Family and domain databases

InterPro

IPR003034. SAP_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.

Pfam

PF02037. SAP. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS50800. SAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

74056.

SOURCE

Search...

Entry information

Entry name

SARNP_HUMAN

Accession

Primary (citable) accession number: P82979
Secondary accession number(s): A8K393, Q9P066

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 102 of the entry and version 3 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.