Reviewed, UniProtKB/Swiss-Prot P82979 (HCC1_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	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	May have nucleic acid binding capability that may participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis.
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 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
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
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 Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT1	Q13838	1	EBI-347495,EBI-348622

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 210

209

Nuclear protein Hcc-1

PRO_0000083916

Regions

Domain

8 – 42

35

SAP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

163

1

Phosphoserine Ref.6

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)
	P82979-1 [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]	"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.
[5]	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.
[6]	"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.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

IPI

IPI00014938.

PIR

JC7830.

RefSeq

NP_149073.1.

UniGene

Hs.505676

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P82979. 2 interactions.

PTM databases

PhosphoSite

P82979.

Proteomic databases

PRIDE

P82979.

Genome annotation databases

Ensembl

ENSG00000205323. Homo sapiens. [Contig view]

GeneID

84324.

KEGG

hsa:84324.

Organism-specific databases

GeneCards

GC12M054437.

H-InvDB

HIX0010705.

MIM

610049. gene.

Phylogenomic databases

HOGENOM

P82979.

HOVERGEN

P82979.

OMA

P82979. XEEEANE.

Gene expression databases

ArrayExpress

P82979.

Bgee

P82979.

GermOnline

ENSG00000205323. Homo sapiens.

Family and domain databases

InterPro

IPR003034. SAP_DNA_bd.
[Graphical view]

Pfam

PF02037. SAP. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS50800. SAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

74056.

SOURCE

Search...

Entry information

Entry name

HCC1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)