Reviewed, UniProtKB/Swiss-Prot O75391 (SPAG7_HUMAN)

Names and origin

Protein names

Recommended name:
    Sperm-associated antigen 7

Gene names

Name:

SPAG7

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	227 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)

Subcellular location	Nucleus Potential.
Tissue specificity	Detected in fetal brain. Ref.3
Sequence similarities	Contains 1 R3H domain.
Sequence caution	The sequence AAC39888.1 differs from that shown. Reason: Frameshift at position 227.

Ontologies

Keywords
Cellular component	Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT5	O95870	1	EBI-348464,EBI-348517

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 227

226

Sperm-associated antigen 7

PRO_0000072097

Regions

Domain

46 – 109

64

R3H

Motif

35 – 51

17

Nuclear localization signal Potential

Motif

122 – 139

18

Nuclear localization signal Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

114

1

Phosphoserine Ref.5

Modified residue

121

1

Phosphotyrosine Ref.4

Modified residue

158

1

Phosphoserine Ref.5

Modified residue

166

1

N6-acetyllysine Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

227

Helix Strand Turn

Details...

Helix

45 – 61

17

Beta strand

67 – 69

3

Helix

77 – 88

12

Beta strand

91 – 95

5

Beta strand

97 – 100

4

Beta strand

103 – 107

5

Helix

115 – 123

9

Sequences

	Sequence		Length	Mass (Da)
	O75391-1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 429566BE9B276EE4	FASTA	227	26,034
	10 20 30 40 50 60 MADLLGSILS SMEKPPSLGD QETRRKAREQ AARLKKLQEQ EKQQKVEFRK RMEKEVSDFI 70 80 90 100 110 120 QDSGQIKKKF QPMNKIERSI LHDVVEVAGL TSFSFGEDDD CRYVMIFKKE FAPSDEELDS 130 140 150 160 170 180 YRRGEEWDPQ KAEEKRKLKE LAQRQEEEAA QQGPVVVSPA SDYKDKYSHL IGKGAAKDAA 190 200 210 220 HMLQANKTYG CVPVANKRDT RSIEEAMNEI RAKKRLRQSG EELPPTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed: 9653160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[2]	"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: Uterus.
[3]	"Cloning and characterization of a fox sperm protein FSA-1." Beaton S., Cleary A., ten Have J., Bradley M.P. Reprod. Fertil. Dev. 6:761-770(1994) [PubMed: 7624517] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-121, MASS SPECTROMETRY.
[5]	"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-114 AND SER-158, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"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.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"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-166, MASS SPECTROMETRY.
[10]	"Solution structure of the R3H domain of human sperm-associated antigen 7." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 44-124.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF047437 mRNA. Translation: AAC39888.1. Frameshift.
BC011934 mRNA. Translation: AAH11934.1.

IPI

IPI00006863.

RefSeq

NP_004881.2.

UniGene

Hs.90436

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CPM	NMR	-	A	44-124	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O75391. 1 interaction.

STRING

O75391.

PTM databases

PhosphoSite

O75391.

Proteomic databases

PRIDE

O75391.

Genome annotation databases

Ensembl

ENST00000206020; ENSP00000206020; ENSG00000091640; Homo sapiens. [Genome view]

GeneID

9552.

KEGG

hsa:9552.

UCSC

uc002gad.1. human.

Organism-specific databases

CTD

9552.

GeneCards

GC17M004803.

HGNC

HGNC:11216. SPAG7.

HPA

HPA024032.

MIM

610056. gene.

PharmGKB

PA36052.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75391.

HOVERGEN

O75391.

OMA

ELPPTRH

OrthoDB

EOG9PK4V0

Gene expression databases

ArrayExpress

O75391.

Bgee

O75391.

CleanEx

HS_SPAG7.

Genevestigator

O75391.

GermOnline

ENSG00000091640. Homo sapiens.

Family and domain databases

InterPro

IPR001374. R3H_ss_bd.
IPR017330. Sperm-assoc_antigen_PAG7.
[Graphical view]

Pfam

PF01424. R3H. 1 hit.
[Graphical view]

PIRSF

PIRSF037943. Sperm-assoc_antigen_PAG7. 1 hit.

SMART

SM00393. R3H. 1 hit.
[Graphical view]

PROSITE

PS51061. R3H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

35821.

SOURCE

Search...

Entry information

Entry name

SPAG7_HUMAN

Accession

Primary (citable) accession number: O75391
Secondary accession number(s): Q96EU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	November 24, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.