Reviewed, UniProtKB/Swiss-Prot P78324 (SHPS1_HUMAN)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein phosphatase non-receptor type substrate 1
      Short name=SHP substrate 1
      Short name=SHPS-1
Alternative name(s):
    Inhibitory receptor SHPS-1
    Signal-regulatory protein alpha-1
      Short name=Sirp-alpha-1
    Sirp-alpha-2
    Sirp-alpha-3
    MyD-1 antigen
    Brain Ig-like molecule with tyrosine-based activation motifs
      Short name=Bit
    Macrophage fusion receptor
    p84
    CD172 antigen-like family member A
    CD_antigen=CD172a

Gene names

Name:	SIRPA
Synonyms:	BIT, MFR, MYD1, PTPNS1, SHPS1, SIRP

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	503 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	Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function By similarity. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells.
Subunit structure	Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds FGR By similarity. Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB. Binds PTK2B.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Ubiquitous. Highly expressed in brain. Detected on myeloid cells, but not T-cells. Detected at lower levels in heart, placenta, lung, testis, ovary, colon, liver, small intestine, prostate, spleen, kidney, skeletal muscle and pancreas.
Post-translational modification	N-glycosylated. Ref.2 Ref.11 Phosphorylated on tyrosine residues in response to stimulation with EGF, growth hormone, insulin and PDGF. Dephosphorylated by PTPN11. Ref.2 Ref.9
Sequence similarities	Contains 2 Ig-like C1-type (immunoglobulin-like) domains. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat SH3-binding Signal Transmembrane
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell adhesion Ref.1 Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78324-1)

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: P78324-2)

The sequence of this isoform differs from the canonical sequence as follows:
     421-421: Q → QVQSL

Note: No experimental confirmation available.

Isoform 3 (identifier: P78324-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 503

473

Tyrosine-protein phosphatase non-receptor type substrate 1

PRO_0000014941

Regions

Topological domain

27 – 372

346

Extracellular Potential

Transmembrane

373 – 393

21

Potential

Topological domain

394 – 503

110

Cytoplasmic Potential

Domain

32 – 137

106

Ig-like V-type

Domain

147 – 246

100

Ig-like C1-type 1

Domain

253 – 347

95

Ig-like C1-type 2

Motif

428 – 431

4

SH2-binding Potential

Motif

438 – 443

6

SH3-binding Potential

Motif

452 – 455

4

SH2-binding Potential

Motif

469 – 472

4

SH2-binding Potential

Motif

495 – 498

4

SH2-binding Potential

Amino acid modifications

Modified residue

428

1

Phosphotyrosine; by Tyr-kinases Potential

Modified residue

452

1

Phosphotyrosine; by Tyr-kinases Potential

Modified residue

469

1

Phosphotyrosine; by Tyr-kinases By similarity

Modified residue

495

1

Phosphotyrosine; by Tyr-kinases By similarity

Glycosylation

244

1

N-linked (GlcNAc...) Ref.11

Glycosylation

269

1

N-linked (GlcNAc...)

Glycosylation

291

1

N-linked (GlcNAc...)

Glycosylation

318

1

N-linked (GlcNAc...) Potential

Disulfide bond

55 ↔ 121

Ref.13 Ref.14

Disulfide bond

169 ↔ 227

Potential

Disulfide bond

272 ↔ 330

Potential

Natural variations

Alternative sequence

1 – 101

101

Missing in isoform 3.

VSP_007029

Alternative sequence

421

1

Q → QVQSL in isoform 2.

VSP_007030

Natural variant

6 – 7

2

PA → RS

VAR_015462

Natural variant

20

1

A → P

VAR_015463

Natural variant

40

1

D → E

VAR_015464

Natural variant

44

1

S → L Ref.4 Ref.6 Ref.7

VAR_015465

Natural variant

50

1

S → T Ref.4 Ref.6 Ref.7

VAR_015466

Natural variant

52

1

I → A Requires 2 nucleotide substitutions. Ref.4 Ref.6 Ref.7

VAR_015467

Natural variant

52

1

I → T Ref.4 Ref.6 Ref.7

VAR_015468

Natural variant

54

1

H → E Requires 2 nucleotide substitutions. Ref.4 Ref.6 Ref.7

VAR_015469

Natural variant

54

1

H → R Ref.4 Ref.6 Ref.7

VAR_015470

Natural variant

57

1

V → A Ref.4 Ref.6 Ref.7

VAR_015471

Natural variant

61

1

I → N

VAR_015472

Natural variant

68

1

W → R

VAR_015473

Natural variant

75

1

A → G: dbSNP rs1057114. Ref.4 Ref.6 Ref.7

VAR_015474

Natural variant

77

1

E → K

VAR_015475

Natural variant

81

1

N → H

VAR_015477

Natural variant

95

1

E → D Ref.4 Ref.6 Ref.7 Ref.3

VAR_015478

Natural variant

96

1

S → L Ref.4 Ref.6 Ref.7 Ref.3

VAR_015479

Natural variant

100

1

E → N Requires 2 nucleotide substitutions. Ref.4 Ref.6 Ref.7 Ref.3

VAR_015480

Natural variant

100

1

E → T Requires 2 nucleotide substitutions. Ref.4 Ref.6 Ref.7 Ref.3

VAR_015481

Natural variant

107

1

S → C Ref.4 Ref.6 Ref.7 Ref.3

VAR_015482

Natural variant

107

1

S → R Ref.4 Ref.6 Ref.7 Ref.3

VAR_015483

Natural variant

109

1

S → G Ref.4 Ref.6 Ref.7 Ref.3

VAR_015484

Natural variant

125

1

R → Q

VAR_015485

Natural variant

131

1

T → V Requires 2 nucleotide substitutions. Ref.4 Ref.6 Ref.7 Ref.3

VAR_015486

Natural variant

133

1

F → L

VAR_015487

Natural variant

162

1

Q → D Requires 2 nucleotide substitutions.

VAR_015488

Natural variant

180

1

T → S

VAR_015489

Natural variant

189

1

E → Q

VAR_015490

Natural variant

200 – 201

2

VG → AR

VAR_015491

Natural variant

213

1

K → N

VAR_015492

Natural variant

219

1

E → G

VAR_015493

Natural variant

221

1

V → I

VAR_015494

Natural variant

235

1

Q → R

VAR_015495

Natural variant

238 – 239

2

PL → SF

VAR_015496

Natural variant

250

1

R → Q

VAR_015497

Natural variant

260

1

Q → L

VAR_015498

Natural variant

262

1

V → M

VAR_015499

Natural variant

270

1

V → I

VAR_015500

Natural variant

275

1

R → T

VAR_015501

Natural variant

301

1

V → L: dbSNP rs2422666.

VAR_015502

Natural variant

338

1

P → S

VAR_015503

Natural variant

352

1

P → L

VAR_015504

Natural variant

356

1

G → S

VAR_015505

Natural variant

366

1

S → P

VAR_015506

Natural variant

369

1

R → Q

VAR_015507

Natural variant

388

1

A → E

VAR_015508

Natural variant

442

1

Q → R

VAR_015509

Natural variant

459

1

P → L

VAR_015510

Natural variant

485

1

A → L Requires 2 nucleotide substitutions.

VAR_015511

Natural variant

490

1

P → L

VAR_015512

Experimental info

Sequence conflict

130

1

D → DD in CAA71944. Ref.3

Sequence conflict

130

1

D → DD in BAA87929. Ref.4

Sequence conflict

130

1

D → DD in CAC12723. Ref.6

Sequence conflict

130

1

D → DD in CAB38874. Ref.6

Sequence conflict

130

1

D → DD in AAH33092. Ref.7

Sequence conflict

258

1

T → I in CAA71944. Ref.3

Sequence conflict

418

1

E → K in AAF19260. Ref.6

Sequence conflict

484

1

P → L in AAF19260. Ref.6

Sequence conflict

498

1

V → I in AAF19260. Ref.6

Sequence conflict

502

1

R → K in CAA71944. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

503

Helix Strand Turn

Details...

Beta strand

41 – 46

6

Beta strand

51 – 53

3

Beta strand

56 – 58

3

Beta strand

66 – 70

5

Beta strand

77 – 85

9

Beta strand

90 – 94

5

Beta strand

106 – 110

5

Helix

113 – 115

3

Beta strand

117 – 125

9

Beta strand

127 – 129

3

Beta strand

131 – 135

5

Beta strand

139 – 144

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: E9C5477363180512	FASTA	503	54,813
	10 20 30 40 50 60 MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVSVAAGES AILHCTVTSL 70 80 90 100 110 120 IPVGPIQWFR GAGPARELIY NQKEGHFPRV TTVSESTKRE NMDFSISISN ITPADAGTYY 130 140 150 160 170 180 CVKFRKGSPD TEFKSGAGTE LSVRAKPSAP VVSGPAARAT PQHTVSFTCE SHGFSPRDIT 190 200 210 220 230 240 LKWFKNGNEL SDFQTNVDPV GESVSYSIHS TAKVVLTRED VHSQVICEVA HVTLQGDPLR 250 260 270 280 290 300 GTANLSETIR VPPTLEVTQQ PVRAENQVNV TCQVRKFYPQ RLQLTWLENG NVSRTETAST 310 320 330 340 350 360 VTENKDGTYN WMSWLLVNVS AHRDDVKLTC QVEHDGQPAV SKSHDLKVSA HPKEQGSNTA 370 380 390 400 410 420 AENTGSNERN IYIVVGVVCT LLVALLMAAL YLVRIRQKKA QGSTSSTRLH EPEKNAREIT 430 440 450 460 470 480 QDTNDITYAD LNLPKGKKPA PQAAEPNNHT EYASIQTSPQ PASEDTLTYA DLDMVHLNRT 490 500 PKQPAPKPEP SFSEYASVQV PRK
	Isoform 2. Checksum: CDFDA403B6781E96	FASTA	507	55,240
	10 20 30 40 50 60 MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVSVAAGES AILHCTVTSL 70 80 90 100 110 120 IPVGPIQWFR GAGPARELIY NQKEGHFPRV TTVSESTKRE NMDFSISISN ITPADAGTYY 130 140 150 160 170 180 CVKFRKGSPD TEFKSGAGTE LSVRAKPSAP VVSGPAARAT PQHTVSFTCE SHGFSPRDIT 190 200 210 220 230 240 LKWFKNGNEL SDFQTNVDPV GESVSYSIHS TAKVVLTRED VHSQVICEVA HVTLQGDPLR 250 260 270 280 290 300 GTANLSETIR VPPTLEVTQQ PVRAENQVNV TCQVRKFYPQ RLQLTWLENG NVSRTETAST 310 320 330 340 350 360 VTENKDGTYN WMSWLLVNVS AHRDDVKLTC QVEHDGQPAV SKSHDLKVSA HPKEQGSNTA 370 380 390 400 410 420 AENTGSNERN IYIVVGVVCT LLVALLMAAL YLVRIRQKKA QGSTSSTRLH EPEKNAREIT 430 440 450 460 470 480 QVQSLDTNDI TYADLNLPKG KKPAPQAAEP NNHTEYASIQ TSPQPASEDT LTYADLDMVH 490 500 LNRTPKQPAP KPEPSFSEYA SVQVPRK
	Isoform 3. Checksum: E4479F67E64D76F9	FASTA	402	44,165
	10 20 30 40 50 60 MDFSISISNI TPADAGTYYC VKFRKGSPDT EFKSGAGTEL SVRAKPSAPV VSGPAARATP 70 80 90 100 110 120 QHTVSFTCES HGFSPRDITL KWFKNGNELS DFQTNVDPVG ESVSYSIHST AKVVLTREDV 130 140 150 160 170 180 HSQVICEVAH VTLQGDPLRG TANLSETIRV PPTLEVTQQP VRAENQVNVT CQVRKFYPQR 190 200 210 220 230 240 LQLTWLENGN VSRTETASTV TENKDGTYNW MSWLLVNVSA HRDDVKLTCQ VEHDGQPAVS 250 260 270 280 290 300 KSHDLKVSAH PKEQGSNTAA ENTGSNERNI YIVVGVVCTL LVALLMAALY LVRIRQKKAQ 310 320 330 340 350 360 GSTSSTRLHE PEKNAREITQ DTNDITYADL NLPKGKKPAP QAAEPNNHTE YASIQTSPQP 370 380 390 400 ASEDTLTYAD LDMVHLNRTP KQPAPKPEPS FSEYASVQVP RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes." Yamao T., Matozaki T., Amano K., Matsuda Y., Takahashi N., Ochi F., Fujioka Y., Kasuga M. Biochem. Biophys. Res. Commun. 231:61-67(1997) [PubMed: 9070220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"A family of proteins that inhibit signalling through tyrosine kinase receptors." Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A. Nature 386:181-186(1997) [PubMed: 9062191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PTPN11; PTPN6 AND GRB2. Tissue: Placenta.
[3]	"Cloning of two members of the SIRP alpha family of protein tyrosine phosphatase binding proteins in cattle that are expressed on monocytes and a subpopulation of dendritic cells and which mediate binding to CD4 T cells." Brooke G.P., Parsons K.R., Howard C.J. Eur. J. Immunol. 28:1-11(1998) [PubMed: 9485180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS ASP-95; LEU-96; ASN-100; ARG-107; GLY-109 AND VAL-131. Tissue: Monocyte.
[4]	"Gene structure of mouse BIT/SHPS-1." Sano S., Ohnishi H., Kubota M. Biochem. J. 344:667-675(1999) [PubMed: 10585853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LEU-44; THR-50; THR-52; ARG-54; ALA-57; GLY-75; ASP-95; LEU-96; ASN-100; ARG-107; GLY-109 AND VAL-131. Tissue: Brain.
[5]	"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] (ISOFORM 1).
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-44; THR-50; THR-52; ARG-54; ALA-57; GLY-75; ASP-95; LEU-96; ASN-100; ARG-107; GLY-109 AND VAL-131.
[7]	"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] (ISOFORMS 1 AND 2), VARIANTS LEU-44; THR-50; THR-52; ARG-54; ALA-57; GLY-75; ASP-95; LEU-96; ASN-100; ARG-107; GLY-109 AND VAL-131. Tissue: Brain, Kidney and Skin.
[8]	"SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages." Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G. Curr. Biol. 9:927-930(1999) [PubMed: 10469599] [Abstract] Cited for: FUNCTION, INTERACTION WITH FYB; SCAP2 AND PTK2B.
[9]	"Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha." Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C. J. Biol. Chem. 275:28222-28229(2000) [PubMed: 10842184] [Abstract] Cited for: PHOSPHORYLATION BY JAK2, INTERACTION WITH PTPN11 AND JAK2.
[10]	"Bidirectional negative regulation of human T and dendritic cells by CD47 and its cognate receptor signal-regulator protein-alpha: down-regulation of IL-12 responsiveness and inhibition of dendritic cell activation." Latour S., Tanaka H., Demeure C., Mateo V., Rubio M., Brown E.J., Maliszewski C., Lindberg F.P., Oldenborg A., Ullrich A., Delespesse G., Sarfati M. J. Immunol. 167:2547-2554(2001) [PubMed: 11509594] [Abstract] Cited for: FUNCTION, INTERACTION WITH CD47.
[11]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-244, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-269 AND ASN-291, MASS SPECTROMETRY. Tissue: Liver.
[13]	"The structure of the macrophage signal regulatory protein alpha (SIRPalpha) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors." Hatherley D., Harlos K., Dunlop D.C., Stuart D.I., Barclay A.N. J. Biol. Chem. 282:14567-14575(2007) [PubMed: 17369261] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-148, DISULFIDE BOND.
[14]	"Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47." Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N. Mol. Cell 31:266-277(2008) [PubMed: 18657508] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-148 IN COMPLEX WITH CD47, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D86043 mRNA. Translation: BAA12974.1.
Y10375 mRNA. Translation: CAA71403.1.
Y11047 mRNA. Translation: CAA71944.1. Different initiation.
AB023430 mRNA. Translation: BAA87929.1.
AK290776 mRNA. Translation: BAF83465.1.
AC004832 Genomic DNA. Translation: AAF19260.1.
AL034562 Genomic DNA. Translation: CAB38874.2.
AL117335 Genomic DNA. Translation: CAC12723.2.
BC026692 mRNA. Translation: AAH26692.1.
BC033092 mRNA. Translation: AAH33092.1.
BC038510 mRNA. Translation: AAH38510.1.
BC075849 mRNA. Translation: AAH75849.1.

IPI

IPI00332887.
IPI00656087.
IPI00848309.

PIR

JC5287.

RefSeq

NP_001035111.1.
NP_001035112.1.
NP_542970.1.

UniGene

Hs.581021
Hs.679042

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JJS	X-ray	1.85	A/B	31-148	[»]
2JJT	X-ray	2.30	A/B	31-148	[»]
2UV3	X-ray	1.80	A/B	31-148	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P78324. 3 interactions.

PTM databases

PhosphoSite

P78324.

Proteomic databases

PRIDE

P78324.

Genome annotation databases

Ensembl

ENSG00000198053. Homo sapiens. [Contig view]

GeneID

140885.

KEGG

hsa:140885.

Organism-specific databases

GeneCards

GC20P001822.

H-InvDB

HIX0041373.

HGNC

HGNC:9662. SIRPA.

HPA

CAB002776.
CAB015122.

MIM

602461. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P78324.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P78324.

Bgee

P78324.

GermOnline

ENSG00000198053. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

Pfam

PF07654. C1-set. 2 hits.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00407. IGc1. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

84534.

SOURCE

Search...

Entry information

Entry name

SHPS1_HUMAN

Accession

Primary (citable) accession number: P78324
Secondary accession number(s): A8K411 , O00683, O43799, Q8N517, Q8TAL8, Q9H0Z2, Q9UDX2, Q9UIJ6, Q9Y4U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)