P78324 (SHPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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):
Brain Ig-like molecule with tyrosine-based activation motifs
Short name=Bit
CD172 antigen-like family member A
Inhibitory receptor SHPS-1
Macrophage fusion receptor
MyD-1 antigen
Signal-regulatory protein alpha-1
Short name=Sirp-alpha-1
Signal-regulatory protein alpha-2
Short name=Sirp-alpha-2
Signal-regulatory protein alpha-3
Short name=Sirp-alpha-3
p84
CD_antigen=CD172a

Gene names

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

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	504 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. Ref.8 Ref.10
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 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 Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome cell adhesion Traceable author statement Ref.1. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
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:
     422-422: Q → QVQSL

Note: No experimental confirmation available.

Isoform 4 (identifier: P78324-4)

The sequence of this isoform differs from the canonical sequence as follows:
     130-130: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 504

474

Tyrosine-protein phosphatase non-receptor type substrate 1

PRO_0000014941

Regions

Topological domain

31 – 373

343

Extracellular Potential

Transmembrane

374 – 394

21

Helical; Potential

Topological domain

395 – 504

110

Cytoplasmic Potential

Domain

32 – 137

106

Ig-like V-type

Domain

148 – 247

100

Ig-like C1-type 1

Domain

254 – 348

95

Ig-like C1-type 2

Motif

429 – 432

4

SH2-binding Potential

Motif

439 – 444

6

SH3-binding Potential

Motif

453 – 456

4

SH2-binding Potential

Motif

470 – 473

4

SH2-binding Potential

Motif

496 – 499

4

SH2-binding Potential

Amino acid modifications

Modified residue

429

1

Phosphotyrosine; by Tyr-kinases Potential

Modified residue

453

1

Phosphotyrosine; by Tyr-kinases Potential

Modified residue

470

1

Phosphotyrosine; by Tyr-kinases By similarity

Modified residue

496

1

Phosphotyrosine; by Tyr-kinases By similarity

Glycosylation

245

1

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

Glycosylation

270

1

N-linked (GlcNAc...) Ref.12

Glycosylation

292

1

N-linked (GlcNAc...) Ref.12

Glycosylation

319

1

N-linked (GlcNAc...) Potential

Disulfide bond

55 ↔ 121

Ref.13 Ref.14

Disulfide bond

170 ↔ 228

Potential

Disulfide bond

273 ↔ 331

Potential

Natural variations

Alternative sequence

130

1

Missing in isoform 4.

VSP_040799

Alternative sequence

422

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

L → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs1135193 [ dbSNP | Ensembl ].

VAR_015465

Natural variant

50

1

T → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855609 [ dbSNP | Ensembl ].

VAR_015466

Natural variant

52

1

T → I. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855610 [ dbSNP | Ensembl ].

VAR_015468

Natural variant

54

1

R → H. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855611 [ dbSNP | Ensembl ].

VAR_015470

Natural variant

57

1

A → V. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855612 [ dbSNP | Ensembl ].

VAR_015471

Natural variant

61

1

I → N.

VAR_015472

Natural variant

68

1

W → R.

VAR_015473

Natural variant

75

1

G → A. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs1057114 [ dbSNP | Ensembl ].

VAR_015474

Natural variant

77

1

E → K.

VAR_015475

Natural variant

81

1

N → H.

VAR_015477

Natural variant

95

1

D → E. Ref.1 Ref.2 Ref.4 Ref.6

VAR_015478

Natural variant

96

1

L → S. Ref.1 Ref.2 Ref.4 Ref.6

VAR_015479

Natural variant

100

1

N → E Requires 2 nucleotide substitutions. Ref.1 Ref.2 Ref.4 Ref.6

VAR_015480

Natural variant

107

1

R → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855615 [ dbSNP | Ensembl ].

VAR_015483

Natural variant

109

1

G → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855616 [ dbSNP | Ensembl ].

VAR_015484

Natural variant

125

1

R → Q.

VAR_015485

Natural variant

132

1

V → T Requires 2 nucleotide substitutions. Ref.1 Ref.2 Ref.4 Ref.6

VAR_015486

Natural variant

134

1

F → L.

VAR_015487

Natural variant

163

1

Q → D Requires 2 nucleotide substitutions.

VAR_015488

Natural variant

181

1

T → S.

VAR_015489

Natural variant

190

1

E → Q.

VAR_015490

Natural variant

201 – 202

2

VG → AR.

VAR_015491

Natural variant

214

1

K → N.

VAR_015492

Natural variant

220

1

E → G.

VAR_015493

Natural variant

222

1

V → I.

VAR_015494

Natural variant

236

1

Q → R.

VAR_015495

Natural variant

239 – 240

2

PL → SF.

VAR_015496

Natural variant

251

1

R → Q.

VAR_015497

Natural variant

261

1

Q → L.

VAR_015498

Natural variant

263

1

V → M.

VAR_015499

Natural variant

271

1

V → I.

VAR_015500

Natural variant

276

1

R → T.

VAR_015501

Natural variant

302

1

V → L.
Corresponds to variant rs2422666 [ dbSNP | Ensembl ].

VAR_015502

Natural variant

339

1

P → S.

VAR_015503

Natural variant

353

1

P → L.

VAR_015504

Natural variant

357

1

G → S.

VAR_015505

Natural variant

367

1

S → P.

VAR_015506

Natural variant

370

1

R → Q.

VAR_015507

Natural variant

389

1

A → E.

VAR_015508

Natural variant

443

1

Q → R.

VAR_015509

Natural variant

460

1

P → L.

VAR_015510

Natural variant

486

1

A → L Requires 2 nucleotide substitutions.

VAR_015511

Natural variant

491

1

P → L.

VAR_015512

Experimental info

Sequence conflict

259

1

T → I in CAA71944. Ref.7

Sequence conflict

503

1

R → K in CAA71944. Ref.7

Secondary structure

1

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504

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

132 – 136

5

Beta strand

140 – 145

6

Beta strand

152 – 154

3

Beta strand

165 – 178

14

Beta strand

181 – 186

6

Beta strand

194 – 199

6

Beta strand

207 – 216

10

Helix

221 – 223

3

Beta strand

225 – 231

7

Beta strand

240 – 245

6

Helix

246 – 248

3

Beta strand

255 – 261

7

Beta strand

269 – 281

13

Beta strand

283 – 289

7

Beta strand

292 – 298

7

Beta strand

310 – 318

9

Beta strand

328 – 335

8

Beta strand

341 – 346

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 5, 2011. Version 2. Checksum: 18D2FD04F6182AD0	FASTA	504	54,967
	10 20 30 40 50 60 MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET ATLRCTATSL 70 80 90 100 110 120 IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN NMDFSIRIGN ITPADAGTYY 130 140 150 160 170 180 CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA PVVSGPAARA TPQHTVSFTC ESHGFSPRDI 190 200 210 220 230 240 TLKWFKNGNE LSDFQTNVDP VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL 250 260 270 280 290 300 RGTANLSETI RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS 310 320 330 340 350 360 TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS AHPKEQGSNT 370 380 390 400 410 420 AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK AQGSTSSTRL HEPEKNAREI 430 440 450 460 470 480 TQDTNDITYA DLNLPKGKKP APQAAEPNNH TEYASIQTSP QPASEDTLTY ADLDMVHLNR 490 500 TPKQPAPKPE PSFSEYASVQ VPRK
	Isoform 2 [UniParc]. Checksum: 098D9B24276FA4E1	FASTA	508	55,394
	10 20 30 40 50 60 MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET ATLRCTATSL 70 80 90 100 110 120 IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN NMDFSIRIGN ITPADAGTYY 130 140 150 160 170 180 CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA PVVSGPAARA TPQHTVSFTC ESHGFSPRDI 190 200 210 220 230 240 TLKWFKNGNE LSDFQTNVDP VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL 250 260 270 280 290 300 RGTANLSETI RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS 310 320 330 340 350 360 TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS AHPKEQGSNT 370 380 390 400 410 420 AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK AQGSTSSTRL HEPEKNAREI 430 440 450 460 470 480 TQVQSLDTND ITYADLNLPK GKKPAPQAAE PNNHTEYASI QTSPQPASED TLTYADLDMV 490 500 HLNRTPKQPA PKPEPSFSEY ASVQVPRK
	Isoform 4 [UniParc]. Checksum: AB4F162B7FF8D97A	FASTA	503	54,852
	10 20 30 40 50 60 MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET ATLRCTATSL 70 80 90 100 110 120 IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN NMDFSIRIGN ITPADAGTYY 130 140 150 160 170 180 CVKFRKGSPD VEFKSGAGTE 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

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96; GLU-100; SER-107; SER-109 AND THR-132. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PTPN11; PTPN6 AND GRB2, VARIANTS SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96; GLU-100; SER-107; SER-109 AND THR-132. Tissue: Placenta.
[3]	"Gene structure of mouse BIT/SHPS-1." Sano S., Ohnishi H., Kubota M. Biochem. J. 344:667-675(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96; GLU-100; SER-107; SER-109 AND THR-132. Tissue: Thalamus.
[5]	"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] [Europe PMC] [Abstract] 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96; GLU-100; SER-107; SER-109 AND THR-132. Tissue: Brain, Kidney and Skin.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-504. Tissue: Monocyte.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-245, 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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-292, 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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-149, 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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-149 IN COMPLEX WITH CD47, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86043 mRNA. Translation: BAA12974.1.
Y10375 mRNA. Translation: CAA71403.1.
AB023430 mRNA. Translation: BAA87929.1.
AK290776 mRNA. Translation: BAF83465.1.
AK312521 mRNA. Translation: BAG35420.1.
AL034562 Genomic DNA. Translation: CAB38874.2.
AL034562, AL117335 Genomic DNA. Translation: CAM28287.1.
AL117335 Genomic DNA. Translation: CAC12723.2.
AL117335, AL034562 Genomic DNA. Translation: CAM28335.1.
BC026692 mRNA. Translation: AAH26692.1.
BC033092 mRNA. Translation: AAH33092.1.
BC038510 mRNA. Translation: AAH38510.1.
BC075849 mRNA. Translation: AAH75849.1.
Y11047 mRNA. Translation: CAA71944.1.

IPI

IPI00656087.
IPI00848309.
IPI01008905.

PIR

JC5287.

RefSeq

NP_001035111.1. NM_001040022.1.
NP_001035112.1. NM_001040023.1.
NP_542970.1. NM_080792.2.

UniGene

Hs.740396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JJS	X-ray	1.85	A/B	31-149	[»]
2JJT	X-ray	2.30	A/B	31-149	[»]
2UV3	X-ray	1.80	A/B	31-149	[»]
2WNG	X-ray	2.49	A	31-349	[»]

ProteinModelPortal

P78324.

SMR

P78324. Positions 31-348.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78324. 4 interactions.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

P78324.

Polymorphism databases

DMDM

29427656.

Proteomic databases

PaxDb

P78324.

PRIDE

P78324.

Protocols and materials databases

DNASU

140885.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356025; ENSP00000348307; ENSG00000198053.
ENST00000358771; ENSP00000351621; ENSG00000198053.
ENST00000400068; ENSP00000382941; ENSG00000198053.

GeneID

140885.

KEGG

hsa:140885.

UCSC

uc002wfq.3. human.
uc002wft.3. human.

Organism-specific databases

CTD

140885.

GeneCards

GC20P001822.

HGNC

HGNC:9662. SIRPA.

HPA

CAB002776.
CAB015122.

MIM

602461. gene.

neXtProt

NX_P78324.

PharmGKB

PA34006.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39917.

HOVERGEN

HBG056632.

KO

K06551.

OMA

PKPEPSY.

OrthoDB

EOG4FR0SN.

PhylomeDB

P78324.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P78324.

Bgee

P78324.

Genevestigator

P78324.

GermOnline

ENSG00000198053. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

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

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

ChiTaRS

SIRPA. human.

EvolutionaryTrace

P78324.

GenomeRNAi

140885.

NextBio

84534.

SOURCE

Search...

Entry information

Entry name

SHPS1_HUMAN

Accession

Primary (citable) accession number: P78324
Secondary accession number(s): A2A2E1 , A8K411, B2R6C3, O00683, O43799, Q8N517, Q8TAL8, Q9H0Z2, Q9UDX2, Q9UIJ6, Q9Y4U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	April 5, 2011
Last modified:	April 3, 2013
This is version 140 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.