Q12815 (TROAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tastin

Alternative name(s):
Trophinin-assisting protein
Trophinin-associated protein

Gene names

Name:

TROAP

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	778 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could be involved with bystin and trophinin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation.
Subunit structure	Directly binds bystin, and indirectly trophinin.
Subcellular location	Cytoplasm.
Tissue specificity	Strong expression at implantation sites. Was exclusively localized to the apical side of the syncytiotrophoblast. Also found in macrophages.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BYSL	Q13895	9	EBI-2349743,EBI-358049

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12815-1)

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: Q12815-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-144: EAPGTIEFVADPAALATILSGEGVKSCHLGRQ → VLVPAPGKLFALRRSPFPPAKCHLARCHGLYL
     145-778: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 778	778	Tastin		PRO_0000065636
Regions
	Repeat	516 – 548	33	1
	Repeat	549 – 581	33	2
	Repeat	582 – 614	33	3
	Repeat	615 – 647	33	4
	Region	516 – 647	132	4 X 33 AA approximate tandem repeats
	Compositional bias	504 – 687	184	Cys-rich
Amino acid modifications
	Modified residue	16	1	Phosphoserine Ref.8
	Modified residue	98	1	Phosphoserine Ref.7
	Modified residue	324	1	Phosphoserine Ref.8
	Modified residue	334	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
	Modified residue	344	1	Phosphoserine Ref.6
	Modified residue	362	1	Phosphoserine Ref.8
	Modified residue	363	1	Phosphothreonine Ref.8
	Modified residue	376	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	113 – 144	32	EAPGT…HLGRQ → VLVPAPGKLFALRRSPFPPA KCHLARCHGLYL in isoform 2.		VSP_042820
	Alternative sequence	145 – 778	634	Missing in isoform 2.		VSP_042821
Experimental info
	Sequence conflict	224	1	R → H in AAA79333. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 530B0481EC8D7E02	FASTA	778	83,857
	10 20 30 40 50 60 MTTRQATKDP LLRGVSPTPS KIPVRSQKRT PFPTVTSCAV DQENQDPRRW VQKPPLNIQR 70 80 90 100 110 120 PLVDSAGPRP KARHQAETSQ RLVGISQPRN PLEELRPSPR GQNVGPGPPA QTEAPGTIEF 130 140 150 160 170 180 VADPAALATI LSGEGVKSCH LGRQPSLAKR VLVRGSQGGT TQRVQGVRAS AYLAPRTPTH 190 200 210 220 230 240 RLDPARASCF SRLEGPGPRG RTLCPQRLQA LISPSGPSFH PSTRPSFQEL RRETAGSSRT 250 260 270 280 290 300 SVSQASGLLL ETPVQPAFSL PKGEREVVTH SDEGGVASLG LAQRVPLREN REMSHTRDSH 310 320 330 340 350 360 DSHLMPSPAP VAQPLPGHVV PCPSPFGRAQ RVPSPGPPTL TSYSVLRRLT VQPKTRFTPM 370 380 390 400 410 420 PSTPRVQQAQ WLRGVSPQSC SEDPALPWEQ VAVRLFDQES CIRSLEGSGK PPVATPSGPH 430 440 450 460 470 480 SNRTPSLQEV KIQRIGILQQ LLRQEVEGLV GGQCVPLNGG SSLDMVELQP LLTEISRTLN 490 500 510 520 530 540 ATEHNSGTSH LPGLLKHSGL PKPCLPEECG EPQPCPPAEP GPPEAFCRSE PEIPEPSLQE 550 560 570 580 590 600 QLEVPEPYPP AEPRPLESCC RSEPEIPESS RQEQLEVPEP CPPAEPRPLE SYCRIEPEIP 610 620 630 640 650 660 ESSRQEQLEV PEPCPPAEPG PLQPSTQGQS GPPGPCPRVE LGASEPCTLE HRSLESSLPP 670 680 690 700 710 720 CCSQWAPATT SLIFSSQHPL CASPPICSLQ SLRPPAGQAG LSNLAPRTLA LRERLKSCLT 730 740 750 760 770 AIHCFHEARL DDECAFYTSR APPSGPTRVC TNPVATLLEW QDALCFIPVG SAAPQGSP
	Isoform 2 [UniParc]. Checksum: 59A5062A4CF71DD2	FASTA	144	15,893
	10 20 30 40 50 60 MTTRQATKDP LLRGVSPTPS KIPVRSQKRT PFPTVTSCAV DQENQDPRRW VQKPPLNIQR 70 80 90 100 110 120 PLVDSAGPRP KARHQAETSQ RLVGISQPRN PLEELRPSPR GQNVGPGPPA QTVLVPAPGK 130 140 LFALRRSPFP PAKCHLARCH GLYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Trophinin and tastin, a novel cell adhesion molecule complex with potential involvement in embryo implantation." Fukuda M.N., Sato T., Nakayama J., Klier G., Mikami M., Aoki D., Nozawa S. Genes Dev. 9:1199-1210(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Fukuda M., Sato T. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 714 AND 742.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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). Tissue: Lymph.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND SER-344, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-334 AND SER-376, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-324; SER-334; SER-362 AND THR-363, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U04810 mRNA. Translation: AAA79333.2. AC125611 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW58064.1. BC011597 mRNA. Translation: AAH11597.1. BC032583 mRNA. Translation: AAH32583.1.
IPI	IPI00029680. IPI00449144.
PIR	I38487.
RefSeq	NP_001094090.1. NM_001100620.1. NP_005471.3. NM_005480.3.
UniGene	Hs.524399.
3D structure databases
ProteinModelPortal	Q12815.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12815. 6 interactions.
STRING	9606.ENSP00000257909.
Polymorphism databases
DMDM	223634724.
Proteomic databases
PaxDb	Q12815.
PRIDE	Q12815.
Protocols and materials databases
DNASU	10024.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257909; ENSP00000257909; ENSG00000135451. ENST00000380327; ENSP00000369684; ENSG00000135451.
GeneID	10024.
KEGG	hsa:10024.
UCSC	uc001rtw.4. human. uc001rtx.4. human.
Organism-specific databases
CTD	10024.
GeneCards	GC12P049716.
H-InvDB	HIX0010602.
HGNC	HGNC:12327. TROAP.
HPA	HPA044102.
MIM	603872. gene.
neXtProt	NX_Q12815.
PharmGKB	PA37003.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG47246.
HOGENOM	HOG000082520.
HOVERGEN	HBG069140.
InParanoid	Q12815.
OrthoDB	EOG42NHZT.
PhylomeDB	Q12815.
Gene expression databases
ArrayExpress	Q12815.
Bgee	Q12815.
CleanEx	HS_TROAP.
Genevestigator	Q12815.
GermOnline	ENSG00000135451. Homo sapiens.
Family and domain databases
InterPro	IPR026133. Tastin. [Graphical view]
PANTHER	PTHR15289. PTHR15289. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10024.
NextBio	37877.
SOURCE	Search...

Entry information

Entry name

TROAP_HUMAN

Accession

Primary (citable) accession number: Q12815
Secondary accession number(s): Q6PJU7, Q8N5B2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 10, 2009
Last modified:	May 29, 2013
This is version 92 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.