Q99590 (SCAFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein SCAF11

Alternative name(s):
CTD-associated SR protein 11
Renal carcinoma antigen NY-REN-40
SC35-interacting protein 1
SR-related and CTD-associated factor 11
SRSF2-interacting protein
Serine/arginine-rich splicing factor 2-interacting protein
Splicing factor, arginine/serine-rich 2-interacting protein
Splicing regulatory protein 129
Short name=SRrp129

Gene names

Name:	SCAF11
Synonyms:	CASP11, SFRS2IP, SIP1, SRSF2IP

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1463 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. Ref.2
Subunit structure	Interacts with SRSF2/SFRS2, U2AF2 and SNRNP70. Ref.2
Subcellular location	Nucleus Ref.2.
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAC39565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC39565.1 differs from that shown. Reason: Frameshift at position 62. The sequence AAH40951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH40951.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	spliceosomal complex assembly Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay. Source: HPA
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q99590-1)

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: Q99590-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1463	1463	Protein SCAF11		PRO_0000076314
Regions
	Zinc finger	41 – 82	42	RING-type; degenerate
	Compositional bias	841 – 985	145	Arg-rich
	Compositional bias	1225 – 1285	61	Pro-rich
Amino acid modifications
	Modified residue	338	1	Phosphoserine Ref.10
	Modified residue	341	1	Phosphoserine Ref.10
	Modified residue	344	1	Phosphoserine Ref.10
	Modified residue	400	1	Phosphoserine Ref.15
	Modified residue	401	1	Phosphoserine Ref.15
	Modified residue	402	1	Phosphoserine Ref.15
	Modified residue	405	1	Phosphoserine Ref.7 Ref.10 Ref.12 Ref.13 Ref.15
	Modified residue	410	1	Phosphothreonine Ref.10
	Modified residue	413	1	Phosphoserine Ref.12
	Modified residue	533	1	Phosphoserine Ref.10
	Modified residue	608	1	Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13
	Modified residue	614	1	Phosphoserine Ref.10 Ref.13
	Modified residue	680	1	Phosphoserine Ref.10 Ref.13
	Modified residue	687	1	Phosphoserine Ref.13
	Modified residue	723	1	Phosphoserine Ref.7
	Modified residue	726	1	Phosphoserine Ref.7
	Modified residue	769	1	Phosphothreonine Ref.15
	Modified residue	771	1	Phosphoserine Ref.13
	Modified residue	776	1	Phosphoserine Ref.13 Ref.15
	Modified residue	796	1	Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
	Modified residue	798	1	Phosphoserine Ref.12
	Modified residue	802	1	Phosphoserine Ref.10 Ref.12 Ref.15
	Modified residue	807	1	Phosphothreonine Ref.10
	Modified residue	963	1	Phosphoserine Ref.10
	Modified residue	1127	1	Phosphoserine Ref.10 Ref.13
	Modified residue	1169	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	1 – 315	315	Missing in isoform 2.		VSP_037665
	Natural variant	657	1	F → Y. Corresponds to variant rs7315731 [ dbSNP | Ensembl ].		VAR_059722
	Natural variant	1261	1	V → L. Corresponds to variant rs11574973 [ dbSNP | Ensembl ].		VAR_059723
Experimental info
	Sequence conflict	584	1	I → M in AAH40951. Ref.5
	Sequence conflict	623	1	D → G in AAH40951. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 7170B88544BAF7D4	FASTA	1,463	164,652
	10 20 30 40 50 60 MKKKTVCTLN MGDKKYEDME GEENGDNTIS TGLLYSEADR CPICLNCLLE KEVGFPESCN 70 80 90 100 110 120 HVFCMTCILK WAETLASCPI DRKPFQAVFK FSALEGYVKV QVKKQLRETK DKKNENSFEK 130 140 150 160 170 180 QVSCHENSKS CIRRKAIVRE DLLSAKVCDL KWIHRNSLYS ETGGKKNAAI KINKPQRSNW 190 200 210 220 230 240 STNQCFRNFF SNMFSSVSHS GESSFTYRAY CTEFIEASEI SALIRQKRHE LELSWFPDTL 250 260 270 280 290 300 PGIGRIGFIP WNVETEVLPL ISSVLPRTIF PTSTISFEHF GTSCKGYALA HTQEGEEKKQ 310 320 330 340 350 360 TSGTSNTRGS RRKPAMTTPT RRSTRNTRAE TASQSQRSPI SDNSGCDAPG NSNPSLSVPS 370 380 390 400 410 420 SAESEKQTRQ APKRKSVRRG RKPPLLKKKL RSSVAAPEKS SSNDSVDEET AESDTSPVLE 430 440 450 460 470 480 KEHQPDVDSS NICTVQTHVE NQSANCLKSC NEQIEESEKH TANYDTEERV GSSSSESCAQ 490 500 510 520 530 540 DLPVLVGEEG EVKKLENTGI EANVLCLESE ISENILEKGG DPLEKQDQIS GLSQSEVKTD 550 560 570 580 590 600 VCTVHLPNDF PTCLTSESKV YQPVSCPLSD LSENVESVVN EEKITESSLV EITEHKDFTL 610 620 630 640 650 660 KTEELIESPK LESSEGEIIQ TVDRQSVKSP EVQLLGHVET EDVEIIATCD TFGNEDFNNI 670 680 690 700 710 720 QDSENNLLKN NLLNTKLEKS LEEKNESLTE HPRSTELPKT HIEQIQKHFS EDNNEMIPME 730 740 750 760 770 780 CDSFCSDQNE SEVEPSVNAD LKQMNENSVT HCSENNMPSS DLADEKVETV SQPSESPKDT 790 800 810 820 830 840 IDKTKKPRTR RSRFHSPSTT WSPNKDTPQE KKRPQSPSPR RETGKESRKS QSPSPKNESA 850 860 870 880 890 900 RGRKKSRSQS PKKDIARERR QSQSRSPKRD TTRESRRSES LSPRRETSRE NKRSQPRVKD 910 920 930 940 950 960 SSPGEKSRSQ SRERESDRDG QRRERERRTR KWSRSRSHSR SPSRCRTKSK SSSFGRIDRD 970 980 990 1000 1010 1020 SYSPRWKGRW ANDGWRCPRG NDRYRKNDPE KQNENTRKEK NDIHLDADDP NSADKHRNDC 1030 1040 1050 1060 1070 1080 PNWITEKINS GPDPRTRNPE KLKESHWEEN RNENSGNSWN KNFGSGWVSN RGRGRGNRGR 1090 1100 1110 1120 1130 1140 GTYRSSFAYK DQNENRWQNR KPLSGNSNSS GSESFKFVEQ QSYKRKSEQE FSFDTPADRS 1150 1160 1170 1180 1190 1200 GWTSASSWAV RKTLPADVQN YYSRRGRNSS GPQSGWMKQE EETSGQDSSL KDQTNQQVDG 1210 1220 1230 1240 1250 1260 SQLPINMMQP QMNVMQQQMN AQHQPMNIFP YPVGVHAPLM NIQRNPFNIH PQLPLHLHTG 1270 1280 1290 1300 1310 1320 VPLMQVATPT SVSQGLPPPP PPPPPSQQVN YIASQPDGKQ LQGIPSSSHV SNNMSTPVLP 1330 1340 1350 1360 1370 1380 APTAAPGNTG MVQGPSSGNT SSSSHSKASN AAVKLAESKV SVAVEASADS SKTDKKLQIQ 1390 1400 1410 1420 1430 1440 EKAAQEVKLA IKPFYQNKDI TKEEYKEIVR KAVDKVCHSK SGEVNSTKVA NLVKAYVDKY 1450 1460 KYSRKGSQKK TLEEPVSTEK NIG
	Isoform 2 [UniParc]. Checksum: B57FD40EE5E4C48C	FASTA	1,148	128,875
	10 20 30 40 50 60 MTTPTRRSTR NTRAETASQS QRSPISDNSG CDAPGNSNPS LSVPSSAESE KQTRQAPKRK 70 80 90 100 110 120 SVRRGRKPPL LKKKLRSSVA APEKSSSNDS VDEETAESDT SPVLEKEHQP DVDSSNICTV 130 140 150 160 170 180 QTHVENQSAN CLKSCNEQIE ESEKHTANYD TEERVGSSSS ESCAQDLPVL VGEEGEVKKL 190 200 210 220 230 240 ENTGIEANVL CLESEISENI LEKGGDPLEK QDQISGLSQS EVKTDVCTVH LPNDFPTCLT 250 260 270 280 290 300 SESKVYQPVS CPLSDLSENV ESVVNEEKIT ESSLVEITEH KDFTLKTEEL IESPKLESSE 310 320 330 340 350 360 GEIIQTVDRQ SVKSPEVQLL GHVETEDVEI IATCDTFGNE DFNNIQDSEN NLLKNNLLNT 370 380 390 400 410 420 KLEKSLEEKN ESLTEHPRST ELPKTHIEQI QKHFSEDNNE MIPMECDSFC SDQNESEVEP 430 440 450 460 470 480 SVNADLKQMN ENSVTHCSEN NMPSSDLADE KVETVSQPSE SPKDTIDKTK KPRTRRSRFH 490 500 510 520 530 540 SPSTTWSPNK DTPQEKKRPQ SPSPRRETGK ESRKSQSPSP KNESARGRKK SRSQSPKKDI 550 560 570 580 590 600 ARERRQSQSR SPKRDTTRES RRSESLSPRR ETSRENKRSQ PRVKDSSPGE KSRSQSRERE 610 620 630 640 650 660 SDRDGQRRER ERRTRKWSRS RSHSRSPSRC RTKSKSSSFG RIDRDSYSPR WKGRWANDGW 670 680 690 700 710 720 RCPRGNDRYR KNDPEKQNEN TRKEKNDIHL DADDPNSADK HRNDCPNWIT EKINSGPDPR 730 740 750 760 770 780 TRNPEKLKES HWEENRNENS GNSWNKNFGS GWVSNRGRGR GNRGRGTYRS SFAYKDQNEN 790 800 810 820 830 840 RWQNRKPLSG NSNSSGSESF KFVEQQSYKR KSEQEFSFDT PADRSGWTSA SSWAVRKTLP 850 860 870 880 890 900 ADVQNYYSRR GRNSSGPQSG WMKQEEETSG QDSSLKDQTN QQVDGSQLPI NMMQPQMNVM 910 920 930 940 950 960 QQQMNAQHQP MNIFPYPVGV HAPLMNIQRN PFNIHPQLPL HLHTGVPLMQ VATPTSVSQG 970 980 990 1000 1010 1020 LPPPPPPPPP SQQVNYIASQ PDGKQLQGIP SSSHVSNNMS TPVLPAPTAA PGNTGMVQGP 1030 1040 1050 1060 1070 1080 SSGNTSSSSH SKASNAAVKL AESKVSVAVE ASADSSKTDK KLQIQEKAAQ EVKLAIKPFY 1090 1100 1110 1120 1130 1140 QNKDITKEEY KEIVRKAVDK VCHSKSGEVN STKVANLVKA YVDKYKYSRK GSQKKTLEEP VSTEKNIG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel SR-related protein specifically interacts with the carboxy-terminal domain (CTD) of RNA polymerase II through a conserved interaction domain." Tanner S., Stagljar I., Georgiev O., Schaffner W., Bourquin J.-P. Biol. Chem. 378:565-571(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Lymphocyte.
[2]	"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing." Zhang W.-J., Wu J.Y. Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SRSF2; U2AF2 AND SNRNP70, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[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] OF 212-669 (ISOFORM 1). Tissue: Prostate.
[6]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11251 mRNA. Translation: CAA72121.1. AF030234 mRNA. Translation: AAC39565.1. Sequence problems. AC000015 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW57892.1. CH471111 Genomic DNA. Translation: EAW57894.1. BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
IPI	IPI00181359. IPI00746412.
PIR	T09073.
RefSeq	NP_004710.2. NM_004719.2.
UniGene	Hs.210367.
3D structure databases
ProteinModelPortal	Q99590.
SMR	Q99590. Positions 33-74.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99590. 2 interactions.
MINT	MINT-2866162.
STRING	9606.ENSP00000358374.
PTM databases
PhosphoSite	Q99590.
Polymorphism databases
DMDM	251757337.
Proteomic databases
PaxDb	Q99590.
PRIDE	Q99590.
Protocols and materials databases
DNASU	9169.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369367; ENSP00000358374; ENSG00000139218. ENST00000419565; ENSP00000413036; ENSG00000139218. ENST00000465950; ENSP00000449812; ENSG00000139218.
GeneID	9169.
KEGG	hsa:9169.
UCSC	uc001row.3. human.
Organism-specific databases
CTD	9169.
GeneCards	GC12M046313.
H-InvDB	HIX0010567.
HGNC	HGNC:10784. SCAF11.
HPA	HPA038862.
MIM	603668. gene.
neXtProt	NX_Q99590.
PharmGKB	PA35700.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300312.
HOVERGEN	HBG101126.
InParanoid	Q99590.
OMA	LELSWFP.
OrthoDB	EOG7F24SX.
Gene expression databases
ArrayExpress	Q99590.
Bgee	Q99590.
CleanEx	HS_SFRS2IP. HS_SIP1.
Genevestigator	Q99590.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SCAF11. human.
GeneWiki	SFRS2IP.
GenomeRNAi	9169.
NextBio	34387.
PMAP-CutDB	Q99590.
PRO	Q99590.
SOURCE	Search...

Entry information

Entry name

SCAFB_HUMAN

Accession

Primary (citable) accession number: Q99590
Secondary accession number(s): A6NEU9, A6NLW5, Q8IW59

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	July 7, 2009
Last modified:	November 13, 2013
This is version 97 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.